ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A8D8A593 | MCLVTLVAAGILLRATVSLYSYSGHGKRPMFGDFEAQRHWQEVTVNLPIADWYRNTTDNDLLYWGLDYPPLTAYHSFLVGKWAQLQDPKFVELHKSRGITNQGHKRFMRNTVLLADLLIYIPAVLLACHAVRKTIHRESATGVDLLFMATAILYPGQLLIDNGHFQYNNISLGFAAA | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 177
Sequence Mass (Da): 20006
Location Topology: Multi-pass membrane protein
|
M1V243 | RQAIAGVNPVSIERMTVFPPVSKLDPEIYGPQESALKEEHILGYLNGMTVQQALDENKLFMVDHHDVYLPFLDKINALDGRKAYATRTIFVLTPRETLKPIAIELSLPQSGPRSRSKRVVTAPVDATTNWLWQLAKAHVCSNDAGVHQLVNHWLRTHACTEPFILSAHRQLSAMHPIFKLLDPHMRYTLEINALARQNLINADGVIEACFTPGRYCMEMSAVAYKNFWRFDMEG | Pathway: Lipid metabolism; oxylipin biosynthesis.
Function: Plant lipoxygenase may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding.
EC: 1.13.11.-
Sequence Length: 234
Sequence Mass (Da): 26521
|
D3TB40 | MRSRRNIEMHELIGLDVEIKDSTNPNQIGKRGRIVDETYHMLIIEENGERKMIMKKGAKFGVWLGDEYVTIRGDRINYRPHERIKKLMRRRIK | Function: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
EC: 3.1.26.5
Subcellular Location: Cytoplasm
Sequence Length: 93
Sequence Mass (Da): 11179
|
I0BUX0 | MGDMQAKAELVWDIRAALGEGPVWDHRTGRLLWVDIEGRRVHCYDPSEAGDHRTIQLEQRVGAAVPRTAGGLVLAMQYGLYRLDMETEQLTKLGDPEEGIEGNRFNDGKCDEAGRFWAGTMNMKESEPTGSLYCLEADGSLRRALEGITTSNGLGWSPDNRTMYYIDTPTRRVDAFDYDGETGGISNRRTVISYEGEKGFPDGMTVDNEGMLWIAEWGGWQVSRWNPQTGERIGRIPVPAAQVTSCAFGGEDYSELYITTARSWIPDEQLAEQPQAGGLFRARPGVKGSAAGFYGG | Catalytic Activity: D-glucono-1,5-lactone + H2O = D-gluconate + H(+)
EC: 3.1.1.17
Subcellular Location: Cytoplasm
Sequence Length: 296
Sequence Mass (Da): 32659
|
G0XJ10 | NVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALTLLLASSMVESGAGTGWTVYPPLSAGITHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMRSTGMTMDRIPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGG | 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-cytoc... |
A0A367JKI0 | MTKLTFDFKPETPFGIYLYPYFERIYTLLTGKRASSFRFFSSKTSLNRDKEVIITCVAYCIIIFGGQWIMRNRPAFRLQKLFQIHNALLAVISGALLVLIIEQIFPKLYHHGFLYAICSSSNWTQPLELLYYLNYLVKYWELLDTVFLVLKKKKLEFLHYYHHSLTLALCYSQLKGQTTVSWVPITLNLFVHVLMYYYYFRTAAGARIWWKKYLTTLQITQFIIDLCVVYFCTYTYFSYTYLPWFPDWGSCHGTESSALFGCGLLSSYLLLFITFYRSTYKNKRREVADPQQTPTPVASTSTRQKKSKKL | 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: 310
Sequence Mass (Da): 36632
Location Topology: Multi-pass membrane protein
|
A0A4Q4VGH6 | MGRIRYNVAATLDGYIASPDGSTDWIVEDPTIDFTELFSQFDSFIMGRKTWETLVGFGDKNPLRDLQGVKISVASTTLDGSAPENRNVTLLRNEEEILQWVRNRKEEGSGKDLWVYGGGALCEILLRAGLVETVEVAIMPVLIGTGIKLIEARDGQSPKWRLSLQDMKALKSGIVMSRYLVLYD | Function: Catalyzes an early step in riboflavin biosynthesis, the NADPH-dependent reduction of the ribose side chain of 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate, yielding 2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate.
EC: 1.1.1.302
Catalytic Activity: 2,5-diamino-6-(1-D-ribitylamino)pyrim... |
G1E768 | MKMAIIFLVTFFLLLVDTIEQIQPYLIISYIFGLFLGVTDYTLYTCFGPFSKQLRDPFEEHENNFT | Function: May play a role in photosystem I and II biogenesis.
Subcellular Location: Membrane
Sequence Length: 66
Sequence Mass (Da): 7807
Location Topology: Single-pass membrane protein
|
I7KH47 | MKIIKVKDQLEGAKVGLDILKEQIAAGAKTFGLATGSTPVEFYNQIINSDIDFSDKTSINLDEYVGLDGSDEQSYRYFMSQHLFNEKPFKENFLPDGKAADLEAETKHYDAIIEAHPIDFQILGIGHNGHIGFNEPGTPFDTTTHVVDLTESTIKANARYFECEADVPKKAVSMGIASIMKSKTIVLMAWGEGKSEAIQAMVEGEVTESMPASILQKHDDVIVIVDEEAAKLLK | Pathway: Amino-sugar metabolism; N-acetylneuraminate degradation; D-fructose 6-phosphate from N-acetylneuraminate: step 5/5.
Function: Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion.
EC: 3.5.99.6
Catalytic Activity: alpha-D-gl... |
A0A8B6CWH5 | MPVFISWNCVILSIFGVYGVYALWDKPWFSKAMHCWIGWPNHHVTMDMYWYYLIELGFYWSTMFMITVDHKRKDSTEMTIHHLITISLLLFSWCNNFIRFGALVLVVHDAADSLLAAAKMSKYCEKERLTECIYYVFMVVWVSTRLIIFPYVLLYSTDFEIFQVDEPMITLVRQCWQYKIFNVLLHMLLILHFFWTYIIMKAAYLQIKQGEIKDIRSDSEEGNSEGGEKIEDEINRNSDTNNGYISQNNVK | Pathway: Lipid metabolism; sphingolipid metabolism.
Subcellular Location: Membrane
Sequence Length: 251
Sequence Mass (Da): 29825
Location Topology: Multi-pass membrane protein
|
A0A927NTG2 | MLKRTLVGAGIVITIFLLMWLYGWYIKVGVILAALVTQFEIIRSIKNKGIVLPEVILYVYTALLFPAYYFFDLPGVFAVMAAGVSALFIAGILNHEKYPQESIINGIFTMFYPQIYFVFLYMIVCMEDQTLSANLLLTTLANAMVTDTFAYFCGTLMGKHKLCPNISPKKTVEGSLAGILGGILGTLLVMYVLGNTGISLSAMPIVILFAAFASVISQFGDLAASLIKRHFGVKDFGNILPGHGGLLDRLDSTLFILPIVYFFFKIYFKF | 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: 270
Sequence Mass (Da): 29860
Location Topology: Multi-pass membrane protein
|
A0A2G9M2U7 | MPPDLFLGILSCIAGGALLFYGFSRMKKYMLINDTPTSKIRAVAMGLVEIGGAAVSKEYLKTPFSNNECVYYKYEVKEYREHTSVSKGRTTRSYSWDTIDSGEKRMPFFIADETGTIYVNPENAEFNVPIKKEFIEKAGLFKRAYSREGNHSLAEIPVNKITFLNKVGDRKYFESYLSPNENIYILGTADSYSGKAFIHQGQNDKNFIISTRSEKELLKAIRWQMIGGFAAGVALFLWGVHYFF | 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.
EC: 2.3.2.27
Subcellular Location: Membrane
Sequence Length: 244
Sequence Mass (Da): 27730
Location Topology: Multi-... |
A0A8D8AZI2 | SSSFCVSVTQDLCVTADGREGRCVPVNSCAWILTKSLTEKDTFHKSECGTLEDSTPLVCCRKWTNLESCGYGQSDDDGMMRESGAFPWVVDVLFKRLGRNHLFKCTGSLINSEYVLTAAHCVKDMPFRLKPHKVRVKRGQKFKEYNVERFIVHPNYTTDFNNKINDLALLKLAQTVDFTDQVQPACLPVDDVSDQLPKSGQTVSIYAAGPSKTESTRRDKKTHLNAGAGSGLVQQVLSRSLS | EC: 3.4.21.-
Subcellular Location: Secreted
Sequence Length: 242
Domain: The clip domain consists of 35-55 residues which are 'knitted' together usually by 3 conserved disulfide bonds forming a clip-like compact structure.
Sequence Mass (Da): 26875
|
A0A316QZ29 | MPCSVIRWAACTVRSSLPSGRTICLTSVLAFSRIVSMTDICFAPFAYRVYGIEMIFVGPLSRRTGRYHYSIPACFLHPFRRFFCGISPPVVYSGKTSGRLYPMRVVGIVAEYNPFHSGHAYHLAQAKALTQSDFALVVMSGDFVQRGEPAMFSKHLRTKWALAQGADLVIGLPTVCSLTSAAGFARGAIALLDSLQVVDTLCFGSELGDVSLLQQALDAADTPAYAQALTASLKQGGSYPAARDAALRAAQGVTPGPNDILGLEYLRALSLCHSAITPYALRREGAGHDQDGLFGPHASATALRGCIQAGDLESLAPYLS... | Function: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of elongator tRNA(Met), using acetate and ATP as substrates. First activates an acetate ion to form acetyladenylate (Ac-AMP) and then transfers the acetyl group to tRNA to form ac(4)C34.
Catalytic Activity: acetate + ATP + cytidine... |
A0A352UPB2 | QLIKNLTKKEDITVQRKLLEIFRALEFEKNYTKEEIIEWYLNAVYFGEGCYGVYTAARTYFDKDVSDLSLAECASIVAITNNPSKYDPFISTANNKDRQETVLRAMYDQGYIDYARYTAAVNEKLVFVRSENEEYEQQIYSYYVETVINDVIEDLMARKGINKEKARDMLYSGGYMIYSCYDPAIQASVDAVYQDLSALPQSYRGSSQQLQSAIVVMDPYTGDIVGLAGGVGEKTINFGLNRVYSQRPPGSSIKPLAVYGPALEYGLITQNTLVNDGPPSEVSLSGTTWYPRNAGGGYRRIITVRQALVSSINTVAAQIV... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-term... |
A0A8J9SG12 | MYSVVGFGLASSLIVALYMFLNGQQHSQLPRCWLFEPDDDGTCDKLTSALSSCGSGETVEQKCCSLSSVLAARRCHCRLGVPRQAKTQLEHMQHRCMHAHREIIEQQIFNQLPPGASPVAATAGGFQEAAKNLDREAAPGTWADFAKASSGRDASVEGHLADDTSSAGDDLEVDVEDSEDVHGEPTYSVFGSRGFGGQSAGRPVKLFVGVLTAGKNADRRAAIRESWGSDRRLHRVMFFSAKPVDEAVFDALRKEAAEKGDIVVLPGIFEHYDNITHQTLEILRAASMDPVATHALKVDDDSYVHVNNLMAVMARVPQRR... | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 470
Sequence Mass (Da): 52326
Location Topology: Single-pass type II membrane protein
|
A0A455UGT1 | MAMFLDIPYSAVALAAVIPSILYFLGLFIQIDAYAARHDIKGLPAIELPSLKQTLKEGWYFIFVFALLVWMLLIMQREAVAPFYATALLLVLNQLSKHNRWGWKDVSDTLSSAAKLFAELIAILAGVGMLVGALSMTGLSGTIANDFINIAGGSVPLLLIMGR | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 163
Sequence Mass (Da): 17730
Location Topology: Multi-pass membrane protein
|
A0A7Y3P320 | MIISLVAAADKNNVIGMNNALPWKLPADMKFFKNLTMGHAVIMGRKTFESMGCKPLSGRTNVVITRNKSFHTEPNILFFSNLNDALKALVSEKEIFVIGGAEIFREAMPKASIIYLTRINFSFEGDSFFPEIVENEWIEVGRTNHEPDKDNAYRYSFIKLTRKNGK | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
Function: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
EC: 1.5.1.3
Catalytic Activity: (6S)-5,6,7,8-tet... |
A0A149VT15 | MSPSLKQIWLSDWRHFLSLGLGAGLSPKGPGTVGTLVAFPFYFLLQVLGSSLYWFLIVIFLLLGVYICDYTAKALRVDDPSAVVWDEIVAFLILLLWIKPQGIGLLWAFLLFRLFDIWKPYPICWLDQRIKGGLGIMLDDLVAMLFALAVWYSLEGLIVGF | Pathway: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 2/2.
Function: Lipid phosphatase which dephosphorylates phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG).
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate... |
A0A4Q4VD48 | MAFTPFVFASPPTAGLFKFPPAPNPQSIPPPQYNVPFTIPDWLFTAALDAKVPLTIASVYAISAKILNAYNKSTGKKPWAISKTKAFEVFVILHNVFLAIYSAWTWWGMLHALKNSIVSPTGPDGWAATVDSFCRIHGPAGFGNGIFYNEALGKWETTSDQALLTASGEPSRVVPGRLWNEGLAFYGWIFYLSKFYEVLDTLIILAKGKLSSTLQTYHHAGAMLAMWGGIRYMAAPIWIFCFFNSFIHSIMYTYYTATALNIRVPQAIKRSITSLQISQFLVGGSVATIHAMIAYTVPVKVKSESTGLTETQYKGTHCMT... | 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: 432
Sequence Mass (Da): 47700
Location Topology: Multi-pass membrane protein
|
A0A355JDB4 | MKGRRNMLQQNTKTNKTRLYAFVGVFSAAAFLLQVIGTLTGLKVGGFLDVEISDLPALIIAFAYGPLAGVLTELIKNLLHCTMTSTGLVGELANFVMTGTLCFVAGMVYKHNKTFQGAVLSLIFATLALAAAGVLANLFIMLPLYMPSAPFSVKMNLVLFTILPFNLVKGVVLSVLTLLLYKKISPILHK | Function: Probably a riboflavin-binding protein that interacts with the energy-coupling factor (ECF) ABC-transporter complex.
Subcellular Location: Cell membrane
Sequence Length: 190
Sequence Mass (Da): 20483
Location Topology: Multi-pass membrane protein
|
A0A1Y5DZR9 | ALPGYLQQTDMESNGKSVSKSGDKLSWLTAPVVFGQEGTNGQHAFMQLMHQSDDIIPTDFIVALKGRSQYTENHKVLVANCFAQSEALMQGKTLAQVKAELLESGYTSKEVERLAPHKTMKGNTPSNTLVMDQLTPESMGALLALYEHKIFVQGVLWQVNSFDQWGVELGKQLGSRILSAIDGAEDDLLSASSQSLIARFKAGGNSKKNR | Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 2/4.
EC: 5.3.1.9
Catalytic Activity: alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate
Sequence Length: 210
Sequence Mass (Da): 22916
|
A0A8B6F5U4 | MKECFVRSPDIICYPCLSQKGGDLRAYGFSERKARLVTSNFISRVTTMREGTAYIGYGNYCGAGGSGPVMDPIDGCCKEHDECYLVIDTLQGCMSVDTNFMLLFNERRQELNCGRWSEGGIAYPFLAPSTVTYKRYQKNDEIHLL | Cofactor: Binds 1 Ca(2+) ion per subunit.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+)
EC: 3.1.1.4
Subcellular Location: Secreted
Sequence Length: 145
Sequence Mass (Da): 16327
|
A0A1U9NIT7 | MSKSLSKKQLKVLSVIQKGMPLSAAPYADMAESIGMATEEFLDVLRQWKDDGTIRRAGAVVNHLRMGVAGGIMVAWDVPDDSVESVGHLFAAFKQVSHAYERPRVPGWKYNVFTMVHGDTPKAVETTIDRMSEKSGITDFRKLRTVRELKKTPPVYVKEE | Pathway: Porphyrin-containing compound metabolism.
EC: 4.1.1.111
Catalytic Activity: 2 H(+) + siroheme = 12,18-didecarboxysiroheme + 2 CO2
Sequence Length: 160
Sequence Mass (Da): 17894
|
A0A7S2V5Q6 | FFTGVPPLLREKPIALYLQQKNRNGHSDSFSSQSPMITEADREAGVGDSGRASQGSSSHHGGGDHEEHGLGEVVIHQAIETIEFVLGMVSNTASYLRLWALSLAHAELATVFWEKALLSTIEMKNAGFIFVGYAIWAMVTFAVLLCMDVLECFLHALRLHWVEFQNKFYKADGFKFGPFKFKDILKSIS | Function: Essential component of the vacuolar proton pump (V-ATPase), a multimeric enzyme that catalyzes the translocation of protons across the membranes. Required for assembly and activity of the V-ATPase.
Subcellular Location: Membrane
Sequence Length: 189
Sequence Mass (Da): 21054
Location Topology: Multi-pass memb... |
A0A7S2V587 | MVMNTPGGNTVSTAQLAFTLITSMARNVAAADMSMKEGKFERKKYMGVELKGKTLAVVGCGRIGQTVAKWAQKMGMDVIGFDPAMADSVAEDLGIKLVSLSEVWPAADFITLHTPLTPDTRNLICGETISKMKDGVRIVNCARGGIINEADLLSALESGKVAGAAMDVYQKEPPSSEESLALIAHPNVVCTPHLGASTDEAQINVAKDIAKQMCATFEGKEYVGVLNVDYMEHTTDIRLEPFFALSEILGQLQAQTTKNHGKITAVEVECWGEHGVSLMRPKVQKLLKAVVLKGMLKHLQDEVEPTLISAPFLARELGIQ... | Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 1/3.
EC: 1.1.1.95
Catalytic Activity: (2R)-3-phosphoglycerate + NAD(+) = 3-phosphooxypyruvate + H(+) + NADH
Sequence Length: 456
Sequence Mass (Da): 49326
|
A0A8D8FXI8 | MSPIPAIAAIAVVLLFSNCCWSAAQLTAKDQPPVWDVTTLCNIPNEPGQKGTCSDPDDCPAYAAINDPASLSSVGRLSFLKAIQCNVSASTSAPGSAVGGGGGICCPRSGRYKSPTLNENLPRRTRTKSTMVHSRFGDDEMCGFQSYVAKIRGGDIANIDEFPWMAMLLYEMKDSNSVVHGCGGVLISRDFVITAAHCVTGREYDSKGPLKYVRLREYNVYDDPDCVIEQDLRDCSEEKVDAAPLRIQVHPDYDSNSRNKYHDIALIQIERSPEFSDFLRPICLPEPELENGATEGNKLSVSGWGRTDICRVLSF | EC: 3.4.21.-
Subcellular Location: Secreted
Sequence Length: 315
Domain: The clip domain consists of 35-55 residues which are 'knitted' together usually by 3 conserved disulfide bonds forming a clip-like compact structure.
Sequence Mass (Da): 34411
|
A0A3D4YHM7 | MKQQKVFTSGRLHQCSLPSLQRGGIAMLQLLSPGLVAYILGLTALLGLVMGSFLHCWAYRFARAQSAVRGRSSCPACGKVLGPLELIPVFSYFYQRSRCRGCGAGLSLRYPIAELLCGAYFVSVVWHFGVSPEALKYLIAGSLLFCIAWVDWDVHWIPDRLLAGIILNFVLFTAFQGGDPIKNLLTGLLGGLSVSLPLFILVLIMDRLLGRASMGGGDIKLLFAVGLYFSWQANLLLILAACVLGIVLSPMLRKKSPDSEDGEAFPFGPAIIAAYWFVLLWSEPLLNWYRSFL | Function: Plays an essential role in type IV pili and type II pseudopili formation by proteolytically removing the leader sequence from substrate proteins and subsequently monomethylating the alpha-amino group of the newly exposed N-terminal phenylalanine.
Catalytic Activity: Typically cleaves a -Gly-|-Phe- bond to rel... |
A0A2M7T0S8 | MSNLAPHIDTALDVKALDKLKTYLEKTYKAQGGIVTSDRNELTLHLPKKSLPAVMQTLRDDAQTRFTQLMDLTAVDWLGKNKLEERFHVVYHLLSLEHNLRLRVILTTGYSASGKAQKPDTTLADPVPSLQSLFPAATWYEREVFDMFGIPFTDAQDLRRILTDYGFQGHPLRKDFPVFGYEEVFFNEATSQVEYKAVDMPQETRFFNATSPWEGVNNPTPLADEDNTFPNKALK | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ... |
A0A7C6TNQ6 | MKINVVAVGNIKQKYFVEAIKEYEKRISRYAKLNIIEVKEFGDNEKTLLQEEQGILKNLKGKVILLDLEGDDISSTELADLFENSLVSGDSEITFVIGGSRGVSKNVKDAIPNKIRFGKVTYPHQLMRVILLEQIYRALSINAGSDYHK | Function: Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
Catalytic Activity: pseudouridine(1915) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(3)-methylpseudouridine(1915) in 23S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.177
Subcellular Location: Cytoplasm
Sequence Length: 149
S... |
A0A3D4QZ99 | MNIENISIVGLGLIGGSMAKALRRTNPNFIITGMDKNEENQLLAKQDGGIDKAADNLRDAVKDAHVIFLCTPVHSISEMLRELGTIVRPGTIITDVGSIKSSIMKEAERTFPVDIHFIGGHPMAGGERSGYASSIAHLFENAYYVLTPRTGTPSSAVKNLESLISSTGALPLVLDPLTHDIRVGAVSHLPHIIAATLVNTVKEWDNSEQSIQKLAAGGFKDITRIASSQPEMWRDICLSNKEQLLPMINDFIQKLTQFKKELESSNKAEIEVFYRQAKDFRDQIPSTESLYLLPYYMVYVDVEDRPGSIGEVASFLGDRN... | Pathway: Amino-acid biosynthesis; L-tyrosine biosynthesis; (4-hydroxyphenyl)pyruvate from prephenate (NAD(+) route): step 1/1.
EC: 1.3.1.12
Catalytic Activity: NAD(+) + prephenate = 3-(4-hydroxyphenyl)pyruvate + CO2 + NADH
Sequence Length: 366
Sequence Mass (Da): 40371
|
A0A3D5ZLT5 | MKVKVNAKLNLTLGVVGNIGKFHAIDSVVTSVDVCDVVEVSPRNDFVVTVGGMPWVSDERNTAYRMATALVQKFGVNGADIVVQKGIPVGAGMGGSSADAAAVAAAFCKIYGLEKSALRDVCATVGSDVWYMVSGGFARMTGVGNDIEFFDVPDEIYYVVTTFDTSCSAGEVYAWFDECGRRHLCDNDEVVRLLKQGNTDSAAKLYCNDLQTAVQEKTDYADKYLFFCGSRNIRSVMTGSGSAYFIAFADPIAAQNICDILNKTGYKSFVCKSVKHGVTEVR | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6.
Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
EC: 2.7.1.148
Catalytic Activity: 4-CDP-2-C... |
A0A970UMP8 | MSDYRLKRLAATGIFAAISIVILFAIPKFPLFLPFLEYDFADVPIILLTILYGPVHGLIVTAIVCIIQGFTLSAGSGVMGILMHFIATGTYVAAFGLLTRKLKSPGGYIFSAFIGVLAWTAIMIPFNILITPLFMKVPREAIYGILLPSIIPFNLVKSAGNSAIALILFFTLDRVTKRALTRERDKFLKPKADKKQD | Function: Probably a riboflavin-binding protein that interacts with the energy-coupling factor (ECF) ABC-transporter complex.
Subcellular Location: Cell membrane
Sequence Length: 197
Sequence Mass (Da): 21655
Location Topology: Multi-pass membrane protein
|
D3AIG1 | MKELLLRVSQEGIHGLYLLVFTLLIWLVFFLILAANPGNKINQWCFATGFLCGIGTFKEFLYYELAGLIHSPAAHAIPDWLYSVMSGVFYFFSLPCGLICALYFSHEDVKNPSAFRKKQAASFALAVVMILIFPCTQTLYYQSKVSFCLSTAAYNWLYGIILTSILLKTLREERLSANYNQRMLVTASVLLPLWCWLIAGFPYHALGLGGFSKAWQINLIIIVVILLFIVYHAFHSGIWGLRIRGEQYNWSSDEKLLQKNAHYVGHALKNDLAKISWCTGLLRQEQVRMKELDIIEQSVAHLESFVARTQMYSDRIVLKQ... | Function: May play the central regulatory role in sporulation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress. Spo0A may act in concert with spo0H (a sigma factor) to control the expression of some genes that are critical to the sporula... |
A0A2G6G8E2 | MKISDIKKEMLSLEVSDYENFLEKYSKDDRKGVQNILNTLSNKYNAYKKLLNRYNDLVRFDLENSNEGLVIGVDEAGRGPLFGPVVAAAVIINPNDKLIEVYDSKTIKEDKREFLFEEIINLSKDYGVGIVSAKEIDEIGILNATKKAMEIAVNSLEINVDTVLVDYVDINFKGKKVMPIVKGDAKSFSIAAASIIAKVTRDRIIRKMSKTLPDYDLLNNKGYGTKKHYEMIDKHGLSSEHRRSFLKDRL | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Subce... |
A0A7C6TMN4 | MSKQYGLIGKDLSYSLSKEIHSVVNDNYKYYPCKTVLDVEKLIASQELDGFNVTIPYKETVMSFISKTDTIAKEIGSVNTVVLENGNYVGYNTDYIGIIKTFDRLGIDVKTSNFLILGSGGSSKSVEYVLKSKGNNDYYIASRTKTKKPNYITYDEIDRIKSKINVIVNATPIGMHKYIYKEPLVDVSKFSKLQYVFDLIYNPNNTKLILEAKLKGIKTSNGLWMLISQALAAEECFLDKEISIDKFLLLEKELTLKNTNIVLYGIAGAGKSSIGEKLSKLLGKTFYDTDMLIEQKTNMKIPEIFKIFGEEYFRNLEKEI... | 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
S... |
F4ZJ02 | HAFVMIFFMVMPIMIGGFGNWMVPLMIGAPNMAFPRMNNMSFWLLPPSITLLISSSMIDTGAGTGWTVYPPLSMNMAHSGPSVDXTIFSLHLAGVSSILGAINFISTIINMRXTGMSSEKTPLFVWSVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDP | 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-cytoc... |
V4YIE8 | MKSSAVTAAHCQAAPAAAASIKPSRPVETAYLQGQPGTPFPVIRGIGWSEDQGRRPDMEDGMVAISNLAGVANAWLLGIYDGHGGRQTVEMLLQKIHGNVLQHLRSRAIERWQRYRQRAMSRLQDIRRRLDELHFQQQLACRDVRVLMPPTQRLVELLRLGRICEWVLQCEEPSQEGRTETEKSSASKAPTPPSFLTICTEEDVHRALDEAFVQTDVEILRDRVYQSGATACVCLVRPVLRLDLLLEMRPEEISDADWAWFSVERQKPNVIPASTPSQHAIVQADITVAHLGDSRAVLAYTDGHAERLTHPSDHKAGCER... | Function: Enzyme with a broad specificity.
Subcellular Location: Membrane
Sequence Length: 445
Sequence Mass (Da): 49117
Location Topology: Peripheral membrane protein
|
D8VV81 | TLYFIFGIWAGMVGTSLSLLIRAELGNPGSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSITLLISSSIVENGVGTGWTVYPPLSSNIAHGGSSVDLAIFSLHLAGISSILGAINFITTIINMRLNNLSFDQMPLFVWAVGITAFLLLLSLPVLAGAITMLLTDRKFNTSFFDPAGGGDPILYQHLF | 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-cytoc... |
A0A8J9SHX4 | MAVIEKPSSAGQGSKEDAMDSRLMDIDLSSLEAETRCAVCLGIVKNCRLVSGCMHRFCADCIEKWLRVASEPSCPQCREQMQSRRDCKRDSRFDRLLTLLYENISSYEAQVYDPSADVLQTAKKTGNALATAAAAQRAKRAGARPQQPRRPPAAPSRPATPPPPPVTADGLHAVTDGSSSYAAIAPSNTYPKVHPVLWMPQSTVQEAERMRTQSPSPMPASAGVPSRPSPGPATKGGDARGSKTPEPKQTTKQAKRAAAPKKSKQPKKQRTEQTPEPSKSEPPSSPDPAEAERTAVGQAAALAARAATAGAAEANQTTPM... | Pathway: Protein modification; protein ubiquitination.
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: 417
Sequence Mass (Da): 44868
|
A0A149VU74 | MSKNLVIKRVAVLGAGVMGAQIAAQCCNLNIPVYLFDLASNTSNNKNDITIKAIEHLKKIKPTPLGDNTVTQFITPLNYEDHAHYLADCDLVIEAIGEKLEWKISLYKTVVPHLAQHAVLASNTSGLSLTTLADQLPIERRARFCGIHFFNPPRYMDLVELIATDTTDSTLLDELETFITTYLGKSVVRAKDTPNFIANRVGVANMLFTLIEAKKYNLAIDIVDDITGKKIGRASSATYRTADVVGLDTLMHVVKTLQDYLPNDSFHRHYATPDLVEKLITKGAFGAKSGEGFYKKDGKAILKLDPNTMNYVASGDKAND... | Pathway: Lipid metabolism; fatty acid beta-oxidation.
EC: 1.1.1.35
Catalytic Activity: a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) + NADH
Sequence Length: 795
Sequence Mass (Da): 88578
|
A0A8D8CPA9 | IDSLNMLVNQIRSFSTTTQLGSLARWYQKLWRSKGPSNGPPYAHVTQVGDPVLRQKAQLVPSEAVTSPEVRFLVQAMIDVMRKYSCVGLAAPQIGISLRILVMEFKDKLRDEYTSAEYKIKEMDKLPLTVLINPELKVTNYKKKSFTEACASVKGFSAEVPRYSEVLLSGLDENGKSKELT | Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins.
EC: 3.5.1.88
Catalytic Activity: H2O + N-terminal N-formyl-L-methionyl-[peptide] = formate + N-terminal L-methionyl-[peptide]
Sequence Length: 181
Sequence Mass (Da): 20302
|
A0A0A2U4J5 | MGGLFGVVSKEDCVMDVYFGTDYHSHLGTSRGGMAIWSGNSFNRSIHNIENTQFRAKFESELPKIKGNMGIGCISDTDPQPLTVRSHHGKYAITTVGKINNFDEIADKAFFNHNIHFMETSKGAINPTELVSVIIDHENSFKDGLLKAQELLQGSCSILLLTPQGIYASRDKLGRTPLIVGKKEGSYCVSSESCTFANLGYSLNYELGPGEIILLTQDGVEKIAPSRDEMKICAFLWVYYGYPSSTYEGMNVEVMRYRNGAAMAKNDDVDIDMVAGIPDSGVGHAIGYSNQSKVPYGRPFIKYTPTWARSFMPQDQDIRN... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2.
EC: 2.4.2.14
Catalytic Activity: 5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1... |
A0A7L5BV12 | MTPGLERILRALDALAGSLVGLMLFTMMCLTTADVVSRYLFNRPIGAALELTEALMAITIFAAFPLVAARGRHITVDLTEMMLPKRARLFLDALAQLVCAAMCGFLAWRMIERAVQLHGYGETSAVLGYPVWPTAAVIALGCAVATPMFALRGLMLFRRAAKRGDRSQHAPEGALQYD | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 178
Sequence Mass (Da): 19357
Location Topology: Multi-pass membrane protein
|
A0A943YPU9 | MCKPILLIGMMGCGKSTIGRLLAGRMGLPLIDLDEEIARAAGKSIPEIFAEEGDAGFRLHETAALRRALNAGEAVIATGGGIVTREENIRMMREKGVVVWLCRPLEDMIADVRQDTRPNLAGDKEERMRTLYAQRAHLYEAAAHLQFDNRMPSREAAKMLEKLLTERKK | 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
S... |
A0A3L5TSF3 | MCAAMYLKGIFEFSKQGYLDSPKEFHIIDIHDEVLDMIKEWYTKYKKDPTCIEVSAVLKSSDSDHRSPLNRPPAWQHDERGNKRKPDNFSESQRRAGHVGKEVMQARAADPGPTTIKVVTKFCGKTDILIYTGNVLQLKGIDVVVVSEDGLMKGEGGLSMALLNAGCDRYKKEHKKLKPWILEHKQKTVLLTSGGDKLPFRHVLHAILRRQIAEQEQVFQRKLQTTIDNVLLQTNLLNIKSKKGITIVLPMIGLGSKPTEDVVKKCCWSVKQTIEKFLKTIPKVRIDEIHLVNYHDNVTEILQKYFDQQKPHIKQHPRPL... | Pathway: Protein modification; protein ubiquitination.
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.
EC: 2.3.2.27
Subcellular Location: Cytoplasm
Sequence Length:... |
A0A0M9VRB3 | MNDVLWEDVSDPTDWTGDWSALRPLDESLRCGLCYDIFRAPVALRECSHLFCSSCIRIHINQAGGNGSFCPQCRQKKAYDSELIAQPALEATAEHWRKARTFLMAQSKHLKELETSIADVTIPQLLAPEKAKRPAEESPSGRQLRPRKRVAGTPDMDEETDLDYRHLKEDTIVACPICQRTFDALALNAHLDRGCGADTPEASTSRPSQQNWLATPHSIPTKRLTRPQYQLKSERDLRKMLEACKLPTTGPKERLVERHRQWVNMYNANLDAAPALRESLPALRKQLQKWESAQNNAAASKGVSTEKQARAWLKSNQTQY... | Pathway: Protein modification; protein ubiquitination.
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.
EC: 2.3.2.27
Subcellular Location: Nucleus
Sequence Length: 3... |
A0A151BFZ6 | MAAVILAGGGGERLGRPKPLVELGGRPLIAYALEAALEVVDEVVVVASKGTSTVLRGMLPRGVEVVEDLEGGRGPLMGLYTGLRAVGVHYALVLPCDSPLLNIDVLRYLLERAEGFDAAVPRWPNGYIEPLHSVYRVEPSLRACGEALESGGLEVRGLLERLEGVLYVPTEELRALDPGLHTFFNVNTPEELEEAEHILREKRRGSP | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
EC: 2.7.7.77
Subcellular Location: Cytopl... |
A0A352A2N8 | MYNDNVEKLKNILKTQRYYGSIGALMGWDVWQGQPIEARSYMQEISGFLVRESLAKLTSDESKYLVEYFINYDVDSIEDIYQKRAIKKFIKQFDKITKVPVDLQVEIRNATQQAQLVWEEAYKNSDYELFKPYMFKNFELKTREAEYIDNSRNPFEVLSDSFDEGIDVENVAKLFTELKTAIIPLIKEIAETKLDYEINELTASYDKNLSSKVMLDILKKVGYNTNRSIWGEKMHPVTTGIGPRDARITTNFRNFEGAMFSFLHEMGHGIYNYSANEKAIEYSMWGGIGGAVHESQSRFYEIIVGRSEEFWKYFYPLLQE... | Cofactor: Binds 1 zinc ion per subunit.
Function: Broad specificity carboxypetidase that releases amino acids sequentially from the C-terminus, including neutral, aromatic, polar and basic residues.
EC: 3.4.17.19
Catalytic Activity: Release of a C-terminal amino acid with broad specificity, except for -Pro.
Sequence Le... |
A0A927SZS0 | MKIAAVVSEYNPFTLGHQYHIEQTRAMTNADAVVAIMSGNFVQRGEPAIFDKQIRTRLALEGGADVVLELPTVFALQTAEIFAGGAVGILDSLRSIDYLSFGSETDIAFVGKIAALLADEPYSFKKELSRNLDDKIPFAQARSNAIASYFNMSDAEKAELLLPNSILAIEYIKKLIQLDSDILPVAVHRMGGGYNDDTEYTDYLSATAVRKLIKEKKYGVISQKLPEKIAKMIAAQKTFAEDEDFYRLIQYKLLTSDAEEIAQISGIAEGLENAFKSAAFCKTYAEMIDTVHSKRYTRTAIQRMAFNILLGITKSDVEKC... | Function: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of elongator tRNA(Met), using acetate and ATP as substrates. First activates an acetate ion to form acetyladenylate (Ac-AMP) and then transfers the acetyl group to tRNA to form ac(4)C34.
Catalytic Activity: acetate + ATP + cytidine... |
A0A923UQU2 | MRNIYTLFILAYYTIIRVIALFNTKAKLFVLGRKNVWAQLANFKPNGTETYWFHCASLGEFEQARPIIEALKLKNKLTQVVVTFFSPSGYEVRKNYPLADVVCYLPMDTLHNATQFITAIQPTKVFFIKYEFWFNYIHILHTRNIPTYYVCALFRPNQYFFKWYGKWFANQLKHITNYFTQNTQTAELLTTIGIAQHTVVGDTRYDRVQSIAAQAQPIAIVNQFAQGKKLLVIGSSWSVDEAMWLHIYKNNAELQHNYKLIFAPHNVTTANVDALLELFSNYKVSKYSSYNAGIESNVLIIDNVGMLSSLYSMAHIAYIG... | Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Function: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A.
Catalytic Activity: CMP... |
A0A372LFR6 | MNDCVNALKQGETVILIDDVIKGKEMGYFYLLSEFVTPESINLMVTHARGLVSVTITKEKAKELSLPLLGSLDGNQHKNFTVSIDYEKCTTGISALNEAKQFKH | Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1.
Function: Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
EC: 4.1.99.12
Sequence Length: 104
Sequence Mass (Da): 11533
|
A0A7S3U9P3 | MGTIYDHFSWCGMALETSTFAAIAAAIAPLLVLLKRIQRKKKAVAFFHPFARDGGGGERVLWCAVQAVQAEHPNARVHLYSGDDASAEELQKRALEVFGVEIQRPVHLVRMKLRFLVQAETYPRLTMIGQAVGSILLGLEAILKLTPAVFIDTSGYAFAYPIAKLAGSKVVAYVHYPTISTDMLARVRQRRNMYNNDEGVSGSAWKSGIKVLYYRCFAALYGLVGRCADVTMVNSTWTRNHIAQLWANNGVHIVYPPCDTCKLNNIDLDRPRELEIISIAQFRPEKDHKLQIESFAHALSKVTKTPDMKHLSNMRLRLVG... | Pathway: Protein modification; protein glycosylation.
Function: Required for N-linked oligosaccharide assembly.
Catalytic Activity: alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + 2 GDP-alpha-D-mannose = alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-... |
A0A3D4MW54 | MCSMNDKEHRNLERAGKADTDRILTIPNVLSFFRLALIPVIIVLYAKNEVWWAFGMLVLSGVTDVVDGWVARTYHMVSNFGKAIDPVADKLTQIAVLLCLMPMKCWWVVGILVLKEVSIGIMTLLTLHHTGMVYGAGWYGKLCTAVIYLSMFVLMLWRTAPDWFLYADAALCACLILLAFVKYAIRYGGILREARADGARKQA | Pathway: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
Function: This protein catalyzes the committed step to the synthesis of the acidic phospholipids.
Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + sn-glycerol 3-phosphate = 1,2-diacyl-sn-glycer... |
A0A522JPB5 | MGCRGCRSARPACRAAPDRRWRAGAGAASRRRDVSTAPIRPPPGAHSPVAVLTRPAGQSAWLAGQLAEYGIEPLEFPLLEILPVPDDMPLRAALANLPHYALVCFVSPNAVRHALEKLPCPWPGHVAAAVVGPGSAGALADFGIAAPDVEVFQPPAGPNARFDSDTLLTVLPLARFAGRRVLLVRGDGGRDLLLDRLREAGALVDVVSAYVRRCPTPPGTLWRALDTRLASGRPISLTLTSSEAVGNLDALTRAHFDAAERVRLHRADCFTSHERIAKTARAAGFGRITLCGAGDRNLLQALKSWANPYLAKHADR | 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... |
F8A937 | MSYAVRGMTKDGAFRIFAADTKDIVEEARKIHGTSPTATAVLGRALTAAALLGLDLKTGRVMIQINGGGPIGEVLAEADAQGSVRGLVQKPNIHLTPQKGKLLVGQAVGRDGFISVTRDLGLKEPYQGSTKLISGEIAEDVSYYLTVSEQIPSAVGLGVFVDTDNQVKAAGGFLIQTLPAATDEQIANIEEVLKKLPPVTSLLREEELSPEEILYRIFGRDNVEILEKRPLAYRCRCSRDRVERALIALGPEEIEELIKKNEPARITCDFCNREYIFTVEELEKLLSQIEEKSRRELDA | PTM: Under oxidizing conditions two disulfide bonds are formed involving the reactive cysteines. Under reducing conditions zinc is bound to the reactive cysteines and the protein is inactive.
Function: Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversi... |
A0A316A1W7 | MGGVVSSKISKKLWGEINGEEIYLYSLKNKNGNEAVLSNYGANWVSFFHINTQGVRTDVLLGYDDLEGLQNDQLYMGAIVGRHANRIAKGLCKIGGKDYSFVINNGPNHLHGGIEGFHRKIWATEIVDDRIVFSYESADGEEGYPGNLKVQVSYHLSEDDELEIEYSAVSDKDTIVNMTNHAYFNLNGTGTALDHAIQINADRFTPTDEYSIPTGELQDLENSVMDFRTQKLIRTDLYEEDQQLEFGKGYDHNYVLNKSKDGALELAASAVSLESGRKLSMFTTEPGMQFYSGNWIGGTQGKAGVIYEERDGFCFEAQHF... | Pathway: Carbohydrate metabolism; hexose metabolism.
EC: 5.1.3.3
Catalytic Activity: alpha-D-glucose = beta-D-glucose
Sequence Length: 351
Sequence Mass (Da): 39342
|
G4WE55 | GMISHIISQESSKKETFGALGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLNYSPSMIWALGFVFLFTMGGLTGVVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLFTGLTMNSKFLKIQFLTMFIGVNMTFFPQHFLG | 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-cytoc... |
Q5CXA8 | MTQIIKNQKISRKKSIAISRKNKYKCLIKEIRKSKDFFLNLLQDKNLIYFKTELTKISNRSNLHIARRSDLSSTHMENILKITRDNMKILYDENPWGDIWSQGWDDHLKMNELCHNLSNYIIIYERNTDNATNTIMSTDCSSDISFHNDLRTDINILSFLSFRFELEDEFDSCNKHIIGYMYELQSLVKGKGYGRLLIDLLRFICNELQIYKIICTVLRKNVDAVRFYTKKCGFAIDETSPENEPYIILSTNTSK | Catalytic Activity: acetyl-CoA + N-terminal L-seryl-[histone H2A] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-seryl-[histone H2A]
EC: 2.3.1.257
Subcellular Location: Cytoplasm
Sequence Length: 255
Sequence Mass (Da): 30069
|
A0A970XMB5 | MNFFKLKMLTPENVLFEGNVSSLKVMLNDGGIEILASHIPSIAYLSSGECKIILEDGSKKTFVSHDGILNIERSRVTLSSDFLEWSENLSATIQEKQKRISLEKERRSESFSQHQLGSLDLIKTFIKKNKDENI | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 134
Sequence Mass (Da): 15204
Location Topology: Peripheral membrane protein
|
A0A061ET07 | MTEAVIRNKPGMASVKDMPILQDGPPPGGFAPVRYARRIPNKGPSAMAIFLAAFGAFSYGMYQVGQGNKIRRALKEEKYAARRAILPVLQAEEDERLESRRKCIQFWEMDAPCNWRAAS | Function: Complex I functions in the transfer of electrons from NADH to the respiratory chain. Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 119
Seque... |
A0A8D8AFQ7 | MSNKATKNQQPPAGNTSTKQHQNHQHQHNHSSNSPKKTKNPSTPSSSSTWHISITSLALLSRLFVITLQVISNHLVPDHDAGVFVAPRDPETPPAKLDGAVNFFLGGLHRWDGQYFLHISEYGYSYENTLAFFPLFPFLIKIATSSLGGSTPMITYRELSLVLAVLLNLVCFVLAAKALYKLSNLVLGNKK | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Function: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis.
EC: 2.4.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 191
Sequence Mass (Da): 21066
Location Topology: Multi-pass me... |
A0A7S3XCQ2 | MATCESKDVDEVERRTKAMEKEEERGKAAMEECAKMLEEKAQPKGALGTLETWAKRLAKLQCRAVPQASQFAYACFCADHGLVETQVCTPYPSSVTQKVATALAAGGAGGAVMCATVGRVRHFRVVDVGMLRPANGCDLDTRVACGTKSIVQECAMNAEECAKALDVGRRTIADFVKEEIHAVVLGEVGIGNTTSSSALLAALTRRRPVQVCGRGSGLDDIGVERKAKVVEMALHRHRSIVKSASESPMKVLQALGGLEIAAMVGAVLQAREDSVAVLVDGFIATVAALVAVRVDPRSADCLFLTTRCPEPGHAIALTEL... | Pathway: Nucleoside biosynthesis; alpha-ribazole biosynthesis; alpha-ribazole from 5,6-dimethylbenzimidazole: step 1/2.
EC: 2.4.2.21
Catalytic Activity: 5,6-dimethylbenzimidazole + nicotinate beta-D-ribonucleotide = alpha-ribazole 5'-phosphate + H(+) + nicotinate
Sequence Length: 383
Sequence Mass (Da): 40514
|
A0A7S3UCC3 | MERDVEATPAREDFDPVVFEADEGECRNGSFVKLAKDGAEVLQWMVEPCSLEEFMEECWDQKPLLVKRNLYTDYYRDVFSMEEVDRLLRKVGLDYGLNIDVTSYQGGKRQHFNRNLDDSLEQADPDLVWKRFHDGASLRILHPQRWSNSVWKLLSGLEGYWSCGVGSNVYLTPPGSQGFAPHYDDIDAFILQIDGKKQWKVYTPPTSWEILARESSEDYDESELDDPIFEVELGPGDLLYLPRGVVHQAHCLADTHSLHLTVSCNQHNTFADLLELALPRALEITIEEEVEVRQSLPPGYLDYMGVVHADDVGNPARQVF... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase.
EC: 1.14.11.-
Subcellular Location: Nucleus
Sequence Length: 467
Sequence Mass (Da): 52853
|
C1A6A7 | MHPLLRPLYAGAGALATLIASASTADSAAPQANKLLRTFRARRGVLARWERQAKQHRDPSRPLVWMHAPSVGEGLQARPVAHALREQHPGVQLAYSWFSPSAASFATSIGADFADYLAFDTASAADRMLTALTPSVLVFSKLDIWPVLVERAAARGVPVVLLSGTVAPGSGRRGTLARALTQDAYRALSAVGAIDQANGERLIELGVRTDTLHITGDTRFDQVWQRAQRVDRASPLLTALHSDRPTMVAGSTWPADEAVLLPMWEAVRRAHPAARLIIAPHEPTTSHLTPILTWTRNAALQCATLREVEEGTVDVSTADV... | Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Function: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A.
Catalytic Activity: CMP... |
A0A0K0EE66 | MKKLNYFLKFLTIFSITIYLFYCNRVFFQKTIVKLENISTLERKRVLMYTKYFLTDEIEMFNKCEPINCEFTRDKRLFSKSDAVVFHFADILENDLPTRSFPSQKFIYFSLEAPFSTVDRNPPKNYFNWLMSYNNKSDVIFQYGSKWIKSNGTQKRYNYSYDKIILKKLNKGIVGYISNCFSNSAREIFIKKLEKYIQVNVYGRCLINPITNITCNVSDYKCEKNLIDSYYFFFALENAICNNYITEKYWKRFYFDSIPIVMKRKIYTDVGIPNSSFIAIDDFKSGKEMANYLNYLIKNPIEYLKYFDYRKENITVIPNS... | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 371
Sequence Mass (Da): 44378
Location Topology: Single-pass type II membrane protein
|
A0A3C0PBJ0 | MFFDNLLVNSINNITCYIKNSYYVLLNFAIFIMERINLQIDSKLNCMKKFARISISIFIVLTLVALIFIGGIFVYINTAKSDVRFDKAMLEAQNTNIDIYDIDNNKINDISGKKALVRLDELPSFVPQSFISIEDKDFYKHNGLNYKRIAKAFINNLKSKSLKEGASTISQQLIKNTHLTNEKTITRKINEMALARELEKNFSKDEIMETYLNVIYFGNGAYGLENASQIYFGKPAKELEIEESAMLAGIIKSPRTYSPILNPENALKRRNLVLNEMKKDGAITEEQCNIAASKPIEIKNEISRDISKNFYEEATLLEAE... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-term... |
A0A3C2C4A2 | SYQMDYCNAREALREIRLDLEEGADIVMVKPALAYLDIIRQARDQFNCPLAAYNVSGEYAMVKAAAQRGWLVERAVVLETLTAIKRAGADVILTYHAKEAARWLREERG | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
Function: Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensat... |
A0A8B6BLA3 | MPIQIQEAEGLLSVESEGEGTQDIESVNNPAPECPLEDKENASSDSEEEVIQDHGVDRHLSKTLIYVLRHGASKWGLKVLPGGFVYVDELLSRHPGLSGYTLKELTRLVESVLTQDQGDPGGEERGEIPGSLWFEREDTSLAAVAMASYGEPQGSWDSTEDHSPPRALRSGAVFRVPIKVQGQSLFAVVDTAAEVTLISEGGIQVPKVCAPHPQGSHHEYSRKGDANEWVCCRAREFGTGFQTHTNKSVCGPYRGRHAVGFRLIKGTLHRLANVRWTAAGRRRGHTHDYG | Function: Catalyzes the last step of tRNA splicing, the transfer of the splice junction 2'-phosphate from ligated tRNA to NAD to produce ADP-ribose 1''-2'' cyclic phosphate.
EC: 2.7.1.160
Catalytic Activity: 2'-phospho-[ligated tRNA] + NAD(+) = ADP-alpha-D-ribose 1'',2''-cyclic phosphate + mature tRNA + nicotinamide
Se... |
A0A3G9MC61 | MVVTGDEIRREGPLRRGQTRDALGPVLPQFLSWCGIRTVADTHLRDTSDSFDELFREVRQPDLIVIVGATGGGAADQLRAALDRAEARIVVGRVRCRPGGSQVTALLPDGRVVLGLPGNPYAAVVTLLTTVPSIAAALTGRTPAPRQLARIANASEVSGDATRILPAVPQPDGTWRVDPGIRTAHLAGLIDREALALVPAGAADGDLAELVPLPR | 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: 215
Sequence Mass (Da):... |
I4YGL2 | MVRSAQVERNTGETQIKVNLTIDAVFNKQKQVIDVHTGIGFLDHMYSALAKHGGMSLEMHCKGDLWIDDHHTAEDSALALGTAFKQALGDIKGIKRYGSAYAPLDEALSRAVLDISGRSYCVAELDLKREKIGDLSCEMIPHIFHSFADTAAITLHVDCLRGNNDHHRSESAFKALALAIKDAISYTGSNEIPSTKGVLAGY | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
EC: 4.2.1.19
Catalytic Activity: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
Sequence Length: 202
Sequence Mass (Da): 22012
|
A0A355JFT9 | PLAGPVFAAAVILPPDFPGEGIRDSKKLSEKKREALEAIIKEKALAFSVCAAEVPLIEEVNILNATLIAMKSALAKLTVCPEFVLVDGNRSPGIELSHDCIVGGDDKSLSVAAASILAKVARDRFVKEVLAKEYPQYQFEKHKGYG | Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Length: 146
Sequence Mass (Da): 15676
|
A0A2N6AQB9 | MQRRRKSTLSDNIKSLSHKPKRKSNKIAIISALVLVLAAASFFTYSYITKSFFFDDKAEDEPVIDQVYALDEFVLNLKDSNSRRYLKTKIALGYENKKDVEILAENNFQIRDVIIQTLRMKNAEEIMAAEKTEDLKRELMDDINGLFEPDLVLDIYIIDFLVQ | Function: Controls the rotational direction of flagella during chemotaxis.
Subcellular Location: Cell membrane
Sequence Length: 163
Sequence Mass (Da): 18946
Location Topology: Single-pass membrane protein
|
A0A061E291 | MLTNFQAYEQDSTTNFVILKSNGRAFCAGGDVVAVLGALIIGHWSFGANFYRKQYALDYLLATYEKPLISLINGVVMGGGAGLSMHAKFRIVTENAVFAMPEASIGLFPDVGASYFLSRLPGYFGEYLGLTGARLDGMEMLACGLATHFVLSKDLVLLENELDKVGTSDTTEIARQIERFSCAAPIKRESAYARLDTINKCFSKNTVEDILLALIKKGREQTLEQCLRFEYIVACNILRGSISKDFWEGGRAKLIEKDNKPKWAPSNLQSVSEETVNRYFTEVDDPHWEILRLPDRPNLVDALKSKITENLFLILSHLFA... | Pathway: Amino-acid degradation; L-valine degradation.
Function: Hydrolyzes 3-hydroxyisobutyryl-CoA (HIBYL-CoA), a saline catabolite. Has high activity toward isobutyryl-CoA. Could be an isobutyryl-CoA dehydrogenase that functions in valine catabolism.
EC: 3.1.2.4
Catalytic Activity: 3-hydroxy-2-methylpropanoyl-CoA + H... |
A0A7J3QDN4 | MVYGVCVVDRCISLRGRVFSGVGEGRIYVSLYRDVIRRVLGIEPYPGTLNIALDNT | Pathway: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (CTP route): step 1/1.
EC: 2.7.1.161
Catalytic Activity: CTP + riboflavin = CDP + FMN + H(+)
Sequence Length: 56
Sequence Mass (Da): 6232
|
Q5CT23 | MSTKENVIVYWEKQGNDRMCALHCLNSILQGPYFDEAFLSKIAYEIDDMERRLLEKSNSTFKTISDNNSQNASYDGFFSIMVLQECLQRHGYSCIPAANPRVQDYILYPSSCCGYIINSSEHWTSIRCVKGKWFNLDSLKAAPIHIDYFEVSKYLQEIMFSGKSVFVVQKIQNETDSHSIPLPDPDPFLRPIKNNGKQRFYLTASEIENLVLEKQKEENRVSQMGDETPNKNFMYSKKPVEYSWPTSGGNVLQSTLNNVDQSNEMTSEEKELEKVLRESAIEFAKSIPLPDEPPADHVNSIQIRVRSKVGSSFVRRFDKT... | 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: Nucleus
Sequence Length: 397
Sequence Mass (Da): 45527
|
C1A4L8 | MTVVVRESNETKIRLAIVQGTGRATVNTGEPFLDHMLVAFARYAGVDLDVQATGDLRHHLIEDVAITLGQAVAAFAPAGCARYGERTVPMDDALVQVVLDIGGRPYYRGPLPSKLYDHFLRSFADNAKATLHVRVLRGTDHHHIVEAAIKGLGFALREALVESGAVFSTKGSVKLEITD | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
Catalytic Activity: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
EC: 4.2.1.19
Subcellular Location: Cytoplasm
Sequence Length: 179
Sequence Ma... |
A0A455TZK4 | MASPTWPRLAYSAALYALSPLIGWRIWREQVPTYSRLQRLGIRLEPLPEAPRIWLHCASVGEVRAARPLIEGLLASYPAHSLLITTMTATGAQQSHSIINEQAAADQARLSHRFLPLDFPGAAKRFLRSVQPELAILFETELWPNLIHACRQQGSARGDREWALIAPCL | Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Function: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A.
Catalytic Activity: CMP... |
A0A832AAH6 | MINTIALSQSLAAYTLTFRKLSPDILASLRTKHRDLYRAMCSNGISCVVLSTCLRFEVYIHTEGEDRWNFIEKHLENMLGDYKIYIDKHVGIDAIRYLFEVSSGLHSQIVGEWEILEQVEEALKRSIEFSCSSWLLEKLFRKAVDVGRKVRIQFMGLETHDRGYPQIGIKILSKALGDLNDKRLMFIGSGHAIRRAIRYLMKYYRPSIVVVISEDINKATSICSMYGESCIPLPFSDLVEWLTKIDGIFIAISNLGNEYLSKIRQVVESLKIPVVDISLPPIVKEIHEKIYTFYDIQRYAEEANETTVSCIDKIKKTIDR... | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
EC: 1.2.1.70
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tR... |
A0A8D8AH66 | LEGTGWKVGPSCTDKEYSMVSAIINPPLTIGIIVCRYNSTLTSFGTTENCHLSSAIVVFSVLLLRIIIKICCASMSGAIKKATGLTGMAVAKNPHHTLTALYNKILRAVAKMPQEAAYRRYTEQIVGERAKIVASTSSVKEIEQKVNCGQVEELILQAENELVLARKMLGWKPWEPLVKQAPATQWAWPPAQIHELK | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in 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.
... |
A0A8B6EDZ7 | MGLGFMKYVWKNVNNMEENSTENCTRALRVSQLDAQELDNEVIAIIKNQLTKLLKYHKTNILVRYDPEVSAFLKLLVWKVS | Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Membrane
Sequence Length: 81
Sequence Mass (Da): 9458
Location Topology: Multi-pass membrane protein
|
A0A8B6ERD8 | MSYRPGSDIIVPFGVLTKKKYPNKQLNYTKIFKEKQKDLAWIVSHCKTDSRREDYVKELQKYIQVDIYGGCGTLSCQRRHPFELKDHNRCKSYVSQNYKFYLSFENSLCNNYITEKVYDIFEEGNMMLPVIRGAPNIASFLPEGTFIATSNFTSPKELSAFLSKIGSSEKEYTSYLKKKHSYSVSNWGFNFQIAICDMCTRIKNEKIVNKKLNVYDRLKDDICSKPSDIKYD | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 232
Sequence Mass (Da): 27066
Location Topology: Single-pass type II membrane protein
|
A0A0M8MJQ6 | MSDTARGKAAPAWKTLSVGGMAGLTSCVLLQPMDLLKTRMQQERSPTVSSLSATQRLVRAFRSVVDTSGTLGLWRGTVPTIVRNVPGVAAYFYTLNELRWLVATWQIPVLSSRPGPARTQDSSTMARLSSTGNILTGAVARVSIGLVLNPISIVKARYESSHYAKDAYPTITASLRSLYHDGGFRGFFRGFSATALRDAPYAGLYLAVYEQYKVWLGQWTRAGTGAWWVVGMSGMCAGAIATVLTHPFDILKTRMQTTPKSMLEPHLASAGQRSIWGTTRHILATDGVRAFADGLGLRCARKAASSMIGWSIFELGHRWV... | Function: Mitochondrial glycine transporter that imports glycine into the mitochondrial matrix. Plays an important role in providing glycine for the first enzymatic step in heme biosynthesis, the condensation of glycine with succinyl-CoA to produce 5-aminolevulinate (ALA) in the miochondrial matrix.
Catalytic Activity:... |
A0A8B6FVC1 | MQNYEEVCLKNKEMTQLHIAVFKSESDSSSIKSLMNIVGQYQKRYGGADIEIIYADGTFNRAKALDIGMSRLSEDSLLFFIDVDILFDKFALFRIRYNTIKNIQVYYPIFFSQYNPLLVCTISDSCDINWTNFTSDHGYWRNTSTGMVSTYKRDLKSVGGLNTSFKGWGKEDRALYKTFVESNLTICRSIDPGMIHVFHEVICDTNLKKDQYNMCKGTERNTFGSQRQISHIVFSIPVISKKNDKEIMLRNKRKPDYDCDDSGSKNNQRLHVTLLIDQ | EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 278
Sequence Mass (Da): 32150
Location Topology: Single-pass type II membrane protein
|
A0A871QZ02 | MDDNADDVESYICRRYQKYIAQYTVSPYAQSPLKGSLNRAVFSTFSRFKSQVFYWAVPLCIVYGFWAKARDYNAYLYTKAGREELERVNV | Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrom... |
A0A1V5WD61 | MLQQGQLLQERYRVIALLGQGGMGAVYRAWDTRLNVVVALKEMLSQPGTEPALLARLREQFYQEATILARLSHPYLVRVTDFFLEGPNAYLVMDFVQGESLEAIIKREGALSETQVLTWAEQLLDALEYCHEQGIIHRDIKPQNVIIRPDNRAVLVDFGLVKLWNPADPRTQTIMRGLGTPEYAPPEQYDTQAGHTDPRSDIYSLGATLYHALTGQAPPTATQRIARRAAFQPPRLLNSQISSTTDAAILQALELTVEYRFPSAAAMAQALRQRVPAARPAPPPSPGVTTPYPQPSAVTSSAHGLTQYPPLPPAYGSGGR... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.1
Subcellular Location: Periplasmic flagellum
Sequence Length: 628
Sequence Mass (Da): 67116
|
A0A3C1B1K8 | YPFIDDQSVRLIGAEAAGEGLESGRHAATLSRGTRGVFHGMHSLFLQDDDGQITPVYSISAGLDYPGIGPEHAYLMESGRAEYYAVTDREAVDAFVWLARLEGIIPAIESSHALALLRRMAACGDLTPDKTVVVTLSGRGDKDVAAIQEWQIEHGDIPVKEEKQ | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
EC: 4.2.1.20
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Length: 164
Sequence Mass (Da): 17794
|
A0A4U8YUQ2 | MNEQELIQSVIGKLVEQGVIQGGASSRERGAAPVVSSDSRLSSGDPVTLSPLDEVKVDNPKNMAALEAMRKTTPARILMGRCGARQKTHSFLHFQADHAAAVDAVFLDVSDACLAESGLFGVQTVVKDKDEYLMKPELGKRLSEDAKKMISERCEKGAQVQIIVVDGLSSTAIEANIGDTVPALVQGLKAEGLSVGTPFFVKYGRVGVMDEVGALLGCDVVVELVGERPGLITAESMSAYMVYKAGEKTVEADRTIISNIHRGGTPPAEAGAHMATVVKQMLAHKASGVALSEAMKA | Cofactor: Binds between the large and small subunits.
Pathway: Amine and polyamine degradation; ethanolamine degradation.
Function: Catalyzes the deamination of various vicinal amino-alcohols to oxo compounds. Allows this organism to utilize ethanolamine as the sole source of nitrogen and carbon in the presence of exte... |
A0A0K0E8I2 | MITKFFSKNITYIKHISPLEDNIVIEPSMLKYKTYYYISRHYKLILKHIFDELNYEAVIILEDDLDVSEDFFSYFNATYHKLLKKDKSLYCISAWNDNGLPELINLNFYIGLYRTDFFPGLGWLMSKNLWDEIGSQWPTGFWDDWIRKPEQRKDRMCIRPEISRTSMTKFGAVGASKGYFFNAFLSRIKLNEIYVDFNNLDMSYLLEDNYEKYYMNMVYNISKLVSFNNLPHYINQSISQENHLLRIEYTTFKEYQSITKLLNVMRDFKEGVGRTAYKGIITTYKNGLRIFIAPNKNNWKGYNRSWEYIP | Cofactor: The cofactor is mostly bound to the substrate.
Pathway: Protein modification; protein glycosylation.
Function: Initiates complex N-linked carbohydrate formation. Essential for the conversion of high-mannose to hybrid and complex N-glycans.
EC: 2.4.1.101
Subcellular Location: Golgi apparatus membrane
Catalytic... |
Q5CXC9 | MGIQGLLPNVDNISIKSKIDFFKGKRVAIDTYGWLHRSAANCAESIVLGKPTRVHINYCIEKIRTLQGKGLIPVCVFDGATLPMKRVTEEERSKRRSDAKREIIRLKSEKKSYSSYNMRSLCQKALDITPNIAHQVLEVLRDEYKIECIVAPYEADAQLSYLSRIKYIDAVITEDSDMLVFGSICTIYKYDDKTGNCRVIYWKDLYKSGVISQLMFSYETFVLGCILTGCDYVKSPQGVGIKTAMKLVQECNADLERIILQLKDLGKDIPQSYAIDVQNAMITFFHQTVYDPIEGNMVPLSNSDRPKSEIETNVTLDNVP... | Cofactor: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.
Function: 5'->3' double-stranded DNA exonuclease which may also possess a cryptic 3'->5' double-stranded DNA exonuclease activity. Function... |
A0A3G2SW34 | WGGMIGTGLSMIIRLELGQPGSFIQDDQIYNVVVTAHAFIMIFFMGMPVLIGGFGNWLVPLMLGAPDMAFPRLNNMSFWFLMPALTLLLLSSMIETGAGTGWTVYPPLSSNLAHSGMSVDFAIFSLHLAGISSLLGAVNFISTIFNLRSYGMILDLTPLFSWAVLVTAVLLLLSLP | 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-cytoc... |
A0A0M8MZ65 | MRMRTMSMSMNEHWKEQLAWEKGGEDLKSVCGEDSFLGESGVCLPLMLSPPPPVPSEADMRRAVELDVSHQLSLLPVIDKETVQFFGKWPHLRVLGMQEPMSVVFSLMNLAVQVHAIQYVFRDLLPSTFPLRSVYLTHAKIASVAWCASSVFHTRDLWWTERFDYFSAAAVLVSGFFLAMCRILSIRPGTPLYYRIRAGCILAWVLHVLYLLSRWRLDYSYNMAACLVLGVMHNVFWLLYAHMPNLCLRLRASLGSMDSVNASIPLAPTKGSSSERPSPAMLTPQPMKLSNPQRRRLELLILAMFAAPALELFDFPPLFR... | Function: Involved in the lipid remodeling steps of GPI-anchor maturation.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 451
Sequence Mass (Da): 50569
Location Topology: Multi-pass membrane protein
|
A0A0M9VQ42 | MVRRAKGRSAPASAPKVPPSEQVLQPRDAGRWPIWHILQLVFFTMFLQPALLTLTLIDLARYVDASSFLGGLLHKISLILRPGDRLADRSAERLAWDMVLAVQGTALTQAWYCMRMHSWCHRAEGHERREPPSELKKRSLAVHTQIEGVVFSSFSLPLLWLLASVALVLVGAPLHTGYLGTATLAGYLALLGLWPMAHIFGAPPSPVWTRWLAAPSTALPREILVIVPCLCAWLGAGLSAAVLALDWGRAWQAWPVPCVYGAAVGVVIGHALALGLCIAQVYRDLRKSVHD | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 291
Sequence Mass (Da): 31859
Location Topology: Multi-pass membrane protein
|
A0A358AUS0 | MKKQLNVEILSNEEIAENTYLLKIPCPEDVLKFFRPGQFAHIGIPGAGELLLRRPLSINSVDYEKKEAHIAYHAAGKGTTILRDAKAGSTLDVLMPLGNGFAVKPAMRKIWLVGGGIGCAPLKSVFGKYADREYKAFLGFQCKSAVYQESDFKKYADVNISTDDGSYGTHGFITDVLREALETAQPDVILACGPLPFFRALVKVTRDVPVQVSMEQHMGCGTGGCAVCVCSVGGENRRVCVEGPVFDSREVDVLW | Cofactor: Binds 1 FAD per subunit.
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (NAD(+) route): step 1/1.
Function: Responsible for channeling the electrons from the oxidation of dihydroorotate from the FMN redox center in the PyrD type B subunit to the ultimate ... |
A0A8B6DZE7 | MSDIFNDNGIATADDTIDFDTKSNELCNSFPCFANYFEIRLKNRLFNYVNQPFANMILTDSGQTITVYLLTKHVLFFQLSYGFVVVAMSVVCCNNFRKYREARNIFIVATVTYAFGFFLWEIDQNFCGGLKLWRSEVLGPFAPIFELHAWWHLLAGTGTYLSVLYSAYLRSLVLGNKPEIKYWKKVWPYIRITNGKALT | Function: Hydrolyzes the sphingolipid ceramide into sphingosine and free fatty acid.
EC: 3.5.1.-
Subcellular Location: Membrane
Sequence Length: 199
Sequence Mass (Da): 23035
Location Topology: Multi-pass membrane protein
|
A0A239QM07 | MAVDKHLFLIGMQGCGKSSLGKRTAKETGVPFADTDAMVAQSAGGTVNEFFEKYGEETFRRAETNALAALTYARPMIISTGGGTVLNPVNRHIMRSWGTIVLIDRPLEDILSDIKLDRRPTLRDGGLAEVERVYHERLPIYRDLADITLRNDQGYHMAVYILTRLVRERL | 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
S... |
A0A8B6FCT7 | MRIIVCDILSRLRTSVKLTRSYCTTQTYVGCKSDEAPCKRLFNQKLFPEGISDYVTSEVLKFSPSIPVEEAITPPASWYSQPQFHTLDKASVFRKHWIPVGRVDQLKEPGQYIAGFITDDPYLVTRDETGKLQAFYNICRHHATLLVDDNSGTVSKFQCPYHGWTYTLSGRLAKATRLRGIKNFNAKNFGLIPLEVTTWGPLVFIKLSTDDTNSSDDLGVQLKEVKTRLDKMGLDNLRFVERRHYRVKCNWKVFIDNYLDGGYHVEYAHKDLAGLIEPKDYKTAVFDGFSIQSSSGNKGEKEGQDRIGSAVLFSHVYPNL... | Pathway: Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine aldehyde from choline (monooxygenase route): step 1/1.
Function: Catalyzes the first step of the osmoprotectant glycine betaine synthesis.
EC: 1.14.15.7
Catalytic Activity: choline + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin... |
A0A8B6EFC9 | MVSPWKIGYCVVCVGIIVYGIWDYLSNFEKNKCLMTYMFEMPEYIQIPLGKRLKEKYPRYRLFIYGEGQYARKLESNRKVPVNGVPVLFIPGNAGSYRQARSLASVAHRRANDKRYSFHFNYYTIDFNEELSALFGGMLQSQTEFVHECVKKILSLYEYNKPSSVVLVGHSMGGMIARALFTLPEFEQSFVNTIITQATPHQAPGQLLS | Function: Involved in inositol deacylation of GPI-anchored proteins which plays important roles in the quality control and ER-associated degradation of GPI-anchored proteins.
EC: 3.1.-.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 209
Sequence Mass (Da): 24009
Location Topology: Multi-pass mem... |
A0A7C6FKJ4 | MQRTNRTVDLTFAALMTALAIVLSYFPEIPLAFFAPWLKLDFSFTPLLLLGFSVGPGMMVIALLVTNLVHILGGTTGGPGELANMIMGLAFLLPPTLMYHKNKSRKNALIGMLIGTVMMVIAGVIANRYILLPVFFRGNLEEEMAKRGMSMNGYLLGAVVPFNLIKGAINSLMVFGLYKRLSMLMKEAKDDDTPAVK | Function: Probably a riboflavin-binding protein that interacts with the energy-coupling factor (ECF) ABC-transporter complex.
Subcellular Location: Cell membrane
Sequence Length: 197
Sequence Mass (Da): 21546
Location Topology: Multi-pass membrane protein
|
A0A8D8CYD0 | MNLRASRVIFNQIRCYCYKPVRRVSLPPASKRAPKASASVDNFSLQNEFKSRILATGPIPVAAYMKQVLTNPAGGYYMNEADVFGSKGDFVTSPEIGQIFGELVAAWCLNEWTKFGKPTPYQLIELGPGKGTMMRDILRVFKRLGASEGLSVHLVDMSEHLSEVQAELLCRSSEECADKAYYRAGVTRAGTKVFWYRHLEDVPAGFSIVLAHEFF | Function: Arginine methyltransferase involved in the assembly or stability of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I).
Catalytic Activity: L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) + N(omega),N(omega)'-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-homocysteine
EC: 2.1.1.320
Subce... |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.