ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A7C1BA35 | MELTKTAEVVLKKRYLLKDDKGNVIETPEQMLWRVANAIAKAEEKYGNDVKKIAKQFFDMMDKQLFMPNSPTLMNAGTELNQLSACFVIPVEDSIDGIFKALWDMAKVQKSGGGTGFAFSKLRPKGDIVKSTMGVASGPVSFMKIFDAATEQIK | Pathway: Genetic information processing; DNA replication.
Function: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
EC: 1.17.4.1
Catalytic Activity: [thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [... |
A0A2G6IF02 | MKICRTIPEFRAALSGLRGEGKTLGLVPTMGALHDGHMALVEAAKAECDAVAATIFVNPTQFGDPADLETYPRTEAEDLALLKARGVAAVLIPEVGDIYPEGDETIVETTRLANMLHGEVRPGHYRGVCTVVTKLFNIAQPDAAFFGEKDYQQLQVIRRMARDLHMPIAIHGVPTQREDDGLARSSRNRRLTPEDRAAAPVLSRALAAAEEAVASGTTVEDLRTLIANTITAEPRATMRAIDIVAPGTLAPVEGPVKAPIAIMLSAEFGGILLIDQREIGVTH | Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-... |
A0A2N9D122 | MPDDSVRAATYVLPRPSFRAPRVRSDMLNFSDTAIYGAPIVLADLAAWRLFGRGRSAARAIRRCAAFAALTAVLFATGVSPLAVPASLAWLDRIAVQAICIAWWLQCAIVFSLLLNHLLLPRAWRNQRLFHDLAEAIVFGAAAVAALGYVLGLPLSGLVATSGAVAVILGLALQNTLNDVFSGLVLNTTQPFRLDDTVSIGELEGRIVESNWRATKLIDSLGNLVVVPNSTAARATIVNLSEPAGLHGVTLALDLDPAVRPAVAVGALERAAASSLDVLARPAPIAVVKAFRANAIQYELVCYVDALQKKITVRNALYDL... | Function: Mechanosensitive channel that participates in the regulation of osmotic pressure changes within the cell, opening in response to stretch forces in the membrane lipid bilayer, without the need for other proteins. Contributes to normal resistance to hypoosmotic shock. Forms an ion channel of 1.0 nanosiemens con... |
W6MY17 | MTLLAAAGIFLVLDVNSPLENSHINRYEPWNSYNKEYLTRIFKVVEQFSGYNNTLAFFAGNEVINDEKSALVSPKFVKAVVRDLKSYIEYNKLRKIPVGYSAADDLNYRVSLAKYLECSNGDSSDSIDFYGVNSYQWCGKQSFHTSGYSILSINSAPRFGCNEVQPRLFEEIQAIYSETMAQVFCGGLVYEYSQEPNNYGLVNVNSDGAVKLRQDFITLKDQLADTPDPDLPKQSRIKSFRQNSASAIPFCKDFYQGLGVTTSLPASPAESIIRQGVAGQKGSFVPLLESDLESHFQVLSQDGSNYGKQVKVSLVPRPNH... | Function: Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall.
EC: 2.4.1.-
Subcellular Locatio... |
A0A191ZF24 | MSEPDDKHPHTGKNRLSRIVTRTGDAGTSGLADGSRLSKTHPRMQALGDIDECNAQIGLLRAVIDQHPVANEGFTKLDPFLADQQHALFDLGGYLAMGSMATPMQLPSLEQLEEWIRQANTDLPPLKEFILPGGSPSLAQAHVVRVTIRRAERTVWHLVESSADSEADLIVPVAVYLNRLSDALFVLARLLGLWENSVVYWRKKVSPTA | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 2/7.
EC: 2.5.1.17
Catalytic Activity: 2 ATP + 2 cob(II)alamin + reduced [electron-transfer flavoprotein] = 2 adenosylcob(III)alamin + 3 H(+) + oxidized [electron-transfer flavoprotein] + 2 triphosphat... |
A0A940F989 | MSGGVRVRVPASTANLGPGFDVLACALDLWLELEVQPAPTFSFTTDLPVPMDPTNIAVDAFGRLGDPARVAFTMRSQIPLSGGMGSSAAARVAGVLAALVMGGEEPKDALELALAIAAELEGHADNAAAAIYGGVTVELPDGPLKLAVPQRLGFVIVAPHEAVDTPAARAALPAAVPMADAAFNVGQATALAAGLASRDLDLIARGLGDRLHQPHRAPLYPRSMELIASARELGALGGTVSGAGPTVLLWCDRDAVRDVEREAGIWSAGWADTLAVDPSERGAQIERL | Pathway: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 4/5.
Function: Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
Catalytic Activity: ATP + L-homoserine = ADP + H(+) + O-phospho-L-homoserine
EC: 2.7.1.39
Subcellular Location: Cytoplasm
S... |
A0A0G0WU26 | MNLKNIRNFSIIAHIDHGKSTLADRMLEITHTVEARKMRDQVLDSMELERERGITIKMQPVRMEYTPSQPSPKGKGQAPSLWGRAGDEVYVLNLIDTPGHVDFSYEVSRALKAVEGSILLVDSTQGVQAQTLTVLSAARGEGQEEAKKIISVITKIDSPLARISEVKEEVIKLLNCRADEILEISGRTGEGVENLLKEIIQRVPPPRTSQSEVRPTNPSDLFRPQDILQALVFDFKYSNHRGVIVFVRVFHGEIKKGDNLIFAVSGEKFIALEVGTFSPEETARENLSGGEIGYIVTGIKKPGIASVGDTVTKYQNPSKA... | Function: Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex ... |
A0A940J7B1 | MAGDESTIASSDRAEGFSDAIFAITITLLVVEIPRPPIDEPHLGRHLLDAWPEYAAFGVSFVYIGALWLNHHALFARIGRVDLRLHWINLFILGTSALLPFSTAVLAGAFSADAPTSNQEAAVALYALVALLTSAAWIPVFPHLSRHPELLANPEEGDLIAAQSSRPWVGVASYGAAGISGWLVSPIVALALFVWMIAYHAVTSEGLHANRVARWLTPPGRARRAIARRHAE | Catalytic Activity: K(+)(in) = K(+)(out)
Subcellular Location: Membrane
Sequence Length: 232
Sequence Mass (Da): 25051
Location Topology: Multi-pass membrane protein
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H8MI59 | MQAEAPGAMHVAFADLIDLAARKVGGKALLANDEFFAPKESMLEPGRGVFIADKYTERGKWMDGWETRRKRVPGYDWCIVKLGLPGAIHGIDVDTNHFLGNFPEYASLDACEVDGDPSPESLAEDVSRWTELVPKQRLRGGSRNLFAVANERRFTHVRLNIYPDGGVARLRVHGQVLPDWHALKKAGLVDLAAAANGGSVVTCNDQFFGTKDNLIFPGRAANMGEGWETRRKRVPGFDWIVVKLATAGTLRRAEVDTHFFKGNFPDRCSLEGIHLEEPLLDFANATHLQWKELLPQSKLQADHCHVFEKELKDVGPITHV... | Pathway: Nitrogen metabolism; (S)-allantoin degradation; (S)-ureidoglycolate from allantoate (aminidohydrolase route): step 1/1.
EC: 3.5.3.4
Catalytic Activity: allantoate + H2O = (S)-ureidoglycolate + urea
Sequence Length: 340
Sequence Mass (Da): 37798
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A0A976E3F4 | MQSGERDRVTQTRPANRGWPRLVGHRRGAERVREIVQACPDLGIRWLTLYAFSTENWKRSTEEVLGLMAIFARYIEREADRLAAAGVRMRFIGERSRFDPKLQRLMAGIEARTAGYDRLNLTVAVNYGGRDEILRAARKVAEAAALGLLDPNHLTEAAFSERLDTGGLPDPDLVVRTSGETRTSNFLPWQAAYAEYEFTATLWPDFTAEEMAAIIARFSNRERRFGAAKA | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
EC: 2.5.1.-
Sequence Length: 230
Sequence Mass (Da): 25963
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A0A2S6QEI1 | MIRFTLCMIVSLAGIVAAAVWFSDRPGMVSIVWQGWLVELTVGRFVLATAFLLFVLVFIVGIVRALGRTPRRLREWHRASRRERGYRALTHGMVAVAAGDPGEANRQARRADILLNEPPLTMLLSAQAAQLNGDEAAAARYFKNMLDRPETAFLGVRGLLIQAQKKNDRYAALQYAERAYELQPKTPWVLTTMFDLQVAEGRWRAALTTLEETVKRRLLPADTARVRRTTVLLGCSLEAEDNGDLPEALRFARQGNTLTPEFLPAALRTVDLMVRNGKTGHAARIIQNAWAYTPHPVLARIYGEIGIAGEDQLKIVKRYE... | Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis.
Function: Involved in a late step of protoheme IX synthesis.
Subcellular Location: Cell inner membrane
Sequence Length: 471
Sequence Mass (Da): 52014
Location Topology: Multi-pass membrane protein
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A0A8C4XF26 | MSYSAKIGPSILNSDLACLASECTRMLECGADYLHLDVMDGHFVPNITFGHPVVECLRKHLGQAPFFDMHMMVSRPEQWVKPMAAAGATQYTFHLEATSNAGALIKDIRESSMKVGLAIKPGTTVEELAPWASQIDMALVMTVEPGFGGQKFMEDMMPKVSWLRTQFPSLDIEVDGGVGPDSIHKCAEAGANMIVSGSAIMSSDDPRSVINFLRNACMEAIQKRSLDR | Cofactor: Binds 1 divalent metal cation per subunit.
EC: 5.1.3.1
Catalytic Activity: D-ribulose 5-phosphate = D-xylulose 5-phosphate
Sequence Length: 228
Sequence Mass (Da): 24870
|
H6Q5A6 | MIPLYLKDISCILNVPYIGKNCKIHTISIDSRTIKKNQKCIFVTIQGKKNNSEIFIHEAIKNGAIAILNTRLLPIDMPQIIVRNTIEALRKIAKWLRNKINVKIVAITGSCGKTSVKEMVFKILNICEKTLATKKNFNNTLGVLLTLLELKKEHKFAVIEVGGSRFNEIQHSSYLIRPNLILINNIVESHLLGFRSLYGVSQAKGEIFSGMLNDSMILLNSDSHNWSLWKNKIKNQSVFWFGLKKCQKNFFHLIDIIQKNLITKIRLNTPTGTLNIKLNTIGNHNISNAIAASILSYLLGVNLCTIAFGLKNFFSFPGRL... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein.
Catalytic Activity: ATP + D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-d... |
Q1D497 | MAPAALTLGARRFEWGSRTYVMGVVNVTPDSFSDGGRHAGTDAAIAHGLALAESGADLLDVGGESTRPGSLPVSADEELARVIPVIEGLRARTDVPLSVDTTKAAVAREALKAGAHLINDITGFSSDAGLSRVVAEAGAACCLMHIQGTPATMQQAPRYDDVVEDVLAFLEAAILRAESAGIPRGRILLDPGIGFGKTFEHNLFLLRRLPELRVLGLPLLVGTSRKGFLGRLAGGKPASERLAATLGSVASMAALGGADVARVHDVTEARDALAVADAIRRCEDGGTFYAR | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2.
Function: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7... |
A0A3N4ZG15 | MTNFAGAVPGPDGRPLDQIRITGVNGRGRHGVLASERATGQEFRADVVLHVDTRAAAEGDDLRATVSYADVAQEAHDVLVGEPVDLIETLAERIAAAALGHEPVRAVDVTVHKPQAPIPVSFTDVEVSIRRDRVAVPPVVGAAAFAAEASPVDRWAAEAADPHAAAGEFAQPERAESVEPTTADRPAAPAVDPLTAPIADLTAGDAAPGAEPAGWSAEAAADTPVSGENLVIPEITPADPVGAVEGHDRHQNGFEHAGAPAADQAAPVAEAVEPQPQDAGMIDGVPSVEHGVPAFEPHADAPARPVEDEAIARRPAYDPA... | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4.
Function: Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin.
Catalytic Activity: 7,8-dihydroneopterin = ... |
A0A1E4SQ08 | MALAVVPVLAASTSKQEMQQLQPPLSTQEIQYLQKDPLITHKVTFTVAQRTENGDQELGDLTMGMFGTVVPKTVENFVQLANMTFGYGYKNSILHRIISGFMIQGGDFERGVGTGGHSIYPSGKFIDENFELSHNKMGRISMANSGPNTNGAQFFITNIEDNTRLDGVHVVFGQLIGGFDALHKISSVKTGAMDRPVEEVYIKDVSVVTLSKGGKDLLRFDLVPVNIEVDDAGSNFYMYFFGLLLLAGCFFFYNHWYHKKQYITDIKDSAYF | 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: 272
Sequence Mass (Da): 30298
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N1R5R2 | MAFVPIKNAVQVMGTSIFLLVVRKKLQNDFRFVHVQKRMNLQGAAYFVVANAMACVYSAVALAACRSRSAVAPLMVGDLVVQALLFSAVGAAAEFGILGERGNSHVRWGKVCHVYSSFCERAMAAVIVSLVAAFANLVHLMFAILDVHKNSSYY | Function: Regulates membrane-cell wall junctions and localized cell wall deposition. Required for establishment of the Casparian strip membrane domain (CSD) and the subsequent formation of Casparian strips, a cell wall modification of the root endodermis that determines an apoplastic barrier between the intraorganismal... |
A0A449B730 | MNLIVFYSIVANLSALLLGYLWGSLNTSIILSKKYKNDDVRNHYSKNAGATNSLRAFGKKFAFVVLIIDIAKTVLAVYSAYFISYAWQSNYSQIVFFPILAGVGTVFGHVFPVFFDFKGGKAVACSVGLLISINITLFFIAALIFFGSLYLKKMVSLSSILTATVMIALMYVPWIVTGILAVTAGQNNPYWWINSLIATVSLILLIISHHSNIKRLLKGQESKIK | Pathway: Lipid metabolism; phospholipid metabolism.
Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl pho... |
F2JJY8 | MKIEKVAIIGIGAIGAFMASKLSSVLSNGKLVVIAEGERKARLEKGLLINSKSYQFQIVTPEEKSEPADLVMIATKYQGLDAATKAIKNQVGKHTVIMSLLNGVNSEEKLQEVYGDKVIYALMRLSSIRTDEGISFNERNGYIEFGEERNDVLSERILAIKTLFETAGIQYKIPLDMRKALWHKYACNVAENQSSAILGIPFGAWQVSETANHLREAAMREVFAVAAKKGIIFTEEELLAQRELLSHVPYGNKTSMLQDIENKRATEVEMFAGEMIAMGKEVGVPTPINEVFYDAIKILEEKNKGLI | Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 2/2.
Function: Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
EC: 1.1.1.169
Catalytic Activity: (R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH
Sequence Length: 307
Sequen... |
C6XC01 | MEFPTSFVHKYSKAAPRYTSYPTALHFHTGFDAAAWQHELQASRDSGRDISLYAHIPFCDTLCYYCGCNMVATRDYSKAERYLEVLLQEMALVADTASADRLVRQMHWGGGTPTYLKPDDLVKLHQAFARRFRMADDAEIGCEMDPRELTRAHVDALASCGFNRLSLGVQDLDTQVQEAINRIQSQDLIEQVYGWIRDAGINSINFDLIIGLPHQTPERFARTLDAVIAMAPDRLAVFNYAHVPWMKKHQRLIPEAALPTLDQRLELLRMTLDRLTAAGYVHIGMDHYAKPEDELVRAQQQGSLYRNFQGYTTHKDCDIL... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrinogen-IX from coproporphyrinogen-III (AdoMet route): step 1/1.
Catalytic Activity: coproporphyrinog... |
A0A1I5QJL5 | MIDYSFSYGDLEIFLLVVVRVTSFIFVCPFFGGRQTPNLVKIGFGILLSILIYGAVPFNPPDYVTTIEYTIIVLKEVMAGFLLGYAVQLSTLIVNFAGMIVDMQIGLSMVNLFDPNTNEQSTITGTFYAQVLTIMLIISGMYHFILKALADSFSLIPINGIVINSDRMLNAVVAFLRDYIVIGFRIALPIFIITFITNVVLGILAKVSPQMNMFSVGIQIKIVIGLAIMLITVTMLDNAANFIYVNIKELMNEFVYSMQSS | Function: Role in flagellar biosynthesis.
Subcellular Location: Cell membrane
Sequence Length: 261
Sequence Mass (Da): 28972
Location Topology: Multi-pass membrane protein
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A0A923ZS91 | MFKISKRPTIQEIHALYQTKKATPIQVVQFFYNRIKETNPKLNSFLRLTEDLASQQANNCQDILESGQTFESIIKQYPLFGIPYGIKDIILIEGLEFTSASNILKGYIAPYSSTVYNRINQSMGIVMGINNMDQFAMGSSGESSAYGTTKNPFDLTRTAGGSSSGGAASVASGQVVFSLGSDTGGSIRQPASFCDVVGLKPTYGLVSRWGVMPMASSFDQVGPFTNTVYDNLLVTRVLAGIDTNDQTTIESVDLIDQLEVIINKQNISHRHSTAVTKSIHPMRIGIPKEFYQPEGVDPSIYESLQDLLLQLKELGHKLIE... | Function: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
EC: 6.3.5.7
Catalytic Activity: AT... |
A0A1F3D4G9 | MNRAMSTIIDFPPQLDIQQNVPLSHFTNIKIGGPADYLSVIKDQNIYIELFRFCREIGLPFLALGDGTNVFFPETGYHGIVAIIKFDSVGLMSKNTIVAEAGTSLNKIRELCIETGLTGFEFASGIPGSIGGAIYGNAGAYGSNVGEILTRAKVLTPDGQIRFVKNDFFKFSYRHSDLKINPAIVLQAEFQLKKGDPAAIKSRCDEIINIRTKKLPPSDTLTAGSWFKNIKDEQGNSTAAAQYLEAVGSRQTSVGDAAVHIRHANIFYNKGKATATDMLKLEDILQKRVYKKFGIRLEREVMYLD | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
EC: 1.3.1.98
Subcellular Location: Cytoplasm
Sequence Length: 305
Sequence Mass (Da): 33664
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A0A1F3DHZ9 | MKKKSNLSERSVDADPFRQFKKWYADRLKTEIYYPDSVTLATSTADGHVSARTVLLKDFSDNGFVFFTNYNSKKGQQLSQNPGAAMLFYWPESGRQVRIEGVVEKVSAEESEAYFRTRPRESQIGAWASEQSAVIPGRAHLEKRVEFHIKKFSDNPVPKPYSWGGFLLIPEWIEFWQEGEFRLHDRIIYTRNVNQWKIERLAP | Cofactor: Binds 1 FMN per subunit.
Pathway: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
EC: 1.4.3.5
Ca... |
A0A010ZIV3 | MMSWVDIRRFDPLDKNACRTQRYQVSLAPGMSVLNLLEQIYSEQDETLAYSRCCRAGVCGLCAVMVNGEPRLACRTAASPEMLLEPLRGFPVRKDLLIDREAYEAHRSRLHLYLERQSCRGARAEALEPVAREDFERFKIPSRCVECYCCVAACPAYKAHPDTFLGPCSLVLLARHSFDPRDTMDRRPLALEAGISRCINCKKCDAVCPMGISPSSVIAALKQQIEEEHHDL | Cofactor: Binds 1 [2Fe-2S] cluster.
EC: 1.3.5.1
Catalytic Activity: a menaquinone + succinate = a menaquinol + fumarate
Sequence Length: 232
Sequence Mass (Da): 26167
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A0A1I5U3B9 | MKDTIKIIPLGGFDKIGMNMTIIESDESIIIVDCGTSFPPNDMPGIDTSIPDISYLKEHKEKVKGIVVTHGHEDHIGAIPYVLPELDIPIYGTPLTILLIEDKLKRYNINKPKTKVIRQGNTFILGDFKIEFIKTNHSIPDAVMLAIYTVAGIIVCTGDFKIDLTPTIGDTTDLRRLAAIGSKGVLAVLSDSTNALIKGSSPSENEVSISMDRLFNNYKNERLIIATFASNMDRVSQIIDISKKYGRKVILQGDVMLEIFKSAEKLGYISLQNDVLIEPDEASCYKDSELVFLTTGNHGEPISCLSDIANGLNENIKIKE... | Function: An RNase that has 5'-3' exonuclease and possibly endonuclease activity. Involved in maturation of rRNA and in some organisms also mRNA maturation and/or decay.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 550
Sequence Mass (Da): 60593
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A0A2H6FXU8 | MKKIYLDNTPLSEAIEKWTDKVRASGGKLPQAETVGVIDSLRRITAEAVFAKVSSPFYHSSAMDGYAVKFTDTVGASERTPKRLKVPEQAVYASTGDPLPDNYNAVVMIEDVNIIKLPKNSQSSVGSRQSQETTENPDIVVPPYGAGGQLTNDNTYIEIIKPVTPWQHVRTVGEDIVTAELILPENHRIRPVDIGVMLAGGFTEIKVREKPKVVIIPTGNELVEPGSELTKGNIIESNSRILSALVTEWGGEPVRWKIVPDRIEDLKKALVEASRAADVVVINAGASAGKKDFTSAVIAELGEITLHGVNIRPGKPVILG... | 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: 691
Sequence Mass (Da):... |
A0A8C4SGN0 | MGLEKERSDTRIIMNDDEFNRSFEPILPKKEKEVAAPDRDPHDINSHIKVNFEDVIAEPEGTHSFDKVWVCSHAVFELVKYLLYAFLTTVLAIPLSFVAGIYFAVISAIHIWIVMPCIKSCLMALPPFKAIWKSLVDMFISPFFESMGKCLSSFKINKMQD | Function: May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity.
Subcellular Location: Cell membrane
Sequence Length: 161
Sequence Mass (Da): 18433
Location Topology: Peripheral membrane protein
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A0A3C2D146 | MFFWVPNTITALNLVCGSLSVFFAIDGQLGLAAVFIFAAAIFDFLDGFSARLLNAYSSIGKELDSLADTVSFGLAPAAIIFTMLELTLFGKNQHIQDIEANLSQWIFLLSSLVIPIAGAFRLAKFNTDDRQSDQFLGMPIPANAIFFASLALVLVLGDRTIIEPIILNKYTLLASIFSCSFLMVSELPMFNLKFKNLKLKENGLRYLFIAITILMLILLQVYALPLIIIWYVLLSGISYLAGSK | Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + L-serine = a 1,2-diacyl-sn-glycero-3-phospho-L-serine + CMP + H(+)
EC: 2.7.8.8
Subcellular Location: Membrane
Sequence Length: 244
Sequence Mass (Da): 26955
Location Topology: Multi-pass membrane protein
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A0A914C7K4 | MAQALIIVNALNHAFHEDPNVGLVIIKGNHKAFCAGGDVVDLTSAFASGKIDHNKIFIQLMHTVHSFSKPYVAIIDGITMGGGCGLALNGEKFIIATERTMVAMPETYIGYFPDSGAAHFFKGKLGMFLGLTGFRLKGADVFHTGLATHFVSSNDLPILERHLLSLSTNEASKEKIQEILSKFHLKNLPPHTLQPHLEEIEKHFSKNSIEDIMDSLKNSNSEFSEKIYSDLQKLAPTALKVTFQHIRNAPQSTFHELLTIENRLTQRFLRNHDFREGTRALLIDKDKNPKWKPSTLEEVSQEMVDSYFQPLEIPEFEWFL... | 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. Also hydrolyzes 3-hydroxypropanoyl-CoA.
EC: 3.1.2.4
Catalytic Activ... |
A0A914C2V5 | MGQIADILAKAGHDVVVYQPIYDLNINTTGTQFARVITRPRNFDGPGTVAALQSKIWTTENPKLDKFAELALTTSTCHQILCKNQLDDENLMLQLRKENFDVALGEAFDACYYGVLERIGLSNYITMSSGVMNDFHYGYFGIPPSPSYLPGCDKIRCYERKTGKHDTRGYIDTTVSNKRKTSFTNSYD | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 188
Sequence Mass (Da): 21143
Location Topology: Single-pass membrane protein
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A0A7W5B597 | MNVRMAIVIGGALGALSRYGLSRLFPYHLHGAWPWATFICNITGSFALGLLFAAVVRYGLSSIWREAIGTGFIGAYTTFSAFSLEVFQLFRDGAIGVALMYSAGSMLMAAVAAAVGPVLLPPRMKEEA | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 128
Sequence Mass (Da): 13638
Location Topology: Multi-pass membrane protein
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A0A5C8IEN7 | MTTTRPSRPNPPPDPDPSATADETRRGPAARVVVRRIFAAETPEYFLLLGTTLFLVVFGLVMVLSSSSIESWVSDGDFFARASRQAILALIGVPLMLIAARAPRSFWRRWAWHLIIGALVLQAVVVVVGAGQSLYNNNWLYIGGFSLQPSELIKLGFVVWLALVVTRVAPIINDWRRADWREYALPLAPAVAGIMLVMLGNDLGTTVILAAMVLGSLYFGGVRLSIVSLITIVGSLGAAIAVQASDSRSERFAVWFEGCTDIASRYCYQTLQGWQALGDGGIFGVGLGNSTAKWSWLPEAETDFIFAVIGEELGLIGALL... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-... |
A0A3D1CTC0 | MLARIQTHILPYWQRWLLGILILLGILGRVWQLDQPANYVFDEQYHVPAARAVLNQDWRIFDWWQPPVSTSGIFADWLHPPIFKYLQAMAIGIWGDTAWAWRLPSVLASFGVIWVSYKIAERLGGRLAGWTAAALVAMSGLNLVQSRVGMNDMVVTFFGLLSLKVYFDRLLKPRAVSEMANRWQWLGVGVWLGLAAATKWTGWLFVMGIAGSEVARQIWVWRQTPVRLHQRLWAGWPWQVFCLGVMPVLIYFLSYWPGFFSGRGLNHLVELQRAIWQYHLTRDRTHPDQSGPVAWWFNTQPVTYWRAQVTPIHQTSQIIA... | Pathway: Protein modification; protein glycosylation.
Function: Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins.
Catalytic Activity: a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+)
EC: 2.4.1.109
Subcellular Locatio... |
F2JMH9 | MNVVFMGTPDFAVPTLEMLIDEKYTVSAVVTQPDKPKGRGKKESMPPVKEVALAHGLSVLQPEKIRGDEAFYNHIQSLNPDVIVVVAFGQILPESILNIPKYGCINIHGSLLPKYRGAAPIQWSIINEELITGVTIMYMDKGMDTGDMLLKKEIVIDEADTYASLHDKMKIVGAEALKEAMPMIIAGGKERQKQEESEATYAALIQKSLGEIKWQASTSSIDALVRGLNPWPGGYTYYKGEVMKIWKAVKTLKQGEGAPGTILEVSKEGIFVKTLDGSLCIQEIQMPNKKRMPVSEYIKGNTLDIGVILGI | 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 Acti... |
F2JMJ1 | MLLSDSINELKGVGDKVGDKLRKLGIYTLKDMIEHYPREYEDRRQITPLAACELDEPQNVLVTVCSKPQIAKKGNKILVSFRVKDETSSIMVTFFGQAYMRNNFVMGEKYLLYGKIKHKYGQLEMDSPEYQKVADPSKLGTVAKITPIYPTTQKLSQKVIRGLIEHCLNEVLPEVKDHLPERIIKQYHLVSKEEALRGIHFPKDSEHFFEARKRLVFEELFMLQLSLYQLKADFATKLMGIAHDVTSELKAFMASLPFELTGAQKRVMREIVGDMKSPYAMNRLVQGDVGSGKTVIAAISLFLVVKDGFQGALMAPTEVL... | Function: Critical role in recombination and DNA repair. Helps process Holliday junction intermediates to mature products by catalyzing branch migration. Has a DNA unwinding activity characteristic of a DNA helicase with a 3'- to 5'- polarity. Unwinds branched duplex DNA (Y-DNA).
EC: 3.6.4.12
Catalytic Activity: ATP + ... |
A0A934RUL9 | MKIGIFGLGYVGLTTGACMLRSGFDVIGYEISDIKRKELASGRVPLCEPGVGPVVIAGISEGRFRVADHPSKDDLPDVFFISVGTPSDDRGGTNLKAVNSVFSTLADMRSDLALKGSEIVLRSTVPPGTLEVFARKFEALFRVVPVAFYPEFLREGTAIKDFENPPQTVVGKLANSPNPTKLISIFEHLDFEYRVVDAVSAETLKFACNGFHALKICFANELGRIVSSFGGNPREVMELFVKDTQLNISPRYLLPGAPFGGSCLPKETRSLRNLSASRGLQTPTICSCEESNQSHFSYVIDCILALNPKRLAILGLAFKK... | Pathway: Nucleotide-sugar biosynthesis; UDP-alpha-D-glucuronate biosynthesis; UDP-alpha-D-glucuronate from UDP-alpha-D-glucose: step 1/1.
EC: 1.1.1.22
Catalytic Activity: H2O + 2 NAD(+) + UDP-alpha-D-glucose = 3 H(+) + 2 NADH + UDP-alpha-D-glucuronate
Sequence Length: 446
Sequence Mass (Da): 48776
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A0A1E4SHV5 | MDGDAPKSKVSLSNRQIELISGLSAGFSTTIITHPLDLIKVRLQLSTNQPGKPFEALTNVFRKIHRDGFISSSLIRHYKLFHIMKQYYRGITPNLIGNISAWGLYFALYAEFKTHLRMSNETTNYFGSSMLAGISTSILTNPIWVLKTRILGTSRSQGAAYKSTVDGIRQILRDEGARSFWKGTIPSMFLVLQGSLQFTFYDHLKDFFDKRRGRADRKRQISTQEYLYSSAISKILSMVIMYPSQIVRSRLQFHTKLGVKVTISSTMRQLWENEGRIKAFYKGLSANVLRVVPATCITFLVYETVKDLLHSENEEQ | Function: Mitochondrial transporter that mediates uptake of thiamine pyrophosphate (ThPP) into mitochondria.
Subcellular Location: Membrane
Sequence Length: 316
Sequence Mass (Da): 36057
Location Topology: Multi-pass membrane protein
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A0A940FHF2 | MNPQAIFKEMTPRARIGLGVAALGFLAVTFLLLKLATAPAYATVMSGVEPNQSDKITQALADRGVSYELQNNGTAIAVEKSQIGEARVALANAGVNAGSGTQPGFELLDQQKLGSSDFQQRVTYQRALEGEIANTIGQIDGVNGAEVQLTLPEDKLFSDESNPATAAVLLSGTSTLDGAQVRGIANLVAGSVQGLSPDKVTITDGAGQLLWPTDGGGSGGSGASKSAAQARYDASTESRINDMLTRTLGPNKARVEVVSDLNMDNASKEELAYAKTSTPLSQKVDDETLKGGGAGGGTSGTAANIEGSTAAGAGAGSDYK... | Function: The M ring may be actively involved in energy transduction.
Subcellular Location: Bacterial flagellum basal body
Sequence Length: 508
Sequence Mass (Da): 52194
Location Topology: Multi-pass membrane protein
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A0A945GFH1 | MNRKIILASQSPQRRNLMKSLNIDFEVIPADIDEQAVVAADPKVRAGLVAEAKAREVQKKYPQDIIIAADTYIVLDGETLEKPVDLEEAREMLRKQSGRSMSEMTGFCYLDLKSGIEVVTTAVAEVEFRELSEAEIEQYVTTQPVMTWSAAFCPAYDSGATLIKSINGSFTGFTHGLPLEELIPLLQQSKVL | Function: Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + H2O = a 2'-deoxyribonucleoside 5'-phosphate + diphosphate + H(+)
EC: 3.6... |
A0A5C5XLD4 | MISRAEPTPPENGTSSSPNANSPLAANVGIDGLIPVRMLNEYSYCPRLAYLEFVQGEWAENLETLEGTFGHRNVDKPDRKQIPARSKSNSKAAKSEETEEEGPTSIHARSLTLSSEQEGLIAKLDLLEIEGETITPVDYKRGKVPDLPEGAYEPERVQICAQGLILRDNGYHCTEGVIYYIASKRRVVIPFDDELIARTRELVRLFRETAISEICPPPLEDSPKCNRCSLVGICLPDETNLLIDQQQLTHERSQLPVKPDGLRKLLPARQNALPLYVQHQGAFVGKSGDRITIKLKGEELSSVRLLDISQVCVFGNVMFS... | Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target... |
A0A9E0L6D7 | MDTNPFANLNTISTRPKNSLGRFVLKFIVVVVGAVCVLTLWAYIFFISAPRSLNTYPVSLQISSGDTLNEISVRSEEMNLVRSKTAFQTMMFILGGDTKILAGTYVFDGPQSVVDVALKISRGDRDVTSMKITIPEGFTNKEIAAVFESKLKKFDSQEFLEKTKSMEGYLFPDTYFFFEDATSADVIASMTAQFEKKIKDVELGGKSLEEIIIMASIIEKEASGDDDRKLISGILWKRQSIGMALQVDATFKYILGKESRDLTVADLKIDSPFNTYTNKGLPPSPICNPGLKSIMAALEPETSPYIYYLHSSDGNVYFAK... | Function: Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation.
EC: 4.2.2.-
Subcellular Location: Cell membrane
Sequence Length: 334
Sequence Mass (Da): 37282
Location Topology: Single-pass membrane protein
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A0A2E9GCH2 | MKDFATENIPQFMVAAPASNCGKTTLTLGLLSALKAKGLSVQPFKCGPDYLDTQLHTKASGQQSINLDLFFSSENHVKELYSQYAHNKQATVVESVMGLFDGANRGNGSSANISKLLNIPVILVVDARAMAYSVAPLLYGYKNFDPTVNIAGVIFNFVNTDSHYQYLQAACKDVGIRSFGYVPKNETVKIPGRHLGLVTSPDLQWNDIFTNLSNHIAKHLDLDEIIEATSKPVPVHPTQKNTNSNKQLKIAISKDEAFSFTYYENLKALEALGEITFFSPLHDKELPKVDFVYLSGGYPELYLEKLSANKTMLQSIKNYC... | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from precorrin-2 (aerobic route): step 9/10.
Function: Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of hydrogenobyrinate, using either L-glutamine or ammonia as the nitrogen source.
EC:... |
A0A914CDV8 | MAQLCSSPTLHMKQVLKSRGALLVKYSVASSSNSKNEGVHQSCRRYSSVLPKKKILTKKERPDMNIQPMKVNSKNEETVAEKKTPTPLHRDIITSILDKFLRNLKLRQQANQEQGITEVLFLKAFLSFRAYCLELIPTSDPELVEKFRNVAMSKASEEILYENFVVHAKKVFPHLNCLGDLKIISDLTMPHNWYPVARTLKRRFIYHAGPTNSGKTWAALQAFKASKSGVYCGPLRLLANEIYRRMNTEGLPCDLVTGEERRFAIDNLHPSSHLSCTVEMLPTDMRTELAVIDEIQMLRDDQRGWAWSRALLGAAADEVH... | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
EC: 3.6.4.13
Subcellular Location: Mitochondrion matrix
Sequence Length: 722
Sequence Mass (Da): 81614
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A0A355J0L7 | MRYYFIAGEASGDLHAGNLIGELAKLDPEAVFQGFGGERMEKAGLQLIKHYRDMAFMGFIPVLMNLRTIKKNFRICEQDLLAFKPDVLILVDYPGFNLRMAKFAKANGIKVYYYISPKIWAWKKGRVHKIKALVDEMFTILPFETEFYRKYNYEVNYVGNPILDAVLERKIEADLPKFAKENSLSKKEIIALLPGSRKTEISYLLPVMLEASEAFPQYQFVVAGAPNMDASFYETFTKNYPVKVLWGKTYEIVQNSRAAMVASGTATLEVAILNTPQVVCYKMAGGAFFHLLGLIFITLKWVSLVNIILDREAVKELLQV... | Function: Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
EC: 2.4.1.182
Catalytic Activity: a lipid X + a UDP-2-N,3-O-bis[(3R)-3-hydrox... |
A0A659PQU5 | MTFTASSSSCAITESPVVVALDYHERDKALAFVDKIDPRDCRLKVGKEMFTLFGPQLVRGLPHRRFVVYLVLKFQEIATHKARAFAGEGAQR | Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
Function: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).
EC: 4.1.1.23
Sequence Length: 92
Sequence Mass (Da): 10341
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A0A545U4B6 | MVGYQLFFQQAEFNFPLLLVLLVFGSGIIWLFDALYLQKKRRALVSRVGDEVGEVGEELQDRYREVEAVLGREPLEVEYSKSFFPVLFIVLVLRSFLVEPFQIPSESMVPTLEVGDFILVNKFTYGIRLPVIRTKVLDINEPKRGEVMVFFPPHKKQYFIKRVIGLPGDEILYVNKVLYINGEKMPQQLVASLPPANPRFQIMRESLDGVEHAMRKHVTHGQPDRKRSWVVPEGHYFMMGDNRDNSADSREWGVVPEENIVGRAFGIWMHWEGLLSLPSFSRVGSIQ | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Membrane
Sequence Length: 287
Sequence Mass (Da): 33098
Location Topology: Multi-pass membrane protein
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A0A2M7RL09 | MLDLNIIGSHTPLKKEEIQTVFNEAVEKYGDKKTGHINLIFVRKDEIRNLNWDFRRKNKATDVLTFIYDDKCAGEILICKDFIKENIREDLKTDMVKAFIHGILHLRGFDHEKSEKEAKSMEKKEREIFQKISIKIL | Cofactor: Binds 1 zinc ion.
Function: Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 137
Sequence Mass (Da): 16193
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A0A2D0N113 | MLTGIILLIALVCLLLMGAVLIQNPKGGGIDSTFGGSQANQMFGASKQTDFIEKITWYLAIALFVLCIIAARMVGSTGGAIDL | Function: Involved in protein export. Participates in an early event of protein translocation.
Subcellular Location: Cell membrane
Sequence Length: 83
Sequence Mass (Da): 8660
Location Topology: Multi-pass membrane protein
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A0A2H5WL36 | MLPERSVYTAILTPFTEGGTIDEGLFLRLLAFQEAAGVNGVVVAGSTGEGASLSAPEKGRLYELAVQGRGRLQIIAGVLTSSLTEAQFLCQKAQKLGCDALMIAPPFYFPAPLEGLIAYFRAILETTSLPVILYNIPQRTRVPITPELIEALLGYPHLIGIKDSSGDLAQMEQYLRYMPQLRVWVGEEKFLLKCLQGGGAGTISGLANVRPQPLVQIVARFDAGEVCEGTQAQVDAFADAIDAFPAPANFKYALTHYGFPLSPVRPPLTELDPEQRAAIDQLMRTP | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
EC: 4.3.3.7
Catalytic Activity: L-aspartate 4-semiald... |
A0A2G6IZZ0 | MADANRGNRPLSPHLTIYRWQIAMFMSILNRITGMAMIPCVILIVWWFVAAATGQAHFEFVDWLATSWLGLLLLFCTLWAFWVHLFNGLRHLAWDLAWWMEMPQVNKSGWTAIVMACVVNTIFIYILLVGV | Cofactor: The heme is bound between the two transmembrane subunits.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Subcellular Location: Membrane
Sequence Length: 131
Sequence Mass (Da): 15157
Location Topology: Multi-pass membrane protein
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A0A1Y0C2H5 | MNPNTTNVSGVPVESGSTSHTAGLSGSMGTFRLFALVMAFVSPLVTVAGWLVILIAYGGPAAPAMMLMAAVLITIFSLGFVAMGHHMPNPGAFYSYVAAGLGRVMGLGAGFVAIAVYIFLGLSSFIFFGVAAAHFVSSELHGPSISWYWYTLMLLVVVSVFGYLHVEVSAKVLLVAMALEVVVVLIFDLAIFGGGRVSETGGVSLQPFSSSSLAGASWGLGLLFAILFFNGFEGTAAFREEVRNPARTIGRATLLVVGFVGVFYSVASWGIVSYFGADKAEELANSDPVSMFTTALGASVGTWLVDVANVLLLTSIFAAT... | Function: Probable amino-acid or metabolite transport protein.
Subcellular Location: Membrane
Sequence Length: 500
Sequence Mass (Da): 52491
Location Topology: Multi-pass membrane protein
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A0A318AIK4 | MTKTIGTRVRARLHPAVLLAVGLAGVTGAVVRWLVTVVFPNPSLTPGGLTTVPHGLGFSSTIWELIVINLIGSFLLGIVSGRLATSPRVQRQHLPSWLPPALTTGFLGSFTTVSAMMVSYTTGVWVLGSVVGPSPATTVVIAMLSGALLLAGVLVAGTAVALWGYRLGSRHCASRPSHPAPSTEESA | Function: Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Membrane
Sequence Length: 187
Sequence Mass (Da): 19314
Location Topology: Multi-pass membrane protein
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A0A6N4X3X5 | MNQIEFQEKEEGLDLRKIFGQYISKWPWFVLSVLLFLIVAYTYIRYSVPMYQSETILKFDKKQTDLSSALSDLDNLGIGLGNSDELKSEAAVVISRPILTRVVRNLNLNIQYFREGEIKDAEFFGAIPITAQILSYNDEKKFVSSEYIVTEIKGSQFTLWNDKDGTVKGFFNQPVKLNFGVVVLRKHFNLLPHWKYRISFTTPLEKVKELEKKIKVDLPDQKALLMNISATGAVPEKSEAILNEVTRQYNLDGLRDKNLQAQNTQEFIDRRLEVITRDLSGVENKKEDFQNQNNIVDLQAQAQLALQNTSDNTKALLEQQ... | Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Subcellular Location: Cell inner membrane
Sequence Length: 782
Sequence Mass (Da): 88949
Location Topology: Multi-pass membrane protein
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H8MS89 | MPIVVQKYGGSSVADAEKLGKVARRVKQKRDAGYQVVVVVSAMGDTTDDLLSLAKSVSQDPPRRELDMLLTCGERISMALLSMALQEQGVPAISFTGSQSGIITNDAHAQARIVEVRPYRIQDELAHGKVVIVAGYQGVSYKKEVTTLGRGGSDTTAVALAAALDAEACEIYSDVDGVFSADPRVVPDARKLESLSYDEMQELASAGAKVLNAQAVEWAKARGITILARTAHGQGTGTSVQELAVPTDSRVKGVTADAEMAVLVAHASVPLQELLEFLDARAVRGRTLAHDGLPGAPGRTFLAVPLADIHGPEALQRELA... | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.
EC: 2.7.2.4
Catalytic Activity: ATP + L-aspartate = 4-phospho-L-aspartate + ADP
Sequence Length: 397
Sequence Mass (Da): 41949
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A0A220EY68 | IMIFFFVMPVMMGGFGNYLVPLMMGLPDMAFPRMNNMSFWLLIPSLTMLIMSMFISSGTGTGWTVYPPLSSNISHMGSSVDLSIFSLHIAGLSSIMGSINFIITILNMKLIKLSLVSLFPWSVLITAVLLLLALPVLAGAITMLLFDRNLNTSF | 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... |
A0A251XK50 | MDERTHTVAPHEFLTEPQGVIRIDAVRPFPPVIVMGVSGSGKSTVGELLAQDAGIPFIDGDDLHPEANRRKMAEGHALDDDDRRPWLEEVGRALAGRPEGGPVVACSALKRSYRDILRAAAPDAVFVHLAGDHELLAERLGSREGHFMPSSLLASQLRTLEPLGDDEQGITLDITDDRVALADAAVRELLPGGRTASPGRVDDAPATATEPAAAVPEADVPAVVREARSDADVPRADVPRADVPRADVPRATCIAPTRHRPPAPRARPPPPSTSPSASRSSAAASSARITRACSPSTPSSASPRSSTSRPPPPTSSPTWW... | Pathway: Carbohydrate acid metabolism.
EC: 2.7.1.12
Catalytic Activity: ATP + D-gluconate = 6-phospho-D-gluconate + ADP + H(+)
Sequence Length: 337
Sequence Mass (Da): 35410
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A0A1J4XC68 | MKVAIVGTGITGLSIAYQLEKKGISSVLFDTAKKVGGVLNSSQFDGFLCEKGAHTLEIKTPEVQHFINEMNLTADTFEIPSKSNRYIVHKGQLQALPLSFCSFLKTPLFSIKAKLKLLTEPFVSAYKGSDDESLGHFVTRRLGKEFLDYAIDPFVAGVYAGDPFKLSVKQAFPKLHELEAQYGSLIKGGFLAKRKNGPRFKKRIISFRRGMHMLPEAIEKKLNSPIHLKTTLEAIEQKGDAWELTWNGQKEIFSHLIITVPAHKVKSLPWPQEISNKLSVFDQIEYAPIATVNLGFRQQDISGKLDGFGFLVPRKEKMNI... | Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis.
Function: Involved in coproporphyrin-dependent heme b biosynthesis. Catalyzes the oxidation of coproporphyrinogen III to coproporphyrin III.
Catalytic Activity: coproporphyrinogen III + 3 O2 = coproporphyrin III + 3 H2O2
EC: 1.3.3.15
Subcellular... |
D3LWV6 | MIGRVAAFCREHGLVHDGDLVLAACSGGPDSLALLDVLARCRERLHIEVAVAYINHGIRAAAFDEERRVQQAAAARGCPCYIRRTAVPALARRRKQSLETAAREERYRLLRDVQRQIRAQSIAVAHHQNDQAETVLWHLVRGSGLTGLAGMRPRREKIIRPFLCVTRAEITDYAARRHLHPCHDETNDELHCTRNKLRLQYLPFLAQLNPAIIADLNRLAAVVQAEDDVLRQQTEEAYRRTAQVRAEGIVLSKTRLAEQPTALQRRLIRRAYEALTGHMTGLSLEQVETVRHLLDKEPGKRFAMRAFYVQRTYEALVCTA... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
A0A2M8D5M6 | MGNFGIGEILLIFLVLLLLFGGKKLPQLAEGMGKALKSFRKAVQEPEESEPSKEKENKETE | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
Subcellular Location: Cell membrane
Sequence Length: 61
Sequenc... |
A0A1S2DCG2 | MFDIGFFELLLIGIVGLLVLGPERLPKAARTAGLWVGRIKRSVSTMQREITSQLEAEELRQKLAEQQKKLDEGVNQARRGVEKHFESDSKGGSSPSTSTPSISTPSSGNDRQSAGATSDADPQPSSSPESPPAASSSSPADKDSASR | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding... |
A0A1B8QDN8 | MSNTDLPTHLNQGFANTPLTKTPNKKSKPSARVRKRLQAAAPVALTVNNLAHDGRGVAVYGQVQETTALAEAHPIDKHGKKVFVSFALPQETVSVQITNSRSSFEEGDALAVLANPSPERQTPPCPHFGVCGGCSLQHWQPDGQIAFKQSVLAELLAHQGGLAPEVWLPPLVGERLGYRTKARLGVRYVEKKQRALVGFRERSSNFLADLQVCHVLDARIGKQLIALQTLIASLDAREAIAQLEVAMGETLPDVPDSKQAVAVIVRNLAPLDAADMARLQTFFAERDWQLYLQPKGSDSVQRVAVRDDEPMRASTLDVPP... | Function: Catalyzes the formation of 5-methyl-uridine at position 1939 (m5U1939) in 23S rRNA.
EC: 2.1.1.190
Catalytic Activity: S-adenosyl-L-methionine + uridine(1939) in 23S rRNA = 5-methyluridine(1939) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Length: 514
Sequence Mass (Da): 55932
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M8B9G8 | MGVQGCDASVLISGPGDEHSAGADTTLSPDALDLITRAKAAVDAVAGCSNKVSCADILALATRDVVQQAGGPFYPVELGRLDGKVGTRAVVKHSLPGAGFSLDQLNKLFAANGLTQTDMIALSGGHTIGVTHCDKFVRRLYTGYYQTLQQQKGLLSSDQVLFADRRSRATVNHFAANQTAFFDAFVAAMAKLGRIGVKTAGSDAEIRRVCTKLHVNTVDVLCEVECSVHCTVWHGGPSQPVTEDATCISMDGRGCTRQRRQKTLGQKNTTDMPDPHLCVDLRIEGGRWEEAWGFGSTRRGGR | Cofactor: Binds 2 calcium ions per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress.
EC: 1.11.1.7
Catalytic Activity: 2 a phenolic donor... |
A0A2R6GEA3 | MDDLIEAAREANANAYAPYSEYPVGAAVETADATVFTGCNVEVVNFSNSMHAEEVALGEAIKRGHDEFERVAVSSAARDGVTPCGMCRQTLAEFAGEDLQILCDEGDSVAEYTLGELLPATMTQEMVE | Function: This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
EC: 3.5.4.5
Catalytic Activity: cytidine + H(+) + H2O = NH4(+) + uridine
Sequence Length: 128
Sequence Mass (Da): 13671
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A0A914CPJ3 | MTVKDSSILEPLHSQRWKCGEFDDEILDMVESSEVESIAFQLCHSDTLYNDYFKNMNAGRLKSALTCLVLLCAFEMIIHAISGDWLKFAALNVINVLLLLLIFVWEKQPLILSWIVVAASAIILCFAPVALSSSMTLLTLFLCYTLLPLQLKPSALAAIIITLLALIIQIFHYAKPRELIAEVLLLLAMNISGIFVYYPTELIQRRTFRETRKCVERRIRLVHDNQKQELILLSVLPKHIAHEMKRDFEVGHDDEHTFRKIHIQKNENISILFADICGFTNLASMCKAEDLVKTLNELFARFDKQALENHCEKIKILGDC... | Catalytic Activity: ATP = 3',5'-cyclic AMP + diphosphate
EC: 4.6.1.1
Subcellular Location: Membrane
Sequence Length: 350
Sequence Mass (Da): 39942
Location Topology: Multi-pass membrane protein
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A0A925P0W0 | MTEFELNTIPEAIEAIKRGELIIVVDDEDRENEGDFIAAAEKVTPEMVNFMTTIGRGLMCAPITEERCAELELEMMVGNNTSSHETPFTVSVDLLGHGCTTGISASDRAKTLNALANSNTKADELGRPGHIFPLRARSRGVLRRAGHTEAAVDLA | Cofactor: Binds 2 divalent metal cations per subunit. Magnesium or manganese.
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.
E... |
A0A368NNG5 | MKLWAQRFINLMTEIGVLRLTLVVAGSIIVLGIAINVSLRLAISGDVDTLDIARALLLGFILTPPTVFLFVLVVRELDLSRRRTDRLRAKDREKAEKLEHQLILLEAENAERVKAEQALAEVVAEMEAEVMQRRQAEIKAAEQSAKLGSLIDSSPDVIFYRDDNGYFSSCNRAAELLLGRTREELVGLTPADVYPERLAEQVVQTDAAVMASNRPLKFEQWMRYPDGRKTLFEFSKVPFFGAKGERLGLVAFGRDITERKQAADLLSKASNEKAEFIATISHELRTPLNGIVGLSRILRDTELSAEQLRYVDTIYLSAET... | PTM: Activation requires a sequential transfer of a phosphate group from a His in the primary transmitter domain, to an Asp in the receiver domain and to a His in the secondary transmitter domain.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cel... |
F4PAT3 | MADASVDEVLALKNQFYLGSFQTVINEATNPATTPRTETGKLDRRVLLHRAYICHGRFNLVLSELSAQETSMELRAVRILARYLASMTDQLQQQEAVADAVALAEMIPFDVSPVVYVLLGTVFYHEGQTEEALKLLVRAPKHLECIALAVQVYLKMDRPDLAKKELDLFKSWADDATLAQLIESWVNIAVGGPEKYQEAYYIFEEMANTGTSTCRLLTSKAVAMIQARKFEEADAILLEALNKNPNDPDTLANMVIIATALQKPTSVLNQFMSQLKDVAPHHPLVQEQLLKESLFDRSAMRFSQTA | Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. The coatomer complex is required for budding from Golgi me... |
A0A961IXE6 | MSVETGIWGVVALGILLILRLPVALALIIVSFSGIWAMIGLKPALGILENTPYSFVASWTMSAVPMFLLMGFVAFHTGMTGGLFAAAKVLLARLPGGLAISSIFACSAFASVSGSSVATAAAMGRIAIPEMVNAGYRPSIAAGSIAAGGTIGALIPPSILMIIYGIIAETSVTQVFVGGLTIGILTAISYATVVLIISFTRPDVIPPRVARVEGESTRVLVQLLPVSALVVIVFGGLFSGMFTATEAGAVGALGTVVLAAVTGKLTRKAVSRSLIETVTTTGSLLIIGIGATMFTRFLGLSGLQNFIAQAVAGADLGYVG... | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 341
Sequence Mass (Da): 34814
Location Topology: Multi-pass membrane protein
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A0A2G6IBG8 | MIVDVIIEEPRWEAVGLSDLAERACGAALAHLGVEGAEISLLACGDERIAGLNSDFRGRPAPTNVLSWPSEERGADEPGGAPEPPQDPELGDIAIAYETCAREAAAAGKPMGEHVTHLLVHGTLHLLGYDHIHDKDACLMEALEVEILGKLGLADPYESESG | Cofactor: Binds 1 zinc ion.
Function: Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 162
Sequence Mass (Da): 17110
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A0A920KYV4 | MPLAALSEKDRADLDFICGLGIDWLALSFVQRADDIIEASKLVAGRAAIISKIEKPSAVKSFEDILKVSDGIMVARGDLGVELPVQNVPPIQKRLVRKCRAAAKPVIVATQMLESMVESPMPTRAEVSDVATAIYEGSDAIMLSAESAAGQFPIQAVETMNNVAIEVESDPTYTEVMEASRRAKRNSVADGIVSAAREIAETTDIKAICCFTQTGTTALLTARERPRVPIIALSSEIGTARRLALTWGTNCVLSGNKTRFKEAVVSAVRAALAEGLADETEQVVITAGVPFNITGTTNILRVAPCNERMIYAMDPE | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
EC: 2.7.1.40
Catalytic Activity: ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate
Sequence Length: 316
Sequence Mass (Da): 33836
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A0A1G0GKM0 | MPTYHFSRKERLARKQDFQSILKSSNKITYKYLLVLYRSNQCCFARLGMILPKRIVQKAVDRNMIKRVMRESFRHHKQVLQNLDIMIVLRSKLHVTYQKTLRQDLENIWEKLGSVCN | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of... |
A0A251XDU3 | MPGTKKLVIVESPAKAKTIAQYLGSGYEVQASVGHIRDLIEPKNLPPELKKGTLGKFSVDVENGFEPYYVVSDQKKKTVADLKRALKDADELFLATDEDREGEAIAWHLLQVLKPKVPVKRMVFHEITKEAIERARDSTRDIDTALVDAQETRRILDRLYGYEVSPVLWRKVGPGLSAGRVQSAATRLVVDRERERLAFVTASYWDLTASLSPVDQQLPFDARLVRIDGARIATGRDFDDKGALKNDSRPLDASSAEALAEALRDPSVPLKVQSVESKPYTRRPAAPFTTSTLQQEAARKLRFSARQTMSVAQSLYENGY... | Function: Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is ... |
A0A914D3N6 | MAAYSDFPPPAEFANFMHNTQMLKYLELYATQFDMLKYIKFNHRIVNIERAKSYNEDGKWIVTYTDDQGQKQQEEFDGVLVATGHHAKPYYPEKWHGQDSFKGKIIHSHDYKSCQGYDDKVVVVVGIGNSGGDVAVELAKICKQVILSTGYSFDFSLLEGGTLVPVKDNEVSLYKYVFPPDLSDHNSLGIIGLIQPLGSIMTAAEMQARLFFDAFVGNTKLPSKSEMLAEVKAKKDYLTNRYVHSRRHTIQVDFKYLGELALLMGAYPHLKDYIFSDPVLTYHLLFGPGTAYKYRLNGPYPWHGARDAILTTQYRVDKGF... | Pathway: Siderophore biosynthesis.
EC: 1.-.-.-
Catalytic Activity: L-ornithine + NADH + O2 = H2O + N(5)-hydroxy-L-ornithine + NAD(+)
Sequence Length: 454
Sequence Mass (Da): 51976
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A0A1T4MIC3 | MLDELDARVSSLTLDGWAAVRSSCVVPLSRAEFDASRLIALREALAFARAKSPFYGIRGDWPEDGLTSLADLSRWPFTNAGDLLRDDPPLAAVASRDISRLVTLPTSGTTGRPKRVPFTAEDLEATIDFFHHGMALFTRPGDRVLIAFPANRAGGVGDALGRAMTRLGAHPLTSETGLAAEALAARLRLERPDVVVGSPIQLLSAARVSVADGGPRIGVRAALASADAVPPVLADILAQSWGCELHAHWGMTEIGFGGAVDCHFHQGMHLRETDLLAEVVDPVSGAVLPPGREGEIVITTLRPRALPLVRYRTGDLGRLV... | Pathway: Organic acid metabolism; glycolate biosynthesis; glycolate from 2-phosphoglycolate: step 1/1.
EC: 3.1.3.18
Catalytic Activity: 2-phosphoglycolate + H2O = glycolate + phosphate
Sequence Length: 718
Sequence Mass (Da): 76048
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A0A327VAZ5 | MTADTGTTDTGPETDTYTGTDTRTDTGTNITADDGASGGVHHTVVDSPLGALTLVADGGALTGVYFEDHLRGPSPGALGPRDETGFDEARRQLAEYFAGERQRFDLPLAPRGEPFRQRVWALLRQIPYGETRSYGLLARELGDPALAQAVGSANGRNPLSVIVPCHRVVGADGSLTGYAGGLARKRFLLELEGAASVTRTARLF | Function: Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irrever... |
A0A945QC74 | MSGKPFYVTTPIYYVNDKPHLGHAYTTVATDAKARFHRLRGEAARMLTGTDEHGQKLEQAALDAGKDTLAFATENSEKFRALWKKLNIQCDDYIRTTEERHKRGVQEIWRRVSKAGDIYKDEYEGKYCVSCENFLTDLQLDDGKCPDCGRPAESVREESYFFRLSKFQEPLLAYYEKHPEFIQPEGRRKEIISFVAGGLRDLSVSRTSFKWGIPVPDDPAHVIYVWFDALSNYATAAGFGAEGVGEDGFPEGTAWPADQHFIGKDILRFHSVYWPAFLMSAGLPLPGQVFSHGWWTIEGQKMSKSLGNAVDPHWLIEEYG... | Cofactor: Binds 1 zinc ion per subunit.
Function: Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
EC: 6.1.1.10
Catalytic Activity: ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met)
Subcellu... |
A0A927FAX0 | MAEAELRDRWMQLKAEIAYHDELYYQKAAPEISDAAYDALKQEFLRLDALFGAEEGHRRVGDDRGNGQGTAVHLSPMLSLDKAYSKSELERFHHQVAALAGREDISYSIEPKVDGMAVSVLFEDGKFVRAVTRGDGESGVIVSENVKRIDGFRTQLLGDSHPRRMELRGEVFVRFEDFVRINERRLARGEEAFAHPRSVAAGSVKLSDPAVFADRGLSIVFFAMGACEPNEDAPARQADFFEQARAWGLPVLEERMEVRGKLELLQSAEAMQDERLNYAYPTDGTVVKVDSFALQSRLGESRDAPHWALAYKSNGTQVES... | Function: DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
EC: 6.5.1.2
Catalytic Activity: NAD(+) + (deo... |
A0A1F7LQ66 | MEKRAILAAVLMAGVLLLYQTFFVSQQEPQAPQKAQQAAAPATPGAAAVPAASAVPEPPSPVPPVAPATAAPEKTAVVETPLYRAVVSSSGGALQEWQLDYRGQKPMIVAGLLGPRGLLIERPGGQATPVPFRLSAEALRLGEGAPQGEVILTGDDGFGLRITQALRFRADTYVIEQALRIENRHSVAQSADVVLPWAGPAEWPKEQPEKFPGQHPTRAVRFVSGNVHRDEVANISGFGGDGTWVGLESELYLSALVARSPGFKVTTAKNGTTVSVSLRATLPRLEPGQAWEGRYATYVGPKEYDRLKALGVGLEKSIFF... | Function: Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispa... |
A0A2H6ET22 | MNFSKLKRLMPLLLPLSWVYGGAMLFRGFLYDFGILKSHQAQAPVVSVGNITAGGTGKTPVLIFLGQFYAERGKKVGILTRGYGRKSKGQILVTGEHASLAPEEIGDEPCLIHRELKKIPIAVDKIRWKGANALSQKMTVAAFLLDDGFQYRAIRKQVEIVVLDAAQPFGNLRLLPAGFLREPIRSVKRASLIWFTRVNETDNFTETARRFSRYSRAPMIESVHQPLEFRRVDESRVEPKEAFSGEPVVAFCAIGRPESFRRCLNQLKLNLRAFREYSDHHLFSEKDILDIKNLAKKKGVRFILCTEKDAVKLQKTAPDF... | 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 te... |
A0A2H6F058 | MYHISTDYVFSGENGPYREEDKPDPRGFYAKSKWAAEIAIRKMGVSYFIARTSTLFGTGENVRPNFVLWLISALKKNQEVTIVDDQTGNPTLADNLAEALRVAIEKRAAGVYHLTGREAIDRYSFAHRIAKIFGLNALLIKRGKTSHLKQLAPRPMNAAFIVEKAEKELGVHLMSVDEALFKLKQQLG | Pathway: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
Function: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose.
EC: 1.1.1.133
Catalytic Activity: dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NADPH
Sequence Length: 188
Sequence Mass (Da): 21110
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A0A8A2VJR0 | MFGNFGSSSGPGPDPDDFEAAREQMIRTVAPRVDDDRVLEAMESVPRHAFVPSNRRDSAYEDRPLPIGDGQTISAPHMVAIMADELDLEDDEDVLEIGTGRGYHAAVTAEIVGEENVYTVEYGEELAERARERLADVGYEGIAVRTGDGREGWAEHAPYDAAYFTCAAPDFPDSVVEQVRSGGRLLAPIGSRTQTLVEATKRDDGRLERTDHGGVRFVELRG | Function: Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
Catalytic Activity: [protein]-L-isoaspartate + S-adenosyl-L-m... |
A0A7C1JN86 | MIVPVGADSFATALRMGAEVYHALRRILHKQGLSTAVGDEGGFAPRLETNEEALKLLVAAIEDAGYRPGEDVALALDPAASEFYRDGRYVLKGEGRNLTASEFVDDYADLVGRYPILSIEDGLAEEDWEGWELLTRRLGKSLQLVGDDIFVTNPRRLSRGISLGVANAILIKLNQIGTLTETLETINLARRAGYAIVISHRSGETEDAFIADLAVAVGAGQIKTGAPSRSERVAKYNQLLRIEGELGESAVFPGKEAFKRF | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5.
EC: 4.2.1.11
Subcellular Location: Cell surface
Sequence Length: 261
Sequence Mass (Da): 28333
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F2JJD5 | MDTQKFNVYVDGQAGTTGLKINERLKLHPYINILKIDEDKRKDPAARKEMINAADIVFLCLPDAASIEAVSMIDPANTRTKVIDASTAHRTHPEWTYGIPELSAQAREAISHSTRTTVAGCYASAFILPLYPLVQSGIIPADYPISSHGISGYSGAGKSAILEYTDPHRDELYPTYGTPRHYALGLHHKHVPEMQQKVGLTYPPIFSPIIADYYQGLAVATQIHTRLLGKKVTPLDVHTYLAKHYEGQNFVKVMPFNPSQCLDENFYNPVACNGTNNAEIFVFGNDEQILLLTRLDNLGKGASGAAVQNMNIMLGLDETI... | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4.
Function: Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
Catalytic Activity: N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = ... |
A0A1J4XDB5 | MSFFKRSCLEEIKLKVSIVDVVAPYVTLKQTGSYFKGLSPFNHEKTPSFFVHPDKNFFKCYSSGNSGDIFRFIQLKENLAFPEAVEVLANRFNIPLEYEDGQDKESMSERKELFDIHEIAAEHYRKAFLADTKEGAWIRNYWEKDRSFLLNTAKEYGVGYAPLDGRDLLNELLEKKFSKEALTSCGLFYTGKGNNRPENWHPRFQGRLMISIKDIQGRVIAFTGRALEITPEKDPARDAKYINSPETPLFSKSHVLFGLDNARQHIAQENHFLLVEGQLDAIRCWEKGLKTAVAPQGTSITMEQMGLLRRYASNITCFLD... | Cofactor: Binds 1 zinc ion per monomer.
Function: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
EC: 2.7.7.101
Catalytic Activity: ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.
Sequence Length: 617
Sequence Mass (Da): 70840
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A0A1I5V8P3 | MHCQSELAIGLMGGTSMDGIDAALVKISQDNSSVEAELLEFECYSYSEEVKETLLSLSKGINGGTREICLMQELLGKLYADACVSLCQKANVNKHDISFVGCHGQTLWHQPKAIDYLGNKIRGTLQIGDPGFICEKIGCPVVSDFRPRDMAAGGQGAPIVPYTEFILYREDKDVALLNIGGISNITILPAKGRIDDVIAFDTGPGNLLIDQMVKDYTQGEKVYDEGGKIALSGETSKVLLDYMMQDDYLKIAPPKSTGREHYNSDFVKDIYEFCTTNNISKVDMIATVSRYTAECVYHSVREFSSVYPSKLIVSGGGTHN... | Pathway: Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate degradation.
Function: Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the... |
A0A944VGV1 | MELSGSQIVIEELKANGVEIAFGIPGGAIMPFYDELNKTKFPHILTRHEQGAAHMADGYARVTGKVAAVVTTSGPGATNIITGLCNAKMDSVPMIAITGQVSSPTIGTDAFQEADTYGCTIPVTKHNWLIKDPNEIQGIMREAVRVATTGRPGPVVIDFPKDIQVAMAEYNPRTPAAIGPSTDLDAITPEPDTKAIDRLIDEIGRAKRPVILAGSGIMKAGASAELAEFARRSEIPVINTLLGLGGFPGTDPLFLGMPGMHGTAYANLALCECDLLINLGGRFDDRVTGKISSFATGATIAHVDIDAAELGKRVETDIPI... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4.
EC: 2.2.1.6
Catalytic Activity: H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2
Sequence Length: 566
Sequence Mass (Da): 61182
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D3KSY7 | ETIRKYPPVDYLMRRSKTTYNHIPDGTLFIVPTYALHHDPDHYPEPEKFDPERFAPSAIRKRHPYSFLPFGAG | Function: May be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 73
Sequence Mass (Da): 8600
Location Topology: Peripheral membrane protein
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F2JGW5 | MAKLVVKRYATALFDIASSEGKMATYEEEVKVIIKVLQDEPDFMAVLENHKVTTEEKISLLETIFTGKVENSILGLLVLLVKKGRQSEMINVLEGFLERIKKESGIVKATVTSAVALKEGQVEAIKAKLEASTKSKIELETIVDEGIIAGLVIRVGDKVVDASIKGEMQALKKQLSKLRPA | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
A0A2S0KLG9 | MFFKKKGNTENNQDAILVVGLGNIGKEYEKTRHNAGFIFVEELALRHKGNWKKSKFSADICDINIAGKKIILAKPTTLMNLSGIAVQKLLKFYKIPLENLFIAYDDIDINIGKIRVRESGSAGTHNGMKSIIKEIGSKDFPRIRLGIGPKPEYGDMVSFVLGKFTAGEMKALDIAVNNAIELIELTVEKNLQLAMNEVLGNKHA | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
EC: 3.1.1.29
Subcellular Location: Cytoplasm
Sequence Length: 204
Sequence Mass (Da): 22618
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A0A1V0AFG1 | MSVLVVTGTGTGVGKTVVTAALAALALARGSTAAVVKPAQTGRAAGEPGDVDEVIRLSGVTTTFELGRFPCPLPPAAAARAAGTPPVSLSAAATLVRELAASNRLVVVDGTGGLLDRYDEEGATIADLARALRAQVLVVARVGGDTVNHTALTLESLAHHGLDLAGIVIGRWPAAPGPAELSSVADLEMLAARPLAGALPEGMGGLRDRRAFTEAARQGLGVTLGGAFRGPLS | Pathway: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 1/2.
Function: Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.... |
A0A1E3REB2 | MLSAGERFDGYVVDAAVGHGGSAAVYRVHDADNPARVRALKILDDRRNLAEVARLRREFDFAHALDHPHIVKTYERGPGWLTMELISGGAIARLPTIGARLGALSQIADALDHTHNHAIVHCDVKPANILIDSHGNRAVLIDFGVAVALRDDICRRPAQVEASLPYSAPELLTGHAPAEATDVYALACTAVELVTGAPPFPYDSKMGLIGAHLYEKPPRPSREHDWLPRAFDSIIAKALAKAPSDRYQSCREFVALIVRALQ | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.1
Subcellular Location: Cell membrane
Sequence Length: 262
Sequence Mass (Da): 28495
Location Topology: Single-pass membrane protein
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A0A2G6I5R2 | MTLPRQHDLWQRLLSYRVLDAAWEKVRANGGCSGGDNVTIPQFQAGAGRRLADLARAVEKGEWSPAPYRRVEIPKRKGGVRTLRIPSLIDRVLHSAIAAVLTPVLEPQFEEGSFAYRPGRSVKQAVRAIEHWRDAGYWHVIEADIVGYFDAVRHDQLLAKLEAALEGWPGGAQITDLVAHILLHQALDCGIEGKGLAQGSPLSPLLANLYLDALDEEIHGRGIRIVRFADDFVVLCKRRKSAEAALEEVEATLTAHGLELHPGGTRVLDFDRGFEFLGHLFVRSMVMQQVSDPEEDMVSLLRGVAEADTALAEEISTEVD... | Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target... |
A0A196NVW0 | MRNLFFYGSLRHKPLLEIVLDHPADKLDLHRAFLPGYAAFAVTEGPFPLIKPCTEGAAEGVILRGLTDADIARLNFYEGSFAYDLVEMVLADGQTAEVYLPEADRWTPFGPWSLTEWEADWAALSCEAAREVMGYFGSRSRDQVAAMFPMIRKRAQSRLNAATSRHGALTKSGKTVIEARQRSYAHFFALDDMKVRFERFDGSMSPVEDRAVFIAADAAILLPYDPLRDRVLLVEQMRMGPLARGDRTVWQLEPIAGHIDPGETPRAAAIREAQEEAGLTLKAIEPIAEVYASPGNSTEFYYIFLGIADLPDAAEGIGGL... | Function: Acts on ADP-mannose and ADP-glucose as well as ADP-ribose. Prevents glycogen biosynthesis. The reaction catalyzed by this enzyme is a limiting step of the gluconeogenic process.
EC: 3.6.1.13
Catalytic Activity: ADP-D-ribose + H2O = AMP + D-ribose 5-phosphate + 2 H(+)
Sequence Length: 377
Sequence Mass (Da): 4... |
A0A8C4REY0 | MLTLYSAFTPCCVELSNPQTKTPSVPKSLEDLRLSLGDIQSTIAMAVMFVTILLPSGWILAHLEDYKHKK | Pathway: Energy metabolism; oxidative phosphorylation.
Subcellular Location: Membrane
Sequence Length: 70
Sequence Mass (Da): 7793
Location Topology: Single-pass membrane protein
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A0A8C4TIN3 | TRHKGLGYPQEKPCITEKKITTNFTNQLHRDGPIGQPSGKTVLRTLVKKALGTKVSHPTGSFQSSCTRVVTSQTTMELGASLINGNKFADENFTLKHTGPGILLMANAGTNTDGSQFFIRIAKTDWLEGKCVGFVHSKIEKNIVTHAE | 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: 148
Sequence Mass (Da): 16110
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A0A251XJB9 | MRAIRFDEAEGAYVVESVDAAGTAHVHRARNLVVGVGTPPWLPEAVRDLPGVVHSSGYLGAKAALQERDAITVVGSGQSAAEIYRDLLEDVDSRGYRLDWITRSPRFFPLEYTRLTLEMTSPEYSDHFFGLPADARDVLLREQRNLYKGIDSELIDEIFQTLYRKRLAFDALRAEGGSRRAATRDPACRPGC | Pathway: Siderophore biosynthesis; mycobactin biosynthesis.
EC: 1.14.13.59
Catalytic Activity: L-lysine + NADPH + O2 = H2O + N(6)-hydroxy-L-lysine + NADP(+)
Sequence Length: 192
Sequence Mass (Da): 21427
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A0A7X8VJ54 | MDFHALNALLNLYDDDGKIQFEKDREAANQYFLQHVNQNTVFFHNLHEKLDYLVENNYYDPIILDKYDFEYVKSLFKRAYSYKFRFQSFLGAYKYYTSYTLKTFDGRRYLERFEDRVCMVALTLADGDKAVAENLVDEIMTGRFQPATPTFLNSGKAQRGEPVSCFLLRIEDNMESIGRAINSALQLSKRGGGVALLLSNLREAGAPIKKIENQSSGVIPVMKLLEDAFSYANQLGARQGAGAVYLNAHHPDIMSFLDTKRENADEKIRIKTLSLGVVIPDITFELAKRNDDMYLFSPYDVERIYGKAFADISVTEHYDE... | Pathway: Genetic information processing; DNA replication.
Function: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
EC: 1.17.4.1
Catalytic Activity: [thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [... |
A0A8C4SZE5 | MAHHSSALRVLPLWIVLAASMPAGFFSLKSPSCHEVKTAFQQRQIGLLKWVPDVPGTEEDLSICQHKEPTCCTRKMEDSYQLAVRRETIEKIQALSMEIKYHIAKNAQSFQDAFQSLIQFAKNHTTSLFETAYRAMAHEATGPTAEFFTDISLYIFGSNGSVEAAVQHFYNNIFPSVYNRLLNPGITQLSMEFTECLRMTRPSVNPFGPHSQALAQNLSRSLNAARSLSEALSLGMEVINITEHVSFTRDCIQGLVKMHYCSHCQGLTLIKPCANYCLNIVQGCFMGLTELDHPWRDYIFSLKEVTNVMAGAHDLEFDLL... | Function: Cell surface proteoglycan.
Subcellular Location: Cell membrane
Sequence Length: 386
Sequence Mass (Da): 42959
Location Topology: Lipid-anchor
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A0A1Y4TFS5 | MEQLNKEFVFSHIPPRAAESHKGSYGRLLVVAGSRRYRGAAGLAAEGALRSGAGIVTLASVEPVIGAAASRLPECCLLPCPEGEEGGIAAAGLEMLQAAAAHATVLLLGPGLGHTGDTCALVQGLPAQMRGTVVLDADGLNAAADLLAQGGAMPLPASGSLIVTPHPGEMARLTGLPAERIAADRPGVASRFAAQWGCTVVLKGHRTLIAAPDGRLWQNTTGNPGLARGGSGDVLAGMIAGLAACGLDAPAAAACGVWLHGAAADRTAARLGQYGMLPHDILADLGGLFAENGR | Function: Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or ... |
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