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Synthyra 8

A0A7V8SWA7

DASRPMRGEPLLPAGRLREPLSAMSRANVVVFTRTEVVPGAPEAIEKLSHFPVFAATTRLLGFRRHGGGMQLESATGISAGPFFAFCGIGNPEAFFGDLETWGLAICGRAVFADHHRYTEQDVLRIKKAGTDGGAKAFITTEKDAMNLSGLKFEGVPLFTAVIDMAVSPEADFLNVLDRLLARKMGAAA

Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 6/6. Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA). EC: 2.7.1.130 Sequence Length: 189 Sequence Mass (Da): 20236

D7G294

MERDRPLKGKGGGKRGKGRGGGGGRGRGGRPKSSQGRGHGHRHHAQGDSWRRNGGAAREMIDRERDESGELAQSITVSLRMWDFEQCDVKKCTGRKLCRLGLVREMELGAPFSGLVLSPNGELTVSPADREVVETLGMSVIDCSWARLDEIPFHQMRRGHHRLLPFLVAANPVNYGKPMKLTCAEAIAATLYIVGHQDEAVKVMDQFGWGAEFLRVNEDVLETYAACADGAEVVKAQAAFLARCEEEANSRRDAVSMEDMMPPSYSDEEEYGNHGSENGSENGSENGSSEGVTERGKFCDALLMPAAVLVASVLLFFLIPCGYIVTSDVKTGQQ

Function: Aminocarboxypropyltransferase that catalyzes the aminocarboxypropyl transfer on pseudouridine in 18S rRNA. It constitutes the last step in biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi). EC: 2.5.1.- Catalytic Activity: an N(1)-methylpseudouridine in 16S/18S rRNA + S-adenosyl-L-methionine = H(+) + N(1)-methyl-N(3)[(3S)-3-amino-3-carboxypropyl]pseudouridine in 16S/18S rRNA + S-methyl-5'-thioadenosine Sequence Length: 334 Sequence Mass (Da): 36359

A0A2C6KU51

MAPSRLGRLPPVIPSLLPPLGLRSRGEVKRRWESGRVFLRRIFHAARRQVASSEASTSDLPVHPSLQTCFSEEFPQSRSSYHPHRHHTIPRCLFLSAPLPSIVSSCSFVIDTRCNYVGTSAFSSLSSCANSSLQYIQCASLHQDAYHNDRKDQPSSAMFSARLSFHSEVSSSCPIYRFQSVQSHASSASSSSPSSPCSASSFSFHEPRQSYHRIGAAQVGAPFSSLLLSLCSPRTPKLSSSTPSCLLYSYISDLGFSSASSIPQLGQLTPTHPSSKGEKEESHATVSPNQRHKNAEGQGHGEGGGEGGENKRETRRKLRFHELLRLGYISDGTYRAVRSLLGYNELTEEQTFLLPQILPPTSLPPQNSSSSTSQDLPHHLLPSPRITQPSRDCLVQARTGTGKTLCFLLCVIERLLLHPPSGVGGLVIAPTRELANQILREAEQLTTFVPVEAAALVGGNSRKADELLLKRKRPQILICTPGRLLDHLESTFTFSVLLENLQVLVLDEADRLMELGHLEELKQIISYLPRNNARGTSRQSLLFSATVTDKVKELSWRLFSKPDYRFINCIGTNEQPTHERVEQNVVVVPATQTATALYNLLREEFDRHPYNYKIIVFFPTARLTAFFAALFREQLRIGVYEIHRRRESSARATTAMRFSTDRADAGVLFSSDVSARGVDYPDVSLVIQVCAPLTRELYIHRIGRTGRIGKEGRAILLLNNAETSFLEV

Function: RNA helicase. EC: 3.6.4.13 Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate Sequence Length: 728 Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis. Sequence Mass (Da): 80773

A0A3P7IH62

MLNIPFLSRFIQKTVKRQKVADSVDYLNYYVTSILLSFFALAISAKQYFGSPIQCWVPSEFRVCRCEEEAFTRCLTSEAEANSI

Function: Structural component of the gap junctions. Subcellular Location: Cell membrane Sequence Length: 84 Sequence Mass (Da): 9684 Location Topology: Multi-pass membrane protein

A0A6A4YVT0

SYLVHGAALWAAHIPIVPLAPVYTDLYTATASALCRTTNAVQEAPAICLLCGDVVCGGAECCKRNHRGACAQHVTTCGCGQGAFFLMRQCQMLLVSTGGRSCFFASPFVDEFGEEDHNVRRGRPLFLRPNRYMALLQLVFSHAIASEVSKSRRTSEQYIRAYFY

Pathway: Protein modification; protein ubiquitination. Function: Ubiquitin ligase protein which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. EC: 2.3.2.27 Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine. Sequence Length: 164 Sequence Mass (Da): 18046

K0C8U7

MQSNEKTVLVTRPAHQSDHLCGLLTAAGFTPIRYPTIAIQAVENTAHISNTLYQHSNYDYLIFISANAVIQADRLIDHQWQKTPSGMIAIGPKTADTLDQLGLKPAITAAKPFNSERLLTQLPSDLKQKKGLIIKGKGGRTLLAEQLQKRGMTVDTLDVYQRTLPNNYKTSHNKKPAYITITSQLALDNLFLIPPRPIGELKQQCTFVVFSERLARYASSLDCQHLLISHGASDKGLVSAINQDKKR

Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 3/4. Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III. EC: 4.2.1.75 Catalytic Activity: hydroxymethylbilane = H2O + uroporphyrinogen III Sequence Length: 247 Sequence Mass (Da): 27400

A0A484BHT2

MKHRKPYNLRNIILIYNICQMIYNGSIFLMAFYYLLIDGTYDITCMHTLSLDHPKKSIERWITYIFFMNKIFDLLDTIFFVLRKSYKQITVLHVYHHAMMVYFMYWVTRLYGAGGQYAVMGLCNTTVHFLMYFYYFNAGLRPKMKMNLCNTTADPETKEFPILDSAWPSTLICLGYLLFALKLGPIYMKNRQPYNVKPLMLIYNIVQVIYNGIMFSFGVYRVIINPAYDNKCMETLPLDHPLKPTERLAAYIFFLNKLLDLVDTVFFVLRKSYKQITVLHLYHHVIMVYGTYWVLRMYGTGGQYAMMGFFNSFVHTVMYSYYFVSALYPELKGNLWWKKYITRLQLAQFILLFFQPIHVLIFNPTCGFPLGLHLMQLAAAVSFIIMFSNFYYHAYIKPKPLKTQ

Catalytic Activity: a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA EC: 2.3.1.199 Subcellular Location: Membrane Sequence Length: 404 Sequence Mass (Da): 47943 Location Topology: Multi-pass membrane protein

E0SA59

MNNDLLLGQILRVPPITRCMVLLITMVSLLVYVDAVSPYSLYYSPLFLRKFEVWRIFTSFLYFGKPTLDMFMHVVFLYRYSRMLEEGCINTSEYFWLVLVISSTLFAISNIYGISALGTSFSSTITYIWTKRNPRAIVQIFGFISFPAFYLPFILPGFMLLTRRSISIDDVLGIVVGHLFHYFKDIYPRWGRDILKTPCWVKKLFKEHPSGCCKTQKGITIREGREKYKRNIENGNFAKTDENNEVGLIDATDPEINKVDDEYVGEESPSQSCTESLREKDLSIAFSQRPSIVSSTVMTSSIGPEENCLGVVEACSSKEPVAGNDPESRSNEEWDEKWGESDNESTG

Function: May be involved in the degradation of misfolded endoplasmic reticulum (ER) luminal proteins. Subcellular Location: Endoplasmic reticulum membrane Sequence Length: 347 Sequence Mass (Da): 39606 Location Topology: Multi-pass membrane protein

A0A2C6KTZ9

MEVLVRFKGARHKISLPSDATLGDLKHEISVVTDLPSQQQSLKTGYPPRLILLPSSQTDESSTKLRDVGIESKDVVIVEQQTSSSLHQPLSPPQSKSSHLGNSNSKTSSSSSSMPSTSDCRQGVTAPKDLSSRSSLERSSPSSSQASSHMTSASSSFSGSTANQGEKLSSSSSSTSRSPPPPPSTTASSTGAATSSSSSLMYGGKSSCFPPQSSSTSRSSSSSSSSSGKTREIEGDRSDSKGARLTMTNPSSSSSTRSQGNSAMNMDADGTRGSVYTPSSAGDPSSGRHSSYSSANPHFSSKGRSGREEDDEDEEDDEDDEEEEEVSPSSSFFPVAPPDRVGDLLRYVVPSDNSCLFTCLSMLAAPTKTPQCLRDMVGKAILYDPESYSDAILERPRQEYIQWITSPTSWGGYVELAILANQLQHEILVMDIETKRKDVYGDSRTGRRIYLLYDGVHYDAIIGRSKTPPSSSRQKEVYFRVFSPSDLRTEQKAAALAAEFHQKRQYVNLNEMKFQCLVCGVSIRDQAAVKLHAKETGHANYGENKR

Function: Hydrolase that can remove conjugated ubiquitin from proteins and may therefore play an important regulatory role at the level of protein turnover by preventing degradation. Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal). EC: 3.4.19.12 Subcellular Location: Cytoplasm Sequence Length: 546 Sequence Mass (Da): 58873

A0A1X0RGW5

MSREDWVDCYRNKTVLITGATGFVGKAILWHLLKTVGGVIDKVYVLIRPKRIPGGSPSQRLLDEIINTSAFKRLMDKKLLGREKLIPISYDLTLSQLGLSMEESMQMKDTNIVIHCAATSEYESSLEWNLEVYINTKCFVLSILKILLDKCVGNNKINGLPQCMLKYK

Function: Catalyzes the reduction of fatty acyl-CoA to fatty alcohols. EC: 1.2.1.84 Catalytic Activity: a long-chain fatty acyl-CoA + 2 H(+) + 2 NADPH = a long-chain primary fatty alcohol + CoA + 2 NADP(+) Sequence Length: 168 Sequence Mass (Da): 19041

A0A8K0H3V7

MTHTSPQPTPTLDHQAFIFTVIANGIQARGIPPLLLGKDVLGAARTGSGKTLAFLIPAVELLYHARFTPRNGTGVVVICPTRELAIQTHAVAKDLLKYHSQTLGIAIGGANRRGEAERIAKGVNLLVATPGRLIDHLKATKGFIIKI

Function: RNA helicase. EC: 3.6.4.13 Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate Sequence Length: 147 Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis. Sequence Mass (Da): 15657

A0A336N0L3

SVLEYQNQAKLLFRKLTPQSPKRCSIETGPYLFHYIIENDVCYLVLCDRQFSKKLAYSFLEEISQEFDNTYGRRVNSVTRPYAFIEFDIFIQKARKGLSDRRRNINSINTQLQDVQRIMVKLHHISKKTYFSYEISSQVQNIDDVLARGAVLSELDTKTQNLSMLSAKYKKDATYLNRKSMYVKAAAGLIVFLVFIFYFWVL

Function: SNARE involved in targeting and fusion of ER-derived transport vesicles with the Golgi complex as well as Golgi-derived retrograde transport vesicles with the ER. Subcellular Location: Endoplasmic reticulum membrane Sequence Length: 202 Sequence Mass (Da): 23733 Location Topology: Single-pass type IV membrane protein

A0A7V8T000

MFMLLAAGAMAQVPAAQPPAGSVAATSLDSGLYAIFNTSMGTITAKLYEEEAPITVRNFVGLARGTKPWKDPRTGDMAAKPLYNNITFHRVIPNFMIQTGDPTATGSHDCGIKIKDEIVPSLKFDRAGRLAMANTGRPNSGGCQFFITEVPYPSLDPPQGAYTIFGQVV

Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. EC: 5.2.1.8 Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0) Sequence Length: 169 Sequence Mass (Da): 18040

A0A2E6GZ59

MKIAVLGCGNLATAVVSKLEGFEFHTYTPSYIRAEELAKLKNGTAYKELKNIPLTDFVILGMKPQQFEEFAKVYKDFFDDSSVVISLLAGTSTDTIKKALGAKSVARVMSNTPAIIGKGLHALYFSNVDQSSVVESMFKVSGETIVLDSEDKIDGITHFSGSGPAYLFDLARILTSELEKRGLTNEQANMAIKQTLLGSAELLKNSELPAIELRKQVTSKAGVTEKVLESLWDFGIDNAYEKALIAGDERIAQLKGII

Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-proline from L-glutamate 5-semialdehyde: step 1/1. Function: Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline. Catalytic Activity: L-proline + NAD(+) = 1-pyrroline-5-carboxylate + 2 H(+) + NADH EC: 1.5.1.2 Subcellular Location: Cytoplasm Sequence Length: 258 Sequence Mass (Da): 28106

A0A1F3SIV4

MFLVIIFSLSAFLAVAGALSVTFSKNLIHACVYLLFSLVGVAGLYLTLGAEFVAATQLVVYVGGVVVLLLFAIMLTGGTNLHHVTSRFGLESTPLMGNLRTYLMGVVTAVLLVVVLCNVLQGSMTGALVSENKFSSTVEQIGVKLLTDHILAFEISSVLLLGALVGAAIIARPHRSSESEN

Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+) EC: 7.1.1.- Subcellular Location: Cell membrane Sequence Length: 181 Sequence Mass (Da): 19040 Location Topology: Multi-pass membrane protein

A0A8K0DTM4

MDDDSNLEFELEAFPSISREAATEVAACVKVNMVIIMLQLFRDLTVMGTVLSLYTLIHSERQPLHKGLEDHFQCKEVKSASAGLTAAALLAMVPSYISRYVAGSYDNEVVAIFALTFTFYLYIKFALGEATPLLLILFQCMSFYAL

Pathway: Protein modification; protein glycosylation. Catalytic Activity: a dolichyl diphosphooligosaccharide + L-asparaginyl-[protein] = a dolichyl diphosphate + H(+) + N(4)-(oligosaccharide-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl)-L-asparaginy-[protein] EC: 2.4.99.18 Subcellular Location: Membrane Sequence Length: 146 Sequence Mass (Da): 16263 Location Topology: Multi-pass membrane protein

D8LEW5

MQDMFREFSEELGSPENAGKNKAEIEDIFSYTSVGHKHIVRNVPSEDRIAIHQAVVPTIDDKDRKDLDIDSIDTTPFAMFGVFDGHGGPACAEFLTQSVSTVLAHSPVLYDEDLTPTQRRTFATADSFEELEKVHNKWADEIGDLSGSTAILSTFQDGVLVMAGVGDSAGLYVDHMGKQHNLCPQHSTSNEKEVERVLSMGGTIVNNRVAGCLMPTRTIGDLDCKRALGAIVSPHPEITLAAIYAPPDDGEPHDEPFLVLASDGLWDVLSFAEVAFITRKGLRNLRAHEKQERAKAEKAAAKAAQAAAADGLGGGGGHSTGGKTGLWKKMTSRKETAAWMDGGRRSLDVSRAGLRDSSIRGLDASVRGGQSPVLGHPPRGKQPLRHSASLDSSLYAGLRAEEQTRMIDESLHEVVEGVPASYDLGSVAAQAALAGPSTASTMLGEEDAAAAGGEQLPPVKAVTVASTEQTASVRTAGSDKHNVAMKLVHAALRAESHDDISVVVVTFAGTADKSPPGCRTNLPHHLPHRSSKSSLSGSSPIPEERPESMKAS

Function: Enzyme with a broad specificity. Subcellular Location: Membrane Sequence Length: 552 Sequence Mass (Da): 58575 Location Topology: Peripheral membrane protein

A0A3P7I6C5

MMRRTLIRYLVLTQAMVFRDVAAGVRRRFPTMNHLVTAGLMTEKELERFNSIKTKNAKYWVPMHWLFSLIRVAKEEGKIPGEVVYVDLMEVYLKITKVQFEKIRQFRVQILSLTLFDWVPVPLVYTQVVHLAVRSYFAIALFGRQYLQPHPDRDLNIDSAKTRIPGNFFTTGNASALPPSSEPGKSNNLVNQFGRQRHNSR

Function: Forms chloride channels. Subcellular Location: Cell membrane Sequence Length: 201 Sequence Mass (Da): 23353 Location Topology: Multi-pass membrane protein

A0A8K0MSC4

MASSSHERRRKVSYFYEPQIAHYFYGPDHPMKPIRIQMAHHLISRYELLPHMEVYRPLSITKEDLCAFHAENYVDFLSTASLETPARVLGQFGMGTGDCPPFPGLFDFCTASAGGSIGGAVKLNNAESDIAINWAGGLHHGKRCSASGFCYVNDIVLAILELLKVYGRVLYVDVDVHHGDGVEEAFYHTDRVMTVSFHQFEERFFPGSGYINQTGVGCGKDYAINVPLAQGINDECFVDLFLSIMSKVMEVYKPEAVVLQSGADSLAGDVLGAFNLTTKGHAECLRFLRSYNIPLLLLGGGGYNIGNVARCWCYETAVALDIEPNGILPDNYFSRFLESNLLHIEPDKKLDDQNKPKDIEKIKVMIMEQLRRLRHAPSVGFHTAAQVFKFPEMGEEDMDQSKCGVRIWNGEPCPDILTDKVHYQDYCLILEDNSSKVLRRGPKNAREAVKHFGKVPGLPKPYVRDAIRT

Catalytic Activity: H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-[histone] EC: 3.5.1.98 Subcellular Location: Nucleus Sequence Length: 469 Sequence Mass (Da): 52495

A0A4V1XEE7

MEFRRSSPVLDFFSRQTVFLTGSTGGLGGCLLYKLVVTLGVAKVFALVRGDAATAKRKWAASMGKSKSEDILGTGKIVFIPGDITKPSLGMFPEHCAEVQDSVSLIIHAAADINFRDPLPVLVANNTSSTLELASMARDFKKLHLFVHVSTAYVNSFLEDSEVAEEVYRVGDPEKEIADITAGRGSGRVEAYPWPYGYSKHLTEQLLTLKFPRMPLLIVRPSSIGPAAQVPFPQYMPAASSPLSNFYARLLFPTGGINTFPPCRGSASGTNVLDEIPVDLVANILLQHTYRRTMGVVHASSSLYVPKILDDYLADARRHAPASWRPRMAQNIFSTDNRLGTGKLANFYAVLSRDWRFRTSRSRDLDQGGILGLSLNGHDPEKYVEDRLRAIVKQAKQRFKADDQSMIEEPRL

Function: Catalyzes the reduction of fatty acyl-CoA to fatty alcohols. EC: 1.2.1.84 Catalytic Activity: a long-chain fatty acyl-CoA + 2 H(+) + 2 NADPH = a long-chain primary fatty alcohol + CoA + 2 NADP(+) Sequence Length: 412 Sequence Mass (Da): 45508

A0A8K0DKV3

MDVTLTNLRKYFPFLPHNALIKIYKARCARLRLLMDKGMPGDIHWIIEAKVRLAGESSDSIVSYMPRMGKSSYSKRRRAKECKFVTNVPMDLQWRCRSLGMVSINREDKINFIKDESKESLDDILLTLETHPCGVVHRELLNLWHLFKDEQHRHSLGNLTLNDPACQFIRKLDGKHILTHRRRLADSDSGKDKEFLKASTHPSTREKDSFSIWGGSLGLMGTVSLAAHVEGSKVLNIIPKALTATNITGMTVGTEIQVSTMHERISKMLEKSDAFIALPWGYDTLEEIFQMLSCPNEHPS

Function: Cytokinin-activating enzyme working in the direct activation pathway. Phosphoribohydrolase that converts inactive cytokinin nucleotides to the biologically active free-base forms. EC: 3.2.2.n1 Catalytic Activity: 9-ribosyl-trans-zeatin 5'-phosphate + H2O = D-ribose 5-phosphate + trans-zeatin Sequence Length: 300 Sequence Mass (Da): 34160

A0A7V8NTW3

IGTLLARQLAWRFVDLDERIEEAAGLSIPQIFERFGEPFFRQLEAGQLRAALGRASELKQGTVLALGGGTYAQSGCPEFLRSAGVPVLWLDAPMEVLLARCMTMTGRPLFRDEASFRALHAERLPSYRLADYRVESSGEPVDIVADILRLGVVASGGNQTHLMVEKPLP

Cofactor: Binds 1 Mg(2+) ion per subunit. Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7. Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate. EC: 2.7.1.71 Subcellular Location: Cytoplasm Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+) Sequence Length: 169 Sequence Mass (Da): 18552

N1USV6

MWFKPVMFGLMIIGLLWIIVFYITEAQWPIAAAGSWNILIGFGIAIVGFMMTTRWRS

Function: Involved in cell division. Subcellular Location: Cell membrane Sequence Length: 57 Sequence Mass (Da): 6567 Location Topology: Multi-pass membrane protein

A0A3P7J5A6

MLTNSNPYIDFPRPTLHKTVAIGGITVSADLRRNRLPEKWDTILNERNHTVLVSFGSVAKAVYMPDKYKKTLLKVFESMPDTTFIMKYEEEKDTWADHLSNVHLDVWLPQHALLGK

Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP EC: 2.4.1.17 Subcellular Location: Membrane Sequence Length: 116 Sequence Mass (Da): 13396 Location Topology: Single-pass membrane protein

B3M840

MVLGFLLRGSAVAGVVYYTQSVGIWGSTDKTDKLYNNVKSELCPYVQKAKKQLPFEVPQLPKSGEIRFLAKHYYNEGVKSSFRFVHMLPCYAGRGLKKIKDTFEDFAKSPAITGGETGAAK

Function: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. Subcellular Location: Membrane Sequence Length: 121 Sequence Mass (Da): 13415 Location Topology: Single-pass membrane protein

D7G8E8

MVRLEGRWASAGSTEPNVGIYSIAGEKAHDPLWKNQDAGLVIAPFDRREGQALFAIFDGHGKNGGQASRECMERLPKHLASASSQSGSPASALRRSCQRLHHDLATGVAGDCGRSGTTLCAAVLAGRRLTVANVGDSGCLRLSRSTAAASSGSSASPSAAAAAIPGKAALASDRGTPDVVDKAGGARGGGTSNRRRLRTAEKLIAGAAAGEEAAPGGGSRGGGLVTERLSRDHKPESKGELERIRAAGGIVFPLPRSGSGGGSGAGGVTGGAPPTAEGSKKGLKTAARGIAAGIPRVWTASGDGPGLAMSRSIGDKMAHSVGVTYEPEITEFDLDKRSDVMLVFASDGVWDVLSAEDIRKVRAFKPLRVRRNVFNEVLLLFVSQRGKRYRLQHESRCTHRSKHGSIHGGSGG

Function: Enzyme with a broad specificity. Subcellular Location: Membrane Sequence Length: 412 Sequence Mass (Da): 42422 Location Topology: Peripheral membrane protein

A0A365TWC2

MEMPKIARYAGTLAGLVSGVLLLATALLTLADVVGRNFLNAPVPGATELTELALVAITFLLYPRVAWRDTHISVDLLDGIMGPRAKWLQRLLAALIGVAAFGVLAWRLWLLGDRITGYGDVTPYLRIQLGRVYYGMSVLSGVTAIVYALRVALIIVIPRRLPELTGTPSKGIE

Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system. Subcellular Location: Cell inner membrane Sequence Length: 173 Sequence Mass (Da): 18709 Location Topology: Multi-pass membrane protein

A0A7S1CVY9

QHARKDSKKDAASAVEEPESDAEEALATITPGDADEWELFHFSGGLSEYVKHINRDRISAHEPIFFSRTDGDIQVDVSLQWCSDAFSDTLIGFVNSIKTIDGGTHMDGFKSALTRTVNSLGRKTKALKDNDPNLSGDHIREGLGAVVSVKVPAPEFEGQTKTRLGNPEVRKIVDNAVSTCVAEALEEQPNILNSVLSKALQAYKAAEAAKKARDLVRRKSVLTKSTLPGKLADCSSSLKDECEIFLVEGDSAGGSAKQARDRRFQAILPLRGKILNAERHDDAKLYKNNEISSLIVGLGLGLKGEDLDSLRYGKIIILTDADVDGAHIRTLLLTFLFRYQRKLFENGHIFVGMPPLYRLELGSGAKKVTKYCNSEEELERATKDLPPDSYSIQRFKGLGEMMPDQLWSTTMDPDSRMLKRLTVDDAAEASHMLTLLMGDKVGPRRELIEAHGKEYQFDELDI

Function: Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks. EC: 5.6.2.2 Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA. Sequence Length: 462 Sequence Mass (Da): 51078

A0A559MF56

MRHFTITSGLLACAAAVLGHSTFQEMRVDGYVFDVSTLTVPFINSTNSVDEVSTCARLPLNNNPVTSVTSNDLRCNAGTTPVSLLRTVAAGGNVTVEMHDQPGDLG

Function: Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds. Involved in the degradation of complex natural cellulosic substrates. Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans. EC: 3.2.1.4 Subcellular Location: Secreted Sequence Length: 106 Domain: Has a modular structure: an endo-beta-1,4-glucanase catalytic module at the N-terminus, a linker rich in serines and threonines, and a C-terminal carbohydrate-binding module (CBM). The genes for catalytic modules and CBMs seem to have evolved separately and have been linked by gene fusion. Sequence Mass (Da): 11168

A0A2C6KTV2

MMPNPPLPSSSSSLSSPPLPSSHLLSFSKTSPQKVLSSSSSSAAMALKKKAISLVVAMTPKRGIGRQQDLPWPRLSRDFKHFTQLTTRTHQDLFPSSSSSFSSFTYHQRKEEEQEGEKKKQKKIDGDHLSSSSSSSSCLAECDVGNSSFNAVLMGRKTWESIPAKFRPLPNRLNIIISKTMQEEEKEEVEEENKKENSYSSLQTSSSLREETAEKTKKEEVKSSSRTDKERRRFPYDRPVRICSSLPSALEMLDQDEEYSRTVNRIFIVGGSGIYKEALSLGVVSYIYLTRVGKEFSACDVFFPRFPGDEILSNPPSTSKATPTTSSSSCGTGEERPLRVPYKPRLLLSFLQEKKNSHEKEEEKKGNASERDGEKSQDEVEEKEQDDQGKDRKQEEEEEEGYYSPIFISKTYSENEVPFDFVILEKIRKADQHLSHSIQQTTPSLGGFFRLLLLLFFFFFRSDQSCPSSACPWSQGEEEFFLNLFKSFSSERCLSTDSLLLAKTHAVAAPLLAWMKEEEEETKKKRKRNEEEEEEKKTMEKVSYRACPRVVYRHHEEFQYLDLIADILTNGVPMSDRTGVGTLSKFGCQMRFRLDQSFPLLTTKRVFWKGVVEELLWFIRGDTNANHLSEKGVKIWDKNVTREFLDSRGLFRREVGDIGPGYGFQWRHFGAPYTDMHENYTDV

Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. Function: Bifunctional enzyme. Involved in de novo dTMP biosynthesis. Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, DNA precursor synthesis, and for the conversion of dUMP to dTMP. EC: 1.5.1.3 Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP Sequence Length: 683 Sequence Mass (Da): 78143

A0A484AW31

MCAKSQSFWERHELKFYRYGHIYASICGQVIIDYAPQQPMRAPFKSLLIAYSHALSLLLIVVLPGYFGYNYRALTATADRRMQLVLYVGLANTLIKYATVIVTYVANTCHFEAINRRCSLQRARLQASFAASYRASGWPKRRFELFMYLKFVLINLMMIVQICAILAVARIDRAGESDSDSDSASGQGRRLRIQFAIYAFVLWNYTENMADYFYYVNSCVLLYFRLLHMQLQAELEQLRRLGRGRLLLGVRIGLLRQRYAQIHALYTDSFRMHQFQLLGLMLATLINNLTNLFTIFNLLARSSRAFISLPVAVSGLYALGFYLDTYLVSLVGEHIKVEQTRLALTVRQFSDSPASLNQEVPQPNYAPIPIGCQLANHLSIVFQLEQFSLLLRHCRQPMLCGLVHLDRRLIYLISVTAFSYFITLVQFDIYLRTQHNK

Function: Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates. Subcellular Location: Cell membrane Sequence Length: 437 Sequence Mass (Da): 50412 Location Topology: Multi-pass membrane protein

A0A545W8A2

MSRNVMFLLGALATIAIAQMPADAYDVPAVPNVVGQPLDGFVSYSIEFASFPEFAGNMSSPNQFSYNLLKNLGDVMGTNPYIRVGGNTQDYALFNGSQPEALIGIVDPNRSPDYPTSITIGPAYFESYNTWPGFKYSHGLNLGLGGNRSAGWQTLVETVPLVCKTLANGKLYIWEYGNEPDLYGVSAQGPVRPPSWDEASFVWQWLNGTKEIRPQVKKSCPSLAEPRYMAPSFAALSSPLKEPKTWQSGLNTNQDIELYSTHNYISGATSPGVTLQGTLMNFGVTQASVNNHVQAYNSIFKARGKASAPPLIFGETNSLYNQGRPGLSNTFGAALWGVNFNLFSASVGFKRVHMHQGVNYRYQAWQPVDTDKATKGTKAPYYGSMAVAAMLRNSASQPVSVSNIALGNDQHEAAYHIARTIKMSTDKITFLTNWHATPYHAPLYLAQSKGFFAAEGIKVALLEPNDPSDVTEIIGSGSVNMGFKAMIHTLAAKARNFPVTSIGSLLDEPFTGVVYLRDSGITTDFRSLKGKRIGYVGEFGKIQIDELTSHYGLTPEDYTAVRCGMNVSKAIKNGEIDAGIGLENVQMVELEEWLEGQGRPKSDVQMLRIDELAELGCCCFCSILYIANDQFLAENPDKVRAFLRAVKRATDFVLDEPEQAWAEYVDFKPVMGTRLNRKIFERSYAYFSRDLQNVKRDWTKVTKYGQRLGVLGADFVPNYTNEHLEWVLDEASEDPTGDQKRMVELQCEVACNGGFRRLPRATAA

Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis. Function: Responsible for the formation of the pyrimidine heterocycle in the thiamine biosynthesis pathway. Catalyzes the formation of hydroxymethylpyrimidine phosphate (HMP-P) from histidine and pyridoxal phosphate (PLP). The protein uses PLP and the active site histidine to form HMP-P, generating an inactive enzyme. The enzyme can only undergo a single turnover, which suggests it is a suicide enzyme. Catalytic Activity: 2 Fe(3+) + 4 H2O + L-histidyl-[4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase] + N(6)-(pyridoxal phosphate)-L-lysyl-[4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase] = (2S)-2-amino-5-hydroxy-4-oxopentanoyl-[4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase] + 3-oxopropanoate + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + 2 Fe(2+) + 2 H(+) + L-lysyl-[4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase] Sequence Length: 764 Sequence Mass (Da): 84206

A0A1B3T857

HAFVMIFFMVMPIMIGGFGNWLVPXMLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVENGAGTGWTVYPPLSSGIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFFDP

Pathway: Energy metabolism; oxidative phosphorylation. Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O EC: 7.1.1.9 Subcellular Location: Mitochondrion inner membrane Sequence Length: 162 Sequence Mass (Da): 17445 Location Topology: Multi-pass membrane protein

A0A386B2D8

MKMLIMSIIFSLMFLISSTSFWSMWLGLEMYNFFFTPWLMEEEKYKKSSKIFFYFVIQVMASGMFLIGMSNPNSGFFYTLLLVSMLLKLGGFPLHSWVLVVVENMKWIKFSFFLTVSKIGPIVVLMMSNPMVSMIKYVLGGVITPILGLKSSSIRIMLAYSSIAYMSWIVTTICVSKSLLLFFVIIYWSIFICSCFFFKKLMMKSVKDFFRNSCSYLEMSVILSLMGFPPFLGFFPKLFTVKVLCMMSMIPEALILSTLSVIPFYFYLKMLMSMMMSFSFKNHSFLPLMTINKIIFFEVLLIMFSLEVLVYTCM

Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+) EC: 7.1.1.2 Subcellular Location: Mitochondrion inner membrane Sequence Length: 314 Sequence Mass (Da): 36526 Location Topology: Multi-pass membrane protein

V5KD81

TMYFIFGIWSGMVGTSLSLLIRTELGNPGSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSLTLLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMRINNMSFDQMPLFVWAVGITALLLFLSLPVLAGAITMLLTDRNLNTS

Pathway: Energy metabolism; oxidative phosphorylation. Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O EC: 7.1.1.9 Subcellular Location: Mitochondrion inner membrane Sequence Length: 202 Sequence Mass (Da): 21866 Location Topology: Multi-pass membrane protein

Q66UD9

IVLHDTYYVVAHFHYVLSMGAVFAIVAGFIHWYPLLTGLNMNNLYLKIQFSMMFLGVNLTFFPQHFLGLAGMPRRYSDYPDSCTTWNIISSLGSTISFLATLFFMFIIWESMISNRSIVYPVQLNSSIEWYQNLPPAEHSYNELPILTN

Pathway: Energy metabolism; oxidative phosphorylation. Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O EC: 7.1.1.9 Subcellular Location: Mitochondrion inner membrane Sequence Length: 149 Sequence Mass (Da): 17219 Location Topology: Multi-pass membrane protein

A0A2C6KG07

MVPLALNRPQELAVYSVSDAVATYYLYEQYIHNFILALCTIIPMTVRIKTVFLTLSFCLSSYPLSVSRRRRDS

Function: DNA polymerase II participates in chromosomal DNA replication. Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1) EC: 2.7.7.7 Subcellular Location: Nucleus Sequence Length: 73 Sequence Mass (Da): 8420

A0A2C6KZI5

MVVISSCSPSFFHSSSLSFSSFSFSFLCLLKSFSLSPFFITSLVCLIATIIMSTYGSVLRVHTFGESHGVAVGCIIDGLPSRLPLAPARDIQPQLNRRRPGQSFLSTQRNEKDQVQLLSGVENGYTLGTPLTMIVWNEDRKPSDYTDFSSSIPRPGHGDYTYHMKYHIHAKSGGGRSSARETIARVAAGAVIEKWLRLEYKTKIVAWVDQIGDISIPGPIRREWARSPPSREDVDRLGFVRMSCDGNFFLDAEGKLYDRSGEELKDDKHRQKARLLFASPADRSTAGGGGGGAGEKGVETRCPYPSIAVKMAAKIHEIRELGDTIGGCISCAVVRPPLGLGEPCFDKVEAELAKAMMSLPATKGFEIGEGFASVSMRGSSHNDPFVSFHPSPSTHHPTVNSSDCSSPPPPLPPPSSSSLSAAGPRTSASPSSAKSRSSGVNGKTSAASHPVSASSCISSLSPNSSSSSSPAASCQQQGRSSSSSTSAASSSSSPPASAQQEESPQPTSEHSSSSSRSNSSSDSNSNNSDHSAHQRQTKTDQPSSSLTSKTQKPPSSSSHSVSSSAPSSPPPVASPSPCEEGESKISPSVAVGEEKDRKKSEEEKDPPASSSSLQPSTIGEGGGEGGGGRGRSIRSSSGQRTPSYKPTTNNRASATSSQGGGGGAEMKIKSTGMAANEGKGEEGETSLQGSTVPGVGGSDLSLLRCESNHAGGVLAGISSGENLFFRVAFKPVSSISIEQHTADYTGKPRKLAVKGRHDPCILPRSPPLVESMAALVVGDLCLRQRAREGPKPLLVFP

Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7. EC: 4.2.3.5 Catalytic Activity: 5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate Sequence Length: 797 Sequence Mass (Da): 83473

A0A2C6KWE4

MHGRTKKSESALSLEEIEARRQKVKKGLKLLSHLLDQKNRGVYTPENFAATGKILDFAPEMGALWAYRREMLLHFLRQLRSEGEKDEEKEEEEKEGRSHANEEKTEEEEERNAEVHKEEEEEKDGEEKEQDGGHSVSKKRRKTNRIISSSSSSLSSSLPSSSSSRPSASSSVSCLTFLSHLHGGKDSQLDSCQKEGGADSSRDLHLLPPSPHLSFRDRAVFSLLYEELLSTRIAIAKKSSKNYCIWIHRTSCTGYLIHFLLSLSSTSPSLSSPSPASSLSSSPSPSPSSSASSLLSSSSFSLALSCILSLLREEMGSVESLLLSDSEDGRNFHAWHYSSQIASWRDAFLSLLSVVQKKSRKEEKENKEKKKKGANIDRRHLAKKGEAASQEKGEEDGEEEESEEEEKRRRDSEEEERMLQFTKRLIDKDFSNYTAWLYREQALFPSPCLAHRQVSTSSSSSLCRGCSFLRQSHKEAFEKELAWIWQGLYTEPNDQTLWRTYTSIILRFYHRQLKQRLLPSPHLVDLSSFSLPFNRKTHRHQPIDSSSLSSSPSSSSSSSLSSSCQSKDGGEESLVKETAHREETERDGVASEERKKGKEKRKMRIGWCFHFSSFCCIDTKESKCLLEVSRKDKERRERKKTTYSLAGDWKGLTSLSSRLSQGFNT

Function: Catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to cysteines occuring in specific C-terminal amino acid sequences. EC: 2.5.1.60 Catalytic Activity: geranylgeranyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-geranylgeranyl-L-cysteinyl-[protein] Sequence Length: 665 Sequence Mass (Da): 75358

A0A2C6KMH2

MPGRDPKPGGGAAAFVASPQVILQQLLHARNEYRTQQQYSQRRDCEADHGDLERPGGCRATSVSSVVDSAPEGRAAPSETGAEQHSPEKRSEPVLANSVPLKTAEAPQSTEDSACIQGRQGDESFHDDHSPMPGGIAPSKEADWNSPSSHEVAKDESSFAPVVYSLASSSGAEPHSESGLLKIRSDRSGFGERVSGQQAVSQGGSFSPYTTAGEGSGDEDEELRTVVVVMRHGDRKPKQKLKFQTEQDLILELFEGRSPRKEVKLKSPEELKDLLERNTEIITSMGREMASLVAGIKTLSEHKAAAEAAAKASTSSDPKPTSESPGSGTASPCDHVPELGPGTPEGGPPRVVFSQPFGLMKDEASCMATPSPPDSTSNPDGSGHIVADVTAALERQEGLVAKLQKELAQHKQLQKVLLQGDGFAGINRKIQLKPTEWDDAGFSSDSSATTKCEVPCPRDGLSEGQTVSS

Function: Bifunctional inositol kinase that acts in concert with the IP6K kinases to synthesize the diphosphate group-containing inositol pyrophosphates diphosphoinositol pentakisphosphate, PP-InsP5, and bis-diphosphoinositol tetrakisphosphate, (PP)2-InsP4. PP-InsP5 and (PP)2-InsP4, also respectively called InsP7 and InsP8, may regulate a variety of cellular processes, including apoptosis, vesicle trafficking, cytoskeletal dynamics, and exocytosis. Phosphorylates inositol hexakisphosphate (InsP6). Catalytic Activity: 1D-myo-inositol hexakisphosphate + ATP = 1-diphospho-1D-myo-inositol 2,3,4,5,6-pentakisphosphate + ADP EC: 2.7.4.24 Subcellular Location: Cytoplasm Sequence Length: 469 Sequence Mass (Da): 49696

A0A2C6L1S0

MVLNSNKKKKRKKKISLLHGSSPCLRLAPYSCSSFSSSSSYPCLFGRIRLKFVSFLLPLRGACHSHIPLQQHPTLPAVFACCKFFSSSSLSRSSSLPSLSSISPFSFSSFPPSYRFFSSSSFSSSSSVSPLLSSPVLLTSSSSLSFHSSSPPTSTRRSSLIHRCSHLSSAFSSSQTSSTLSLQSNTTPPSSSSQSSSSSSSSSSHSSSSSSHSSSSSSSSDSSSSSSFFSSSFIFSLLRRSLPSSLLSKLSAYFHLSRLHAPIGSWLLFWPCAHSALLALPATPHSLTYSLASSAYIREQTEGSTLHQLIQAWKDRHLPHSPPNTSPSYEAEEEKEEGEKEEEKGGFIENVKSIFLSSLPFGREGDGHTERLLGRQESLSLFFTEKNTRRQNETEGEEEGEKKEKLFAPIEDLWGVCVKSILLCGCGSILMRSAGCIINDLTDRHLDAQVSRTRNRPLASGRLSPKEAFFSLFLHLLLSLFILLQFNPLTVLVALSSMFLVCLYPFMKRVTSFPQAVLGLTFNWGALVGWISILHSFHSSSSSSSSSSLSLSPSLSSSFSDNSPLGGSCTSSSSSSSLSPDEEDKKIYHLSSSQSPTYQQRLHTTHPTPSSSSSFFSSLSGKLVSPFNTSESSSSSSSSFSSFLSPCISLYLSSVFWTLTYDTIYAHQDKRDDVKAGIKSTALFFGDKKTPFYISIFSSLYAVGLIFTGLQADMSWPYYAVGVGGCLAQLLKQSMLTNLNDTLACAKAFRSNHTVGVTLFLGILASKVYERIVYMKREKQDNERRNDDEGMEDNKEAHEEEEEGEKDTKKRREEERRVV

Pathway: Cofactor biosynthesis; ubiquinone biosynthesis. Function: Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of coenzyme Q (CoQ) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate. Catalytic Activity: 4-hydroxybenzoate + an all-trans-polyprenyl diphosphate = a 4-hydroxy-3-all-trans-polyprenylbenzoate + diphosphate EC: 2.5.1.39 Subcellular Location: Mitochondrion inner membrane Sequence Length: 819 Sequence Mass (Da): 89689 Location Topology: Multi-pass membrane protein

A0A1V5Z5V5

MNHQVNLDRIKNAMKPATSIWPWSGGKRPQMRSFKEMTGLSGGIISAVDLLNGIGVYAGMEIIRVPGATGFIDTDYQAKARYAIRALEKLDFLFIHVEAPDEAGHMGSIEEKVKAIERVDEMIGTIMKEFDGRIAVLPDHPTPVRIKTHTAEPVPFAILGKDKDSTTRFSEKEGAKGMYGLMPGTGLIPLLIS

Pathway: Carbohydrate degradation. Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate Sequence Length: 193 Sequence Mass (Da): 21165

A0A2C6KXB1

MSTTATGNPSASPSRSKREGKPAGGFSLLGHLYLCLYNTAALVAWAYVFYLFLEHCLEKRSWMAGGGAPALYRRLEWPLIIAQSMQIMEIFHAMIGLVRSGVVTTFIQVFSRLQLVLFLFRQIPASYNTIAFFSLIGAWCLAELFRYPFFIVQEFLRCFSQGQKAPSSSASSQTGAEVPMALKWLRYSGFTLLYPIGITSEVLCMFESLHTLKLPMFAHYPYPMPNVLNFEANLYFIYIAVLLAYIPGSFLLYNHMLQQRKKNLYGSGSDKEKRQ

Pathway: Lipid metabolism; fatty acid biosynthesis. EC: 4.2.1.134 Subcellular Location: Membrane Sequence Length: 275 Sequence Mass (Da): 31194 Location Topology: Multi-pass membrane protein

A0A5C7UT17

GAAVERGGRDPSTAGPPQGASAPSAGSATGQAFGCLNIHASLLPRWRGAAPIHRAIEAGDAQTGVTIMQMDAGLDTGDMLLAQALPIGPRATTASLHDELAALGGQLIVQALQQAAQGRLRPTPQPAEGVCYAHKIDKHEAAIDWHQPAAQIERRIRAFDPFPGASSQLGDTVVKLWSSEIDSCSRPSDARCGQILAVDEGGIAVACADAVLRLTELQRPGGKRLPAREFLRGFALAPGQCLGEGTGGAP

Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus. EC: 2.1.2.9 Catalytic Activity: (6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-tRNA(fMet) Sequence Length: 250 Sequence Mass (Da): 25768

A0A559M3J5

MSPLKSAASRALRSKLLAQNPRLFNKAKRSVGLAATARSEPNFPTPFISPGNLLDFHSSTITTPLPRGFPTTRPRERNENDFDGLIANLTQTLTTTRSRTPTLPALHQLMKSYTSDPAHWSRFAHVDPSKQYTRNLVYSVPGVFNLLLLVWNPGKESPVHDHADAHCLMKIMKGSLVESRFAIPSRPGEQGPLVQTARKEFGLNQVTYMADVLGLHAISNPHPTEHAMSLHLYTPPNAALRGCNVYDMRNGAVRHVRQDTYDSVGGESGSDTSLHEEDTNRFFGWGW

Cofactor: Binds 1 Fe cation per subunit. EC: 1.13.11.20 Catalytic Activity: L-cysteine + O2 = 3-sulfino-L-alanine + H(+) Sequence Length: 287 Sequence Mass (Da): 31892

A0A559M058

MWVQQYEEMARCNGTYYVVVLVDGERDVIVGTGTLVVERKFMLNLGKQGHIKDVVITASHQGKGLGRALIRALDLIGEQLGCYKTILDCEPKNEPFYRKCGYKRMGIDMEHRYDEDETARSHAA

Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I): step 1/2. EC: 2.3.1.4 Catalytic Activity: acetyl-CoA + D-glucosamine 6-phosphate = CoA + H(+) + N-acetyl-D-glucosamine 6-phosphate Sequence Length: 124 Sequence Mass (Da): 14112

A0A963M9Q5

MKSIAQIAAELQGYDPQALPADAVNGFLARLVAPVADVQRVPVMQALGRVLAEDVVSPVSVPPHDNSAMDGFAFRGTELVAGQPLVLRSVGTAFAGAAWQGTVAAGECVKIMTGAVMPAGLDTVVPQEFARVQGDHITVPAGVVRAGDNRRKLGEDLMAGQPALLKGERLAPAALGLVASLGMGEVPVL

Pathway: Cofactor biosynthesis; molybdopterin biosynthesis. Function: Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP. EC: 2.10.1.1 Catalytic Activity: adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-molybdopterin Sequence Length: 189 Sequence Mass (Da): 19351

G8PCJ7

MFKVLIGIIVVAVLIYIGIVAYQRFLLRKITDLQNRRANIGELPVKQKIQEVGDLSLSGSSQVNFNKIESDYSELTDKRLPEIDDIAEHAKQDVNEMKIFEARKDTTAMTDALNAIEADSNRIDDQLENFKKVDQEQHDSVKILRLKYQEFRKSLLAQNLTLGPSIDMLEENLSNLDSDFDNFSQTVDDGDHEKADGQLKILQERTNNLEQQINEIPPLYERLKTTFPEQLEEIQGGYDQLINHNYAFPDDNVRKEIHDLDAKISENTETLANLRLDAVRDNNESISKRIDALYDILQREIDARKDVDNSFPVISEFMTHAEKQNKALLAEIERLDQSYVLDKEDLNESQSLGAQLEALRTEHDRDTEQMTNQPVIYSEILERLRTENEQLKNIEDKQAELDGKFQSIINSEKAARQRLAQYDTEIHNIKRHVENLNLPGVSDEYMDYFFVVSDEIERVGNNMNQVRINIDMILRELDMVNTDLQTLTKKTTDLTDNAALSELAFQYANRYRNNNEDVDLASRRAQKLFDSDYQYEQSFQTISSVLDKVEPGSVENITENYYQQKTTEY

Function: Negative regulator of FtsZ ring formation; modulates the frequency and position of FtsZ ring formation. Inhibits FtsZ ring formation at polar sites. Interacts either with FtsZ or with one of its binding partners to promote depolymerization. Subcellular Location: Cell membrane Sequence Length: 569 Sequence Mass (Da): 65930 Location Topology: Single-pass membrane protein

A0A3B9QEY5

MAIAVSGVSNRLDYFIASIIGGSLILLATSIKQGTLASVFGVSGAVYIGGLLGCLGLLRVQPDGREWCFVVLFVTWANDMGAYFGGRAFGKRKLAPTISPGKSWEGACFGLGAGVLTGACLSSWTGFAVAEGAVVGALLAVMAQVGDLVESKLKRYCQVKDSGKAIPGHGGFLDRFDSLLFTGAGGLLLKGLYGLLLHT

Pathway: Lipid metabolism. Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-diacyl-sn-glycerol + diphosphate EC: 2.7.7.41 Subcellular Location: Membrane Sequence Length: 199 Sequence Mass (Da): 20525 Location Topology: Multi-pass membrane protein

A0A1F3SR48

MQYFRYELYHRELAGPLASLQRWFQEKNLGIIKALSIGELYFIASTERDCLKKVESAFCDPVLCTTTPPHYDMAVQITFRPGVTDNKGQAAHEALQLIGLQAQVRSGRLYLISGDVSHAELLSAAHALLANGLLEECQVYTRSEFEKLPREVEITGPVGEDLSAKLVREIDLAKSDQELLGLSGKNCWALELPEIKVIQAQFKNEDFLAHRRRLALPENPTDVEMEILAQTWSEHCKHKIFSAKIHYSEGPAATHAFGPAEINGAFRTFIKGVSEEIIAERKIDWAISLFKDNAGIVRFDKNIDLCAKVETHNSPSALDPYGGALTGILGVNRDILGTGQGARPILNTDVFCVAQEKTSAEEIDADAVALSELPKGLLSPKRILEGVHKGVEDGGNKSGIPTVGGAIYFHPSYAGKPLIYVGTVGVLPPAIKGKPTDKKEIFPGDLIVMAGGRVGRDGVHGATMSSLELEESVPLSVVQIGDPITQKRLQDFLLEARDLGLYRTLTDNGAGGLSSSVGEMAQLSGGAEIDVSKCPLKYHGLMPWEIIVSESQERMTFAVPETSWVAFFELSLKRGVEASVLGTFTQSGFFEVKVGPDTVASLPLAFLHDGLPPMELKAYWNGNENIGRAFEWRLAKAPAAPKVDFKHTLERLLSRPNIASKWPWITCYDHEVQASTVIRPMGGMNGEAPHNAGGVWLHPHGGEMENGVLVSMGLNPRLSLVDPYLMGVCAVDEAMRNGIVHGGDPAFTAILDNFCWPDPMQQARPESPGPGDQKLGMLVRTLMGLRDAARALGVPMISGKDSMKNDFKGRHLDGREITISALPTLLVTAISRFDVRKSISPAIPGPGVCLYLMGALRGSLSASEFAEIYADSTKDENLLWQMLEKLKDMRAQYEAIHRAILDGVVVSAHDLSDGGLAVALAEMLLHSQKLGLDCELAVPVDDQVLFGEGPFRMILGVPNEKRAEFESRMSAFTYLGQTREGHELKIRTQDGEESLQMAVSEMSYFWNRSIK

Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 1/2. Function: Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL. Catalytic Activity: ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate EC: 6.3.5.3 Subcellular Location: Cytoplasm Sequence Length: 1011 Sequence Mass (Da): 110509