ids
stringlengths 6
10
| seqs
stringlengths 16
1.02k
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stringlengths 117
4.4k
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A0A423Q923 | MAGSGSRGGRLFFALWPDAATATDIDARAASLAIRGRRIARHRLHMTLAYHGLCDAAQARALVRRAEAIRVPAFALMLDRCGGFERAGVAWLGPASPPSALHELASLLAPEGLDSAAFIPHVTIARRAEPPARTAIAPLPWPVTGFHLVESAAGARSGAYRSRGYWPLTPRPIKRAGV | Function: Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester.
EC: 3.1.4.58
Catalytic Activity: a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + H2O = a 3'-end 2'-phospho-ribonucleotide-RNA + H(+)
Sequence Length: 178
Sequence Mass (Da): 18930
|
A0A520K024 | MTHMLLSPTPAEVNEFADAYMRGMRSKDNVLVVVGCCCVEYVGRARSMLGWGGRVVIVKSDGSVLVHQKVGGAPVNWQPPDTLVRYRTEAGNGISLFVIYSYRLKPPEKMYVRFKTVDMVSAHRLRDDRTLRIMGAESDIVDRIMGDPGVIEEGLRITDREKQTRSGAIDLFGVDRDHIPVIIEIKRSQPTPSAVLQLKAYVLDHQHRHTGAVRVRGILCAPSMPVMIRTLLTENKLEWRVFKCEFEQVDDAQSTLEEFT | Function: Cleaves both 3' and 5' ssDNA extremities of branched DNA structures.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 260
Sequence Mass (Da): 29355
|
A0A172YDA0 | MASPSLIDAWLDTFAPRPSTAAIGGALAGGAFVQHERGIFELRPTVVDQRAVALVISVGVHGDETAPIELLGETLSRLEAGLVRLGAPTLLLLGSPEAVVRATRYIDTNLNRLFERGREGMRPEQLRARELMTAVDRFFSAHQGRARLHLDLHTAIRESLHPRFAIEPFAATSTPAALWNALHGAGLQAGLRQHAHSWTFSHYSRHYHEAQGFTLELGRVAPFGANDLAPLRPLGAAIEAWIEGAPLGLDARDGEVAMPLYRVAREITREAEDFRFAFADDLANFSEFPPGALVGADAVQGEVRVGDRPQRVVFPNPRVELGARAGLLVERLD | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 5/5.
Function: Transforms N(2)-succinylglutamate into succinate and glutamate.
EC: 3.5.1.96
Catalytic Activity: H2O + N-succinyl-L-glutamate = L-glutamate + succinate
Sequence Length: 333
Sequence Mass (Da): 36253
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A0A8J3F7P4 | MIVLVAAMGRNRVIGKAGGLPWHLPADLAHFRRLTTGKVVLMGRKTFEAIGRALPNRVNVILTRRRDWRPEGGTVVHSVAEALARFGGEDLYVIGGATVFRQFLPLADRMHLTHIDVEADGDAWFPPFDEAEWAVVAREKGPKDAQNPYDYWFVEYRRRR | 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-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH
Sequence Length: 160
Sequence Mass (Da): 18164
|
A0A7C8A757 | MVFNDFLIKEATSVLQRSKCGFITSLHLTEVVDKILVEDFDELAKDSKITLLAVGGYGRKELAPFSDIDIMIIANKRDPLTSESAERLLYSFWDKGINISHSFRTINETLEDSLKDLQTRTSLLDVRFISGNKSLFNTFILDAYQKIVKKNKKDFISQIFNEVYRRYKTFSLSLYQLEPNIKEGRGGLRDLHTILWLCRIALGFKSLDDLKTLFTKNEFRHFKRACEFILRTRIYLHVVSRRKNELLTFEYQEALSNLMGFKKTNLFLGSEIFMRVYYRHSRTIMDALKKVMNLFSKTIFSLFPPLIVKKASKHFCISKGEIILDSKYTLDSPELILEAFYVYATTNKEFSERLQDLIGKKKLIINKDRQLSSHSAQLFIKILSTKRVYETLYEMHRLGILDRLFSDFGRLRYLVVYEPYHRYTVDEHTLRTIKHLESLRNNSNQKFPLLNNLTLEIAPYILYIALLFHDIGKGIYGSSMKHEGEGYKRLKTLLEPFEIDKKEKKTIEFLVKNHIFLSKYALKRDIDDIETIKWIADTVENEYNLKALLLITFADMSAVNPEYFTDWKAKLLFEIYHKTISHLRGDVFRIQKGNREFLSLLPERYAVASSHDDIIRDHKLFESFNGNEPMVEIRKIRDENTEIIIVAHDERCLFLKILDVIGSEGLNILNARLYPTKNERILDKITVSNWANLEHPGFTEYFIRKMKQVITSETRILNGINVENYREKIKCEIANLPSHLVNFETFVEIDNESSGNFSIIEFFAGDRIGLLFDVARIFSLFDVDISSAVINTEDNIAHDVFYVQHKAEKLDSLLTLKIIRAVHYVLC | Function: Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen metabolism.
Catalytic Activity: [protein-PII]-L-tyrosine + UTP = [protein-PII]-uridylyl-L-tyrosine + diphosphate
Sequence Length: 827
Domain: Has four distinct domains: an N-terminal nucleotidyltransferase (NT) domain responsible for UTase activity, a central HD domain that encodes UR activity, and two C-terminal ACT domains that seem to have a role in glutamine sensing.
Sequence Mass (Da): 96687
|
A0A5S9QF74 | MTELVGLTVMFFVVLLFLRAASHKALDFLQFQGFVADYQLLPQALVVPISVSLVVVEIAIVVMLVSGFYWQAALFLASSLLLLYGIAIGWNVRRGRRQIECGCGGIPQQLSYRLVLRNLCLALLVLVPVATLGADTASGFLLVPMCASVLLMMTYLLFEQVANNAVAAKLPSA | Pathway: One-carbon metabolism; methylamine degradation.
Function: May be specifically involved in the processing, transport, and/or maturation of the MADH beta-subunit.
Subcellular Location: Cell membrane
Sequence Length: 173
Sequence Mass (Da): 18764
Location Topology: Multi-pass membrane protein
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A0A5E4Q8L5 | MRLFTSMDGVLWLALLFVIFAQTNCNRICDFKVRLTQTLHNEGFHRNLTYYIEYTSQGKINPYNGCSVGLEVVLPPGVYASPDQLASIKSKSIAVFKTNVNTESAAHEADIVIVHLLGTVYEGVAELSLPVHARYHAAVDEGTAATVVILPPRAYLNCGVNSLERCEEPPRETPAVNHFCAHVPQQRCPWRETPLDMSSGPLRWSVPVGDSGHLPLVASVSAAVAALGSFYLLYVIHCVTIRLRTARADKKK | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Function: Essential component of glycosylphosphatidylinositol-mannosyltransferase 1 which transfers the first of the 4 mannoses in the GPI-anchor precursors during GPI-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 252
Sequence Mass (Da): 27730
Location Topology: Single-pass membrane protein
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A0A822IM77 | SGMIEPNMGTMLAFIFTDATLSKVTLDAALRKAVDKSFNMLVVDGDTSTNDMALLTATGFNECEEDVFQEGLDHVCISLAKMIAKDGEGASRLIEVRVTGAKSAKDARKAAKAIVRSPLVKTAIFGKDPNWGRVVAAAGYSGADIDQDKISLKFSDTINEVVLVDSGKIVEGKLDELKGIMESKEIIIEVDIGLGNFGAIAWGCDLTYDYIKINAMYTT | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic): step 1/1.
Function: Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate.
Catalytic Activity: L-glutamate + N(2)-acetyl-L-ornithine = L-ornithine + N-acetyl-L-glutamate
Subcellular Location: Cytoplasm
Sequence Length: 219
Sequence Mass (Da): 23498
|
A0A2W6BE99 | MAGPQLPVLQRFADLLVDRAIPGGLLGPREASTIWDRHLLNCAVLTELIPAGSVLIDVGSGAGLPGLVLALIDPTLRVALVEPMARRADFLSAAVNELGCPDRVDVIRGRVPEVLVDPGLAPAAVVTARAVAPLERLVRLALPTVAAGGRLLAIKGAGASGELATARATLRELGAQGWSILSCGRGRLNPPTTVIEIVASRPDWE | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 205
Sequence Mass (Da): 21267
|
A0A1V5CI91 | MIDRILETKRQEVTELRKRRPPGRKKATITPLVFDSPVNIIAELKRKSPSAGFIRDVDPERIHIYSKYAKAISVLTDTTYFGGSYEFLTEVAEQTSLPVLCKDFIIDPVQVDFAYGAGADIVLLIARILDKEELEALYAHARRLGLSCVVELHDREEMAKLADIRPEIIGVNARNLDTMEVDLKRTASMLPDLHSPLRIAESGIKSRQDVERLIAMGANGFLIGETLMRSANPEAVFQELCR | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
EC: 4.1.1.48
Catalytic Activity: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+) = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
Sequence Length: 242
Sequence Mass (Da): 27193
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A0A662RN56 | MDWGNIWHWFTTTFFLAFAALALIGYNIWSRWKVEEILFVVWSVAILFACFGQNRFAAYYAVNVAILCGFLSWKLLEFAAVRAESKEKGEREQGIKIEKGKRKIKRGGERGRKAKKKYNEKKSKEAQRLAAKKFFRADIIFSFIVILLVVFYPLLNESVAKAKLGSGGPGYGWYESLLWMGENTPDPGVDYYALYPEDYTYPESAYSVMSWWDYGHWITYIAHRIPVANPFQQGIGGPYQGNAPGSCVFFIAKNESEANRVLDSLDVRYVISDFKMADAMNSYYNTYGVMTFWANDTAGHYGGYQTEGRITFEIGKEYFNTMVTKLHMFDGREVQFKGGYIGQSSVLLVKPFHAKPLRHYRLVHESPKYMFPHAVLNAATEDMLGWECVSKNYTEAKELAPKLHSGVRDPKNPEVIRWTPSFISPVSYVKVFEYVKGARIEGRAPDGSIVEIATNVTTNQGREFIYSQTTISNGSYKFIVPYSTTGPVEGGTNYDVLATTYKIRAGHIENETIVWDIGKEIEVKEKEVLEGKTIRVDLFADLGIYIMNTDLRE | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: an archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine = an archaeal dolichyl phosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine.
EC: 2.4.99.21
Subcellular Location: Membrane
Sequence Length: 553
Sequence Mass (Da): 63041
Location Topology: Multi-pass membrane protein
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A0A1V5WIR5 | MKIRKRTFGMLSNGRKVSLYTITNRNMSFSVTNYGCIITSIVVPDQQGKPEDIALGYSTLESYIANPVFFGCLVGRFANRIAGGTFSLAGKEYTLDKNDNGNCLHSGSRGYHRMVWKSKPFSNRKEAGVVFYRTSPDGEQGFPGTLDMKIKYALTANNDIVISYSAKTDAPTPVNLTNHTYFNLGGHDSGSILGQTVQLFADRYVPVDGNAIPTGEVLDVAGTPFDFRSPKEIGKDIEAVPGGYDHNWEINRAGDTPNPVAGVYDPVSGRAMTVYSTQPGVQFYTGNFLSGVAGKNGAVYDKNAAFCLETQHFPDSPNQPSFPDSILLPGDRYRHETIWHFDF | Pathway: Carbohydrate metabolism; hexose metabolism.
EC: 5.1.3.3
Catalytic Activity: alpha-D-glucose = beta-D-glucose
Sequence Length: 343
Sequence Mass (Da): 37636
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A0A3S1CAJ4 | MGDIHSATGKLRRAVLQFTPVSWLYVRWLDPNSTTMRILAVWILILAWQMVELNTFFLKHIFFLQPSHMLNLVRLLLICLISAPTIRQYYVYVTDTRCKRVGTQLWVFCAIMLTESIICIKFGLQMFRQTVVSYIFIWLCIQMVGSFVCIYLCAWFAERWNKWKHLGEYADSPIRSLKTSPTNSPSSSPPYETATLAGDSLPSEKVMSDSAEQDDDDILIISTANKNINQSKHQNKREKPKGSWGDASKVGDRDLQAMIPQTKHSTSKSSNSRRRRKQAVDSDGDGEERMGNSGGGGGGGGRGTRLGNQRTERNFGAEDSNHRGESEPEEPDISAQVESLMTGQLLVNGYHHKPSVSPNKKRSSVNKQGQNSTSTKPSTRAKPSGK | Pathway: Lipid metabolism.
Function: Catalyzes a base-exchange reaction in which the polar head group of phosphatidylethanolamine (PE) is replaced by L-serine.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + L-serine = a 1,2-diacyl-sn-glycero-3-phospho-L-serine + ethanolamine
EC: 2.7.8.29
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 386
Sequence Mass (Da): 43279
Location Topology: Multi-pass membrane protein
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A0A3M5DPA5 | MNPSTAARALGIDFGTSNSTVGWWRPEVEPLIELEDGKITLPSVVFFNVEERRPVYGRQALGEYLEGYEGRLMRSLKSLLGSKLLKSETTVLGSALPFKDLLGLFIGQLKARGEAAAGQAFDAVVLGRPVFFVDDDPEADREAQDTLVQVANKLGFKEVSFQYEPIAAAFDYERCIQREELVLIVDIGGGTSDFSLVRLAPRPLQRLIGILACLCCLGYAGLFMVASYDWVKTLFVAGIGAEDLDHFGILQAYIAVVVPVGFGLVLLRYLEILVNLLRGRQLGLGLADEAAEASKLAGEEAGENRP | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 306
Sequence Mass (Da): 33302
Location Topology: Multi-pass membrane protein
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A0A7V1HZP6 | MDKKNIEEGSALNIDFEKRGGLIPAVVQDMRNGLILMLAYVNQEALAETLESGMATFWSTSRNELWTKGKTSGDYLKIKKIFVDCDQDALVYVVEPQGKGACHTKDPESGDSRLSCFYRLVDMESKKQLAHIKDIDKSGS | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
EC: 3.5.4.19
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide
Sequence Length: 140
Sequence Mass (Da): 15623
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A0A933S5C6 | MATTTLEPETAAADMGISEDQIKDITVIGAGPAGLFTVFSAGIQEASCRIIDSMPQVGGQLTALYPEKNIFDVPGFPKVSAKGLVDRLEEQAMQFKPDVHLNETVVDVQRLKHRVLEVTTNKGNVFYSRAVVIAAGIGAFTPRLPDDDLFAPFGEAQGVYTCVTDKSRFAGRDVVILGGGDSAVDWVLGLADIAKSMTVVHRRNEFRAQGHSITKMRELAQEGKVKVITPYNFKAIHADASGHVTGVAAEDKNGQVLEIKCDRLLVLLGFKNDLGPIVEWDLRFEESAIKVDPDMQTNIPGVFAVGDIAAYPQKIKLILTGFADASIAVQNCIPYIRPGKKASHVFTSVRGLPAGGK | Cofactor: Binds 1 FAD per subunit.
EC: 1.18.1.2
Catalytic Activity: H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Length: 357
Sequence Mass (Da): 38433
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D3E0P4 | MIKIKVSEIFTSFQGEGPYIGTPATFLRLYGCNLNCPWCDTDISTYEILSVDEVFEILMTQMEFNNIRILVITGGEPTLQMEELKRLIKEIPDEIKIQIETNGSIFEYVPEIDYVISPKEDKETVFKNYYKYDNVFFKFVICSQEDIDEVIYLKDKYNYDKTIWLQGEFSKDGEMADLIRENFPHLENVKLSVQTHKYLNQR | Cofactor: Binds 1 S-adenosyl-L-methionine per subunit.
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
Function: Catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-carboxy-7-deazaguanine (CDG), a step common to the biosynthetic pathways of all 7-deazapurine-containing compounds.
EC: 4.3.99.3
Catalytic Activity: 6-carboxy-5,6,7,8-tetrahydropterin + H(+) = 7-carboxy-7-deazaguanine + NH4(+)
Sequence Length: 202
Sequence Mass (Da): 23825
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A0A5C0UEY0 | MLTLFTFLQRIKCSMKLLFPIKKSELKLFVPISLLMLLILFNTSIFKTLKDTLMIADKNSGAEVVNFLKIFIVVPLSFLFVFLYSKACNWVDNRVIFYYVIGFFTLFFLIFTLYLYPNKELLHPSPDHIEYLKLLYPRLKWVMPIYGLWTYSLFYSFADLWCSMCLSLLFWQFANQIVSKEDSRRFYGSFAIIGYLGLIFAGYTVKTIFHLERSSVKLNRNIIHDSLFDSQLKWILFITVICNICIIGLYFLITKYVAHDNVKYTVKKSKLSLMSSFKVIFKQKQVMYIMLLVFCYNFSINIVETTWKAQLRKFAYNKSNFILYIGTINQIVGYTTIALGFLSNILFQRYSWLSCAMITPIFAGFTSLLFLTFIGIQYYGIKYIFGISIIAICVFVGIAHNVLSKSGKYVFFDQTKEMAYMSLSDEIKTKGKAAVDVAGSRLSKSLSGQVQALLLILIPNSSQLKIFPYLGIILCFIFLLWFWSLRKLSQTMINVNK | Function: Provides the rickettsial cell with host ATP in exchange for rickettsial ADP. This is an obligate exchange system. This energy acquiring activity is an important component of rickettsial parasitism.
Subcellular Location: Cell membrane
Sequence Length: 497
Sequence Mass (Da): 57768
Location Topology: Multi-pass membrane protein
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W7HS03 | MASPRCIRYLANLSSKPSISSRWRPALLPSRRVQPHQLTRRPTSSAAAPHPPQSLSHSLAKAIENTGPISLIHYMRQCLTGRGGGYYTSSPDQFGPQGDFVTSPEISQLFGEMLGVWIVYEWLSQGKCNGKKVALVELGPGKGTLMDDVLRTISKFKDLAECISGVHLVEASRPLREVQLSRLCGEESRSHWKEIAPSGSAKHIGAPVNWYDDVREVPVGSDEVPFFLAHEFFDALPINAFQNTPDGWRELLVDVKKSPSNLILTTSEVASQEPEFCFTVAPRQTAPARALNNLSPRYEALSTVPDAVVEMCPDSHGIMIHFCKSIHQAGGGAALIIDYGPAETIPVNSLRGIQKHTRVSPFTKPGMVDISADVDFGALVETALRPEFDIEIHGPTEQAQFLLGMGMKERCDQLAATTEDPTQLALLKSGFERLTDRGGLGMGRIYKALAVVPEADGRPVAGFMQPEVTEEAGRAESSVPEAKAEAS | 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
Subcellular Location: Mitochondrion
Sequence Length: 487
Sequence Mass (Da): 52976
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A0A6F9ZZ10 | MRSVPAHENRRRFMSGHAMSLPVMAPDQGRLVVIDAIDGAGKDTVAERLRTYVRKTGRNLVDLDEVARGANAFYFERGDDPRLDGVDAIYVSQPTYVGIGRVIRGEIMKHNAYDVRATAQAYALDRQVLYERTILPFLRARPGRIVLQGRGLMSTLAYQTVQGLTIPELLELPGNRLELSRRPDCAIILEVSTETAVKRLAGRTNKIDDDKFAEEAFQKRVSRRYRDEDLKKVFTKLGTRIEFVDAEDSPDEVAAKCVAYLESVIAT | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
EC: 2.7.4.9
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Length: 267
Sequence Mass (Da): 30015
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A0A7M5UZJ8 | MAIRQRKGKENSSPPSGTSQTSQTSSKKKSGKNKTHQFAIIFGSVVFAVVASYVWSYMKTIRAYTPLNAPKAVELIRDHNDDLHRLWGTYRSHLYFGVRARAPDSLLFGLLWFAQYPQDGQLKVRYSCEQGDNLPKYGWLQHDGSTYGAQEIVDEDFILTTEYIKRPNHGSKGGDWTARVKGKSRNGDKKSIQAVSLMFAVSNEGAGKLTRIVNGERMAEIRGRSPLLGEFKLKFRNPAGSVKLNSYLTTHTDDIYNPKDTIMKKLHYKTKPKSRDQTPLIGLPGDVPNPNGKPNNLFVHQVTLQLPFQIDAVFESEDGDNDRKESLAGDVFAREVKQKRKDFNEHFENTFQLSEKGFTDEQISFAKAAFSNCIGGITYLHGKSKVTSRRLKEPVDYWETGLYTGVPSRSFFPRGFLWDEGFHQIMIQKWDAGITRQILSHWLDLLNQDGWIPREQILGIEARRKVPDEFVVQHNENANPPTFFITIETLIRTEKAEHGHVTPETLKFLKSVFYRLDQWYQWYNKTQTGPLPGAYRWHGRDATTDREYNPKTLTSGLDDYPRASHPSDDERHVDLRCWIALASGILADIADIVGIKSTKYRETESYLKDNQLLDQMHWSDKLKTYADYGNHTKLVKLEWVPVRYEPHAPKRLARVVKSKKGPSPKFVDEFGYVSMFPFLLKILKPDSSKLRILLDDIRSPEKLWTQYGLRSLSRTAPSYNKHNTEHDKPYWRGPIWININFLTCKALHYYAHIEGPHQGHAKMIYEELRHNLVNNVYKQYQKTGYIWEQYDDKTGKGQGCYPFTGWSALINLIMAEKY | Function: Cleaves the distal alpha 1,2-linked glucose residue from the Glc(3)Man(9)GlcNAc(2) oligosaccharide precursor.
Catalytic Activity: H2O + N(4)-(alpha-D-Glc-(1->2)-alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] = beta-D-glucose + N(4)-(alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein]
EC: 3.2.1.106
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 818
Sequence Mass (Da): 94269
Location Topology: Single-pass type II membrane protein
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A0A0G0K2K5 | MSIFIGIEGGEMVGKTSIVAPIYGVLKSAGYEVIKSREPGGTPEAEVIRRDIFKALRENVGAEELAIMFFKARKLHLDQVLIPHLGKNKEKNTIALIDRYASTTRVLQGAEGGVPQIRLRQMEDEYAHNFFPDLTILMYFPENIFEKTFLERKKFAEAAEPGSRSNTLWDEGDVELQLMRQRHYLNLPVFYRETGVNLNFETLDASRPIEVVTKDALGIISRIIKEKSVTGKIGNEI | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
EC: 2.7.4.9
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Length: 237
Sequence Mass (Da): 26801
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A0A1B8P2G8 | MAFDNRRLAELANHDAFLQRHNGPNAEDVAAMLETLDIDSMGSLIDRTVPAGIRLGRELELDPPRSEAEALDYLYRLARQNRVAKSYIGQGYYDTLLPAVIQRNVLENPGWYTAYTPYQPEISQGRLEGLLNFQQMVMDLTGMSLANASLLDEATAAAEAMALCRRANKKAKTNAFFVAEDVFPQTLDVVRTRAHYFDFELIVAPPSNWPSTMSSAPCCNIPATAARSATSLPCWPAPGKRAS | Function: The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
EC: 1.4.4.2
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[glycine-cleavage complex H protein] + glycine + H(+) = (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[glycine-cleavage complex H protein] + CO2
Sequence Length: 243
Sequence Mass (Da): 26841
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A0A328FAF3 | MSNLFRFKFKDPTNPSFMDLGGQTDFFEWALRLFLGCTFVFASWHKIVSPDQFATILYGYAVFPHQIINVLAIVIPFVELVCGITLITGLLKRSGLLLINAMLVGFIFLISFNLIRGHEFDCGCFSLGSTKGLWASVWLLIRDFVMLGAGIYLFRLFDKKDRG | Pathway: One-carbon metabolism; methylamine degradation.
Function: May be specifically involved in the processing, transport, and/or maturation of the MADH beta-subunit.
Subcellular Location: Cell membrane
Sequence Length: 163
Sequence Mass (Da): 18491
Location Topology: Multi-pass membrane protein
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A0A7V8YJK7 | MFDKVEVRSSGLLAVDGVHEVYWEESGNSNGIPALYLHGGPGGTLGAGGYRTKFDPSRFRIIGLDQRGCGRSTPRVTALGYDLSQNTTSILINDIEMVREHLHVDRWLVNGVSWGSTLALAYAQAHPERVRGIVLMAVTTTDRFQVDWITETVGRSESGR | Catalytic Activity: Release of N-terminal proline from a peptide.
EC: 3.4.11.5
Subcellular Location: Cytoplasm
Sequence Length: 160
Sequence Mass (Da): 17575
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A0A7M5WM66 | FTIKQNRKSYLSLYLQFSPIMKKLEISNFGILPSGEIVKKIEFENKNGLKFSVLNYGATAASLICPDKNGKSDDIILGYNNLEGYLENSYFGSTIGRFTNRICKGKFSLDGTDYQLNCNNGSNHLHGGCQGWDKKLWDWKIETDEVEFHLESKDGDECYPGNVNASVCYKLTEDNEVQIRLKATTDQTTLINMTNHAFFNLSGQEKNTKVLDHEMLINSSKYLPVDSTLIPTGEVKDLSKDPVFDFRTKKIIGQDIEEAGGYDHNYCFDDQNDDFRARVFHENSGRQLEIRSSQPGMQFYSGNFLNGHIGKLNNKYDKHCGFALEPQFYPDNINQPSFTSSITKSGETYEQYIIWKISVKN | Pathway: Carbohydrate metabolism; galactose metabolism.
EC: 5.1.3.3
Catalytic Activity: alpha-D-galactose = beta-D-galactose
Sequence Length: 361
Sequence Mass (Da): 41146
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A0A7M5X9F9 | MEKYILASRPWSLSASLIPALLGNILAYKEVSKDFHIWVAILTTLCIICVHIAGNFINTYYDFINGVDGPKSADLTLVTNILLPSVVWNLSISCYLLSLLFFFVLLCICNVTFDIVLLFTFGVGLSFLYTGGLQLKYAAMGDLVIILTFGPIAVLFAFVSQTYIFSLQPLVLSLPIICLTEAILHANNYRDYDEDQQKQIKTLAMILGKPFSTIFYLALTTMPFVWTFRMGCFVNKAFFLPLVLIPNMLSLQRKCMNGDLEMLDQLTAQMHLLYGALYLYAVIYSF | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis.
Subcellular Location: Membrane
Sequence Length: 286
Sequence Mass (Da): 32244
Location Topology: Multi-pass membrane protein
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A0A2H0Y2Q2 | MNFVLLGIQGCGKGTQGRTLVEKYHFRFLEMGARLRELAKREDAYGSFVRENLKQGNLLPNQDIIRIIEEFVLTKPEQPFVLDGAPRMLPQKLLFDQLMRRVDQDFKVLFLNLDPAKALDRINQRRICKKCKATYAPDYTLNTCQKKWGNVICGGELTQRVDDINIKAIQNRIHNFQTLTLPVIELYQQENKLLEINADQSMEAVTQEIEKKIKIYL | Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1.
Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
EC: 2.7.4.3
Subcellular Location: Cytoplasm
Sequence Length: 217
Domain: Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.
Sequence Mass (Da): 25228
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A0A1H8ZRU1 | METSTNTEPGAVPGNTTAAPVTHESTAAEAGHHAAFPPFDASTFPSQILWLVITFIALYIVMSRVALPRVGKVIEDRQDRLQKDFAEAARLKQESDAAVAAYEQSLADARRRAQTIAQEARDQAKAASEADRKRAEGDLAGRLEVAEARIAEIKGRALGDVDAIARDATEALVSVLIGGNITAEEAKRAVASSAAKGSGA | Function: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). The b'-subunit is a diverged and duplicated form of b found in plants and photosynthetic bacteria.
Subcellular Location: Cell inner membrane
Sequence Length: 200
Sequence Mass (Da): 21050
Location Topology: Single-pass membrane protein
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A0A4Y6U6D5 | MKPVASPAPTISRRLLGHTPKRVVARLLAGVSQRHWQVAGLVLRPLLLALLAGRLLQGRESLRSLKERLGWGGGKSLLAQGDGPLLWCHGASVGEVTALLPILDTLLGAHPTLNVLVTTATLNGQACAERALGHHNNPAPNAACHKACRHKAGKRFHTALAPWDVASWVGRFLRHWHPSALLLVENEIWPTTLGMVQAHNVPVLMVNARLSARSAKRWSWLPGLISPALAAMAWVQPATQPSSHRLRSLGAGRLLPAFNLKAHMPPPPAAPEQRAFFKRACAGRHVIVALSTHGGEEVLLARAAAWAAGLKKGNPQALKLLLVLVPRHPKRGPALAKALQAPLHSRHEVPKPDQNLWIVDSMGQTGAILRAAQAVIMGNTWTPQGQGHNVHEPLSLGLPVLVGPWLGAWGEVLDPWPPNLHQVGGAWVHGDTARSNSANRKGSSPFLKGLAHFMLHPPAPQAADPLVGAEKGPGVGALCRLIMGTIQH | 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-3-deoxy-beta-D-manno-octulosonate + lipid IVA (E. coli) = alpha-Kdo-(2->6)-lipid IVA (E. coli) + CMP + H(+)
EC: 2.4.99.12
Subcellular Location: Cell membrane
Sequence Length: 488
Sequence Mass (Da): 52148
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A0A1V4L0A1 | MTPAECRLLRRLGADAVGMSTVGEATAARHLGLRVLGLSLITNMAAGGGASDDEEEEEAERVGPEVATPNEHAAVLEAAEGAAVLIRDLLVALAPLLANRDAPPKGAGP | Pathway: Purine metabolism; purine nucleoside salvage.
EC: 2.4.2.1
Catalytic Activity: 2'-deoxyguanosine + phosphate = 2-deoxy-alpha-D-ribose 1-phosphate + guanine
Sequence Length: 109
Sequence Mass (Da): 11046
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A0A7M6DM40 | MYNICCFVPWLALVIQLTMQPIHGIPMGNMKEHVGGGLENVQFYNEMLPDEIKSHLNGDVYEEEKEEDSLNNFNDDTNLDIQHAPLKKLENKRWPNGVVPYVIMSKEYTNEEKRLIRAGLRDIEAVAPCIRFVEYSDGDPNCPNTHVQVFKGLGCWSLIGRTASGKAQKLALDYYCITEDKGVIMHEFLHVLGFYHEQARPDRDEYIRIFWDRLSDGAEPQFRKTERTDDLGVAYDPVSIMHYPNTAYAKEYGTITMEWKANPKQVLGGDKLSSKDILQLNRLYCDGGKVVTTTKKPNPTTITTKKPTTTTIPITTTTTSTTTTTTTTTPTTTTTTTQKPTTTKKPKTTKQSTTTTITTETPTTTKKTTPITTKPTKKVCGDYYGLSCMNARPGRCSQWMKIRCPRSCNVCTGPLSETCMNIRNNWSNKYCQTMADKGRCQSSNYWTRYQMKTQCTKTCCQRNELYTFRGQRG | Cofactor: Binds 1 zinc ion per subunit.
Function: Metalloprotease.
EC: 3.4.24.-
Sequence Length: 473
Sequence Mass (Da): 53728
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A0A3M1Y9C3 | MSSKERKKKKINIEAVIFPLFQNNNDLSGLPEEVSATVEMLFKEKIFTAELNKTYPIALPGRKNLLLLLTGLGEREKINNERLRQAGGSAGSFCKEKQIPFIKVELSNLKGILPSPVSFLEGLFLSTYSFSRYLSDKEPYSPTVTVSGIKAGLKKQIPEIKAITDSVHLARDLVNTPSNELTPEKLASRARQLGTKNIKVKVLTERQIEKEGMGAYLAVSRGSKNPPRFIVIEYRGGKKGPVVFIGKSITFDSGGISIKPSSGMEKMKYDMAGGAAVLSAVSAAAKLSLPVHIIGILPAAENMPGGNATRPGDIVSTLSGKTIEIANTDAEGRLALADAIEYAKRYDPDFIVDIATLTGACSVALGNEAAAAMSNSEELIKRAVRASEQTGEKLWPMPLYEEYRDYLKSDVADIRNVSTDRSGSLVTAACFLKDFVEDVPWLHIDIASVAWTDRDRPYIPKGATGFGVRLLIQLLKESYKL | Cofactor: Binds 2 manganese ions per subunit.
Function: Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
EC: 3.4.11.1
Catalytic Activity: Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.
Subcellular Location: Cytoplasm
Sequence Length: 481
Sequence Mass (Da): 52417
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V5RH68 | MDEIIKDLNKKETNNKFSLFLKNNFNKRIAMRRVQKFGGWLSSMIMPIIGLMIAWGLLTAFFIEKGWTPVAIIEEYIVGNVIKYLIPVLIGFNAGRIVHKDRGGFIAAFVVFAVVLGNEYNPGFAENSTSSPQFLSAMIVGPASAGILLGIDKLLDGKVKQGFEMLVNNFVMGFLAFGLGIGAFYGMPYVFNSITWALGELVRLLINNKLIFLSALIVEPAKIFFLNNAINHGVFTALSQDLYRQYGKSILYLLEANPGPGLGALLTIIIFDKKQRGNAAGASVIHFFGGVHEVYFPFILMKIEMLIALIAGGLVGDAIFQIFDAGLIAPASPGSIIAISIFIASGAMNYVGVFLGVFAACATTLLVGSLIHIIMRRKYKSKELSYEEAVDKVNDLKGKESKYLKPNSEHGVSLPNIEDVKTIIFACEAGMGSSAMGASVLRKKLKENKIEVEVINLPVKELPSDAMFVITQEQLTDFAKQKAPNAIHKSITNFLDKNFYDKIILDFNKKI | Catalytic Activity: D-mannitol(out) + N(pros)-phospho-L-histidyl-[protein] = D-mannitol 1-phosphate(in) + L-histidyl-[protein]
EC: 2.7.1.197
Subcellular Location: Membrane
Sequence Length: 511
Sequence Mass (Da): 56107
Location Topology: Multi-pass membrane protein
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A0A7V9BQ04 | AHTVRRFGGVAGDVLGAASELSVTAVLVVLAFGP | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.
Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
Catalytic Activity: adenosylcob(III)inamide-GDP + alpha-ribazole 5'-phosphate = adenosylcob(III)alamin 5'-phosphate + GMP + H(+)
EC: 2.7.8.26
Subcellular Location: Membrane
Sequence Length: 34
Sequence Mass (Da): 3338
Location Topology: Multi-pass membrane protein
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A0A0S7XEI0 | MVELIVVFVIGLAVGSFLNACIYRVPRKISLLSPPSHCPACKSAISARENIPLVSFILLKGKCKHCGAAIHWRYPLVELLGGALLLLTYLRFGFSFGLFFYYSFVCALLVVTFIDHELRVIPDRINLSFMLIGLGGGVLSQLRVVSGLNVDIIPSLLGIVIGGGSLTLVAYLYLKVTGVEGMGGGDVKLAAMIGAFLGWKAVLMVIFIAAAGGSVLGLALVFIFRMSRRTPIPFGSFMAPAGILVLFCESRLLELFSSLSAVRAG | 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 release an N-terminal, basic peptide of 5-8 residues from type IV prepilin, and then N-methylates the new N-terminal amino group, the methyl donor being S-adenosyl-L-methionine.
EC: 2.1.1.-
Subcellular Location: Cell inner membrane
Sequence Length: 265
Sequence Mass (Da): 28345
Location Topology: Multi-pass membrane protein
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A0A7M5UZE4 | MVTFMLFLMIVKVGVFCRPAINKRNFTSAFDQIQWNNEHILNSEDSEDLFEDDIVKSPAIDEIINRKITSPGRQRRDVITGPYAWPNGKVPYVFADDYPEFSKFWVRSSMDEIQKVSCVQFIERTDEKDYIKIVNGTQCYSSIGRRGSNQTLSLGDNCLSDSIIQHELLHALGFFHEQSRLERDYFVTVHWDNIIKGKEHNFEKYGLGEASHLDEHYDTKSLMHYSNYIFAVNESKMTISSKSNASESLGGFEMTDTDVRQLNKFYSCPCADHMFGCEFITSMCGQFRTQQYCQKSCGFCHTSENPPMSSTVSSLTTTMSNNTTTSYTTGRSLPTTKVIPTATTTIQTKTTITTIVSSTRAVITQTTPPETTTTISTPTTAVQSTATALPTTTSTTRGVGNNTCLDMNPCCTELATHGLCNKSEYIRSICNKSCNKECSGSNSTELLATTRSSFFGDEPPTPSKAITLFAPFSSLFLSLLVNVLWRFGYT | Cofactor: Binds 1 zinc ion per subunit.
Function: Metalloprotease.
EC: 3.4.24.-
Sequence Length: 490
Sequence Mass (Da): 54836
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A0A2N2ARK9 | MSETTNPIVKIEMENGQTMEVELYPEVAPITVENFLTLVNDGFYNGLIFHRVIPGFMIQGGCPQGS | 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: 66
Sequence Mass (Da): 7318
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H0ADH6 | MEISAENFRDKAYQNRFVFPVIAIFVLAVGLRYYPARNMEFLQASDPYNLMRMSQQIAYEGSRPALDFMRWFPYATPSYITHVGNIVVPAFIYRLGGFLFFENYLSYAKFIIPVFAGLSSVGMYFLGKEVYDKYTGLAAAFFLAVIPGVMYRSSAGFFEKEPIGTMFMVFSLLFFTKAWKSTSWIYGILSGLALGLFTISWGGSQMLWLLYPMIIGFMLLIDQDIEKLLAAYTPTILIAGAFGSIFNPGNFWFTNTLFLMALGFAALLWVRYLVEELELVSESRLPYFMPSIYGTGAALMLLSPLYSQTLANIMFSIYSTATQSGSSVIGGTVAENASAQLNQIVTQLGSGVVDQIIPELGLLTSTTGTWTLVFLAVPLMLTSTILMIGKRYGIIEQLSGRENYSLTAGIIAAWAIGFAVFFSGYRAIGIGLSLSLSVLAFLMVYYMDEEASFSISSMALIFTAVLMTLLAFRGQNTAALLKGIAYPIWISSIGLGIIYYLEDFKPTEIELEWYKIIPLFWIVTNVLGATARSRIIYLAAFPVALGAGYTFSKVLNRMRNLDLSAIEFKASNVRMIGIVLLVVSAISVNFVAGFAATQGISGSPNEAWMQSLDYLNEDAPNGSVTMSWWDYGYQFQSLGRTASVADGGNFGYYSDEEPINYPLAEYFTSTNTSDHQEFLEKHSVDYMVLDNTMIGKYQAVSQISRRDNSNYFAMSQAYTSGSLEDSVSEQGNRTVATFTRGPSGAPIIDQEPNDPTTFARGYAQIFVPFEQSNTSIDISEPATIRYSNGEEEEVNCVLTDEGVETFGDERTDYCIAEDPYYNFERSSQGTQARVVLVPETLIDHTINRLYFMDGHEIPYAEKVAEGSNDYIKMWEIE | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: an archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine = an archaeal dolichyl phosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine.
EC: 2.4.99.21
Subcellular Location: Membrane
Sequence Length: 877
Sequence Mass (Da): 97656
Location Topology: Multi-pass membrane protein
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A0A352PJ33 | MTTVPASVSENCRVHGLQLLRQGKVRDTYSLPDHPGHLLVVATDRVSIFDHVLAAE | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.
EC: 6.3.2.6
Catalytic Activity: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP + L-aspartate = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate + ADP + 2 H(+) + phosphate
Sequence Length: 56
Sequence Mass (Da): 6151
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C5LF88 | MPRSVDVIVRGDICERVKPGDKIQAVGSMICVPDVPAMMKPGEMATAVKREQTKRFATEMSAGNEGISGLKQLGVRELTHKISFLATYVESDSQWKGGDLRTPEVMMRGGDGGEYPEIQEAMTILMEQAEHRDRLREISEHADPFTRLAKAIAPGVCGQEDVKKGILLQLIGGVPKVTRKEGMKLRGDINVCIVGDPSTAKSQFLKWVSDFLPRAVYASGKASTAAGLTAGVARDPESNDVIIEPGALMLSDNGVCCIDEFDKMDAKDQVAIHEAMEQQTISISKAGIQATMNARASILAAANPKWGRYNLAAGLQQNVDISQPLMSRFDLFYVLIDAPDLEDDRQIAQHLLKTHVRGSRGRLVIAGVLFYHPLEGSGENADVTATDLRLYINEARKIQPRITERARVLIVKYYVKLREAEKGMFKRAYRVTVRQLESLVRLSEAVARVFWSKEVKGTHVELAYQLVRGSIRKIDQTDVEIGDDGEADDEELPDQDGECILNQLTEFGMLLFRGCGYAGGSPKAKGSTRSDKSCLIFCHLILFQRISFAEYEQIARSLAWYLDHREQLGQTTTEEELSNWYLEQLESQLHSEEEMDRFTAIVTMVIKRLVDVDKILCVIRESPDKDKPEQRTLTKHPNFVVGEHVSQMMASDVAPAEGDSA | Function: Acts as component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
EC: 3.6.4.12
Subcellular Location: Nucleus
Sequence Length: 661
Sequence Mass (Da): 73477
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C5KAM2 | MVIPIPALPRDNAEPTDFAKEARPVMVILIVLQLTLGSCRLYTLDIFGGVWTIVLACFGIWAYAGSRGPYMNDVMFWGLLTFFCMWIFDLIMFLERVFKNHTPLFISSSPNEGSSFNFTAFQGLIGHRGTRMIVFGSGRDIAQSPWLEITCEEDIYAAPVEHALFGGDEHLKAHTSGHSLPNGLTQRDRLDSLVKTYAAMVRAFEEVGLDVFLESSCLIGYVRHNGNPIPWDMDIDIGLLQDDCRRVFPGGNAEMYHRISALLGPEYSVDKMGCDCGDSCEGDDGRMVGHVADKVTGFGVDIFSYATVTPDDLRPWQQQDGGRWLERVKDRDDYTFPEEALLPLQRATFAGFLIMHRDPTPIVAALSTVLLSTLGALGINSYVPNAYMDEIFHVPQTQAYCSGHLKEWDDHITTLPGLYFWAAVDMHRLLAVIASLWTYILTALGFIAFLLYNGSIVVGHKENHVASWHWAQIPYLILTVTFFMGPLGWLSTIRSVINGGPLRPIMDTGVMTVSYLMLRFGTIVHPFLLADNRHFTFYLWRHLLRHSTFRIGVLPLAVMVIVRGIGNSGWAVRFFHKTENKIAAVVFALCCVLALVPSPLLELRYFNIPALGVLLVYVDCEDNATKLCATAAWMALINTFDNQRKDYKDTFREGEFDV | Catalytic Activity: a dolichyl beta-D-glucosyl phosphate + alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol = a dolichyl phosphate + alpha-D-Glc-(1->2)-alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + H(+)
EC: 2.4.1.256
Subcellular Location: Membrane
Sequence Length: 658
Sequence Mass (Da): 73873
Location Topology: Multi-pass membrane protein
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A0A2N2E577 | MERENNWSNITLEEIRSILYASNEGEAQKIIVQMQQDKRKGTQIIIAQYKKWLEKEHIEKERIHKLWQLERNLKTAGFKFIAGIDEVGRGPLAGPVVAACVILPHELELPGLNDSKQIVAKERKILSEIIKRKAVAWGIGVVDHQEVDRINILQATKKAMVEAVKLIGQQPDYLLIDALKIPVAIPQDAVVHGDTLSASIAAASIVAKTYRDSLMEMMDVLYPEYGFKEHKGYGTARHREALVRYGSCPIHRTSFLQNII | 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.
Subcellular Location: Cytoplasm
Sequence Length: 260
Sequence Mass (Da): 29382
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A0A7M5XFS2 | MYNQLVNEKCGAWKCEREMGSGGFGSVTAWINQTNGDKMVIKQCKSALNERNRERWLEEIHLMNTIKHKNVVSGRKVPEEIDKFIRGPEKLLGLEFCESDLRKLLGRRIHCCGLREQSVLDVLRDVSCGLQFLHKQPIIHRDLKPENILLSQQTNKTVFKITDLGYAKVMDANSIAMSFVGTIQYLAPELYDRNSGYKYTADFWSLGTLIFECITGHRPFVVPNKAYDWPKYMRQKSDDHIWGAYDEHTQSMNYYRDIPTPNQLSKPLVDAFCEWLKLVLRFDAKHRGNKQIQTHDGHQMLECFYEIQQILHKRIINVFEVLKCQKHSYVLRPGDTGSTLKMFLLNELSIEMEDQLIVFPNHFKLLDDNASLAEQCSDIVQEVFLFDTSAEAKFEISSAMLDKVRELLGNPEEKRKGSELRSYWAQSLFYCLSKANDYAMLLKSQKALLNNIQKRWEHLQHQKELLQRTAIKLEATVDMFKLSYECDRTNRPETYGKAGHDCLHEWGILYNKIENITSHTQLDVLYAVVEQKKEKIKAGLQSTSQSNRNPLEDIASQVGDKYDRLREKIRDIKMKDFLHDSTAISNMLWNCVAKRDTLYTEFYRGLRKALVLDKEISQAVTEVQNRIHAINNDIAKVQSYQKARQCILWKLLASNAAISSLDGSIPFSSLPDLLEESLTVKIPQESPKPIEMDMKFRSAMSNLDQLIGSARPKTSPKRSFTIDSASLSPTEFDVKFQQQHNDKRRQSEPVHLSASQSDNGVFNFDTSPARTNQPFTDFNTPSAHIPHINRPLLVQTDRVPHLHHESTQRYPTTHQPVPNNQFHGNRHPISVSPHNRRNDPNVSLTVTQGQLPATAIPSPRSSPRPHAGALQTSQHVQNFTIGGSVVKMTGSSTVPTNNQTFGTNDDKTNQSLSPRR | Catalytic Activity: ATP + L-seryl-[I-kappa-B protein] = ADP + H(+) + O-phospho-L-seryl-[I-kappa-B protein]
EC: 2.7.11.10
Subcellular Location: Cytoplasm
Sequence Length: 916
Sequence Mass (Da): 104951
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C5L7S4 | MDAKEKRQTLFPGIKATKWTNDITFLTHVEPLPIYRRLDEQSNLVCNGTLPFTNDQALHILDIMIRINAYDQVLYDVQRQGRITFYMTNFGEEATQIGVVAALKEQDMIWPQYRELGVFLYRGFTTQQVTDQCMSTMYDQGKGRQMPVHYCYPEGNIQAVSSPLGVNIPHASGAGYSFKLDNADRCAVTFFGDGAASEGDFATAINFASLMKSQTIFVCRNNGYAISTPVSEQYTGDGIAIRGIAYGIHSLRVDGNDVIAVYEATKRAREITISGEGPVLLELMTYRRGHHSTSDDSSRYRPDAEVQSWLLDGIDPISRYYNLLVNMGLITKEEFLNLGKKYRAEVLDCLKVSAKHKKAPIIDMFNDVYDNMPWNLREQ | Function: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
EC: 1.2.4.4
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] + 3-methyl-2-oxobutanoate + H(+) = (R)-N(6)-(S(8)-2-methylpropanoyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] + CO2
Sequence Length: 379
Sequence Mass (Da): 42818
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D8WYF6 | AFPRMNNMSFWMLPPSLTLLISGSMIDSGAGTGWTVYPPLSSNLFHSSMSVDMTIFSLHLAGISSILGAINFITTIINMRTNEMKLDQMALFVWAVLITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIISNESGKNESFGSLGMIYAMMTIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFS | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Membrane
Sequence Length: 230
Sequence Mass (Da): 25216
Location Topology: Multi-pass membrane protein
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A0A7E4UZJ9 | MLRRNHHPAAHRVIAINIPKERDTVPDYFNTFSEISTALGANCKKSYHDYDHQKRCVDRFFELIQSGERMNMFLHDYKGGYLAEDCGSSVSYDPSKDTHPFIFHLMPHSDVFVYFSHKTISVPPLRWIEESHNHGKVVLGTVLFENNTGEHTTLLANDTSLNERLDHYGQILADLMEAKCFDGYLINVEVKLTLPEINNLLKFIDILKSKIRLTCQFEPIIVWYDAVTVKGDLVWQDAVTEKNNIFFEKCGFILLNYCWKAKELQKTDQIVPTDAKNRVFVGIDVFGRNTIYAAGNKGCADALAMIQEHDFSAGIFAPAYQRECLLHPQDSGITSGYEYWEPVFPYLHYRPFIFAGTFSIGRYFKKCLSEVGSPKQLEYIRNHVFPVCPPTQDGFKCYENGLRFSKAGQYLLQTVEFTETSKCYLILKWFKGELEFQNTSGYFRFTKGKEVHTLQFPAGITKIFFHADSEDFFGGFEITRCDILDSQGIVPRTDDRKIQIARLLP | Catalytic Activity: an N(4)-(oligosaccharide-(1->3)-[oligosaccharide-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl-[protein] + H2O = an oligosaccharide-(1->3)-[oligosaccharide-(1->6)]-beta-D-Man-(1->4)-D-GlcNAc + N(4)-(N-acetyl-beta-D-glucosaminyl)-L-asparaginyl-[protein]
EC: 3.2.1.96
Subcellular Location: Cytoplasm
Sequence Length: 505
Sequence Mass (Da): 58160
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A0A2M7QDJ8 | MMNLEVKNFPGKGDALIYFIAKEKLKNDAKLKQLDALTKGALSQKIKLHLFEAGADEMVSIEMVSPYKHIVLYGLGKTSSVTQATLRNAVANAVRFSETLRASSATFFYQEEFKHIPLFDLGKSLGIGASMGNYHFDKFKGKETLKKAHRLSHICIYIEKAIPKELQEGLAFGELIAKGMQTASNLVNEPASHIHPIELAELATKIADSSKEKISVQILEKAECKKLGMGAFLGVAQGSIQDPKFILLKYSPTTHDKRLKAKKICLVGKSITFDSGGLSLKPPGSMEDMKTDMTGGATVLGIFQVLATNPFSPHEVWGVLPACENMVSGGSMRPGDIVTALNGKTIEVLNTDAEGRLALADAVSYAEKYIKPDIMIDIATLTGACMVALGKDISGIFGNDKSFIKQFLEIAKIEGEEMWELPLYKPYAKFLKSDIADLKNIANAGGGGAITAALFIAEFVNKTKWLHIDIAGPSFRDKPSNGVVVKGGNGVGVASIINLLKNSKPYNP | Cofactor: Binds 2 manganese ions per subunit.
Function: Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
EC: 3.4.11.1
Catalytic Activity: Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.
Subcellular Location: Cytoplasm
Sequence Length: 508
Sequence Mass (Da): 54943
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A0A7E4VXK7 | MLSFPEVNSSADLEQGEMQAAKWTAPDGEILYLRYAYTYPIETAIWEPYLIHRLFTTYWWICFIITGVYIATIYGLRQWMRDRKPFELRWPLVAWNAFLAVFSTVASIRFGEEALYVLLHASERQGICYSIDPAGPAALWAFLFAISKVAELVDTIFIVLRKRPLIFLHWYHHAVVLVYSWHAATELTAAGRYFIFMNYCVHSIMYTYYALVSYGFRVPRRIAAAVTILQTAQMLIGVLLSCRVAYIKFAKPELACQQSVENLAICFFIYLTFAVLFTHYFYQSYIDGEKSRSRTAKEAATKKIE | Pathway: Lipid metabolism; fatty acid biosynthesis.
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: 305
Sequence Mass (Da): 35370
Location Topology: Multi-pass membrane protein
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A0A3P7VUK5 | MLAIEEGKFHDIVVAGIHEDYYSLSLKTYAMLYFKDMRVPSAKCLVKADSDNVLVVRNYERLCEETSMVLQRSRTKWKVPESIYPHPQFPMYCSTGTYMLCGKVPQNYRELKTHLRMLPEDALFTGIFAEKAGIRRKHVGGMSFIDAPEYICRESKHTYSIHMNRAKDPQRYFQRLISMEGFPCRLS | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 187
Sequence Mass (Da): 21835
Location Topology: Single-pass type II membrane protein
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A0A1V4J5M4 | MQHHSNPERLAVVPVALGAAALSAALLLFPREDERPAAAAAEEIVDTFFIGRFVLLAVMSLVLLGCLFLLLVYHLMEPVLAKPLRSR | Function: May be involved in ciliary biogenesis or function.
Subcellular Location: Cell projection
Sequence Length: 87
Sequence Mass (Da): 9491
Location Topology: Multi-pass membrane protein
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A0A8J3B701 | MTRHRLFYMALILILAIVLLFGVWFVMWWTLQQPKAHPLAGQAKPDESAEELLKRTLDTPEIVTNLYSGNFIRIQFKLVLDSKKTREELETRMFQVEHAAIALLSSLTPDDIRGERGLRNVEEKLKARINALLPTGRVERVITTKKMVQ | Function: Controls the rotational direction of flagella during chemotaxis.
Subcellular Location: Cell membrane
Sequence Length: 149
Sequence Mass (Da): 17226
Location Topology: Single-pass membrane protein
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A0A1J5WQM4 | MILFVTVGTTKFELLIERILSGVFFDVLHRRNYRQIIVQYGGGSFNHRLFLDLGRKHGVIAEAFPFTNNIGKYIESAYCVISHCGSGTVFEVLRSSNKPFLVAIANEALLDNHQQELADELKHGEYCHVSTLSQLHGCFSSEAYQRKYKELPAPQPGFLLAEIEGLFF | Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway.
Catalytic Activity: N-acetyl-alpha-D-glucosaminyl-diphosphodolichol + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N,N'-diacetylchitobiosyl diphosphodolichol + UDP
EC: 2.4.1.141
Subcellular Location: Endoplasmic reticulum
Sequence Length: 168
Sequence Mass (Da): 19001
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A0A1V4K346 | MNSLTLNRHTEILEILEIPQLMDTCVRNGYYEEALELAAYVHRLEKKHSSIPVIQSIVDELRTNVQLPACLRIISYLRRMDVFTEAELRIKFLQARDAWLRSIQAAIPDDDPYFHITKTIEACRVHLFDIVTQYRAIFSDEEPLVPAEGQALNEGAIFHGWVLQKVSEFLRTLEHDLQRGVGARLDSLLGQCMYFGLSFSRVGADFRGQLAPLFQRVAAAAFAKAVEETVEKFQEEMNSYTLISAPAVLGSSAAVPVPAAQPGTLQPPMVLLDFPPLACFLNGLLVAFNDLRLCCPIALAQDVTACLENALREVTKTILAFHRAEEAAFSGREQELFVQFCTAFLEDLLPYLNRCLQVLFPPAQIAQALGVPPTQLQRFGRLGCIDLAAALAAGLRRGPCLGLSAPQLGVPLRVFATELTPARCEQYPPPLRRAHRIEPFQLRLLVNPVLRVLDSRLVTGPEGCASLHGFSAYVPRHWAVHVSGVDECGKPVSWEATGWAARIVQHEIDHLDGILYIDRMDPRTFTNVSWMELMD | EC: 3.5.1.88
Subcellular Location: Membrane
Sequence Length: 535
Sequence Mass (Da): 59731
Location Topology: Peripheral membrane protein
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A0A1R1Y8C0 | MVLNELGSKINDVLASLSKAPVIDQKVLDSLLKDICAALLNSDVNIKLVYNLKENVKKTVDLDKLAAGANKKKIIQNAVFDELCNLVDPGKQAWQPKKKAFNVIMTVGLQGSGKTTSCTKLANYYHRRGWKTALVCADTFRAGAFDQLKQNATKAHIPYYGSYSEADPAQIAAEGVAKFKEKKFELVIVDTSGRHKQESALFDEMKQIHKEINPDNVIFVMDGTIGQAAEAQATAFKESVDVGSIILTKMDGHAKGGGAVSAIAATKSPIIFIGTGEHIHDIEKFSARSFVSKMLGMGDISGLVETVQSLKLDDNQDLMKNISQGIFTLKDMRDQFDMIMKMGPLNKIAGMIPGIPPEILSGLGEDDGSKQMKQFMCIFDSMTEKELYSDGKIFEKEPSRIERVAIGSGTSRALLMAMLDRHKMFGGFVKKMGANKGLLKNMAPGAAGMDPSSMSPSQMSRMQQQMSKMMNPQMMQAMKMMKQMMGGGMGGMQDMINQMMGGGRR | Function: Signal-recognition-particle (SRP) assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum (ER) membrane. SRP is required for the cotranslational protein translocation for ER import and preferentially recognizes strongly hydrophobic signal sequences. It is involved in targeting the nascent chain-ribosome (RNC) complex to the ER and is proposed to participate in the arrest of nascent chain elongation during membrane targeting. SRP54 binds to the signal sequence of presecretory protein when they emerge from the ribosomes. SRP54 interacts with the scR1 RNA and mediates the association of the resulting SRP-RNC complex with the signal recognition particle receptor (SR) via its alpha subunit SRP101. Both, SRP54 and SRP101, are locked in their GTP bound forms in the SRP-RNC-SR complex, which dissociates upon transferring the signal sequence to the protein-conducting channel (translocon). After signal sequence transfer, SRP54 and SRP101 act as reciprocal GTPase-activating proteins (GAPs), thereby resolving their association.
Subcellular Location: Cytoplasm
Sequence Length: 505
Domain: The M domain binds the 7SL RNA and the signal sequence of presecretory proteins.
Sequence Mass (Da): 55176
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A0A146K732 | PKFGKQQPQQQIEMTNMMLQPTQPSFLQQQQVISPKPVDEQPDISPVTDKSKRKCRDLICLIIFTAFWGLCAFIIVYFELWNNTANLTLILEPHDYMRRRCGKGAADQKDPLATDYSTILASTDQFNQFCELAKTVYVVEMANDAPVRDADCAVMGQSGTANMATSRQFFAAMSKYGTDQTASDTGITFDGTTVCIPESAVQADTTNLVCNPPSNAIYVCTEDAAKWLAATGYAGPAVGTFLTQAEYDSSYGALPNNRKFIQNMCKKLPDTELVNSKRVDFSRDLIATTLNIKTCSKTSINIDAAVQVFDISTYVADFSRNFIGEITNMYTWILAGIGGGIGAMIVYLLLIRFLVSVLVWVCILAFVGASGGGAIYLLLQWKQMVDANQYKYEYFGFMDQALSQQSQLYYGLGITLAVICGLSLLIVLICCKTIRIAVNVFKQSMVCIGKIPIIFVFPIFTIIMVVIHLAWSVAAAYMQYLTGSYDSTINAFSFETVTRDLDYQVVRQWDYVGSTYFVVLVFGAIWGIFFFYNMLEFNISMMVVQWYFNRQRTFKSMKGATKRSIVAGMKQMGTIVVTSFITSLVVLIRFIFEYVLKRMERAGKIGSSKVVKGAIWFMRCCLKCLQKIVQWINRNVQIYAAISGEGYCKSMRQAMKLLMAKIFAAGFTKMLSTFFLFIGKLIVTVVGICIAGYGAYTVDSQIHFGPPVVAAIVCYLLSYYVIEIIGLVIDTIYFCFLYEDTMMLREREQGMKSWAPDGLASLLEK | Function: Choline transporter.
Subcellular Location: Cell membrane
Sequence Length: 765
Sequence Mass (Da): 85683
Location Topology: Multi-pass membrane protein
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A0A1G1N9G4 | MKISIRNLSSQALPISYGAAKKLIRKILPCLGKSKQPEEWLLGIVFLNDTRIKLLNQKYLKANRPTDVLVFNYGQNTADLAISLESAKRNAKFYKASLKKELVRYIIHGLLHLYGYDDRSPKDKKIMFKHQEQILNQIIHVNSR | 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: 144
Sequence Mass (Da): 16651
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A0A4R4DXV4 | MKARPAKAPPLPAHPGVTVLEDEVVWDGRFPLQRVRFTYTRFDGRPSGELTWELWRRHAGVAVLPYDPAADAVALIEQFRLPALAAGIDPVMIECPAGLREPGEAPEAVARRETREETGLQPDRFEPICRTMLMQGGSDELMHYFVARVRLPRPDQAGEHGLVEEQENTRVIVVPAEAAFAMLDANRIMNATTMICLWWLRHHRARLRRDWA | 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: 212
Sequence Mass (Da): 24048
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A0A6I5NBU1 | MGQRTDESSPATTAGRPASATANASRRRSMASRTMIRAIRWYQRRVSAGRPACCKYYPSCSNYALTAIRRFGAVRGGTLAALRLLRCRPWSDGGIDDVPRRFSVFYRFSWSRAHEAPRLTPLPKDEEGEDVPNE | Function: Could be involved in insertion of integral membrane proteins into the membrane.
Subcellular Location: Cell membrane
Sequence Length: 134
Sequence Mass (Da): 15055
Location Topology: Peripheral membrane protein
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A0A067MK75 | MPILDKIKEKLHLQKDSTKDSTKDTTKEPAQESATTAATAAPAGPVFDQSKVDVIFVLGGPGAGKGTQCAKIVQDFDFAHLSAGDLLRAEQAREGSPYGELIRTHIREGRIVPMEVTVKLLENAMAAIIAENRTANGWGDGRGRFLVDGFPREMDQGLKFENEVCVSRFVLFFTCTEEVMLDRLLERGKTSGREDDNAESIKKRFRTYQEVTMPVIEHYRKQDKVREVDATSSVEEVHAKVKETLEPLFGLKKD | Cofactor: Binds 1 Mg(2+) ion per monomer.
Function: Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and dUMP as phosphate acceptors, but can also use CMP, dCMP and AMP.
EC: 2.7.4.14
Catalytic Activity: ATP + UMP = ADP + UDP
Subcellular Location: Cytoplasm
Sequence Length: 254
Domain: Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.
Sequence Mass (Da): 28315
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A0A813BZF8 | MAFHDPADDDRIPVFRVMDESGMLREGVEGFGEDREDVTNMYTTMLRIHQLDTIFYEAQRQGRISFYMTANGEESIHVGAALGFNNDDPVYAQYREAGLLLMRGFTLQQFADQCCSNEDDGGKGRQMPVHYGSPEHHFYTISSPLTTQLPQAAGTGYAMKMEGKGRCCAVFFGEGAASEGDFHAGMNFASTLEAPVVFFCRNNGLRRFMESKGWWDDEREKAANKAERKAVLQALTAAEKKPAPDMSELFSDVYAGEQPWHLAEQEVALRKHMARHPEHYAGEGH | Function: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
EC: 1.2.4.4
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] + 3-methyl-2-oxobutanoate + H(+) = (R)-N(6)-(S(8)-2-methylpropanoyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] + CO2
Sequence Length: 285
Sequence Mass (Da): 31982
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B2KCH5 | MSKTNIIAGLDVGSGKMTCVAAVQDFETNTLRVEAANSISCKGLRAGVVLDIRETSAAAVSLLTGLERECGKDIGALFLGVRGSHLESFTNHGTYNISRADKEITINDMQLAIENAKAIPIKNDNEIINVIPQSFAIDKEKGIINPEGMEGSLLEVDVHVTTGSSTHLNNLVKSIQKPGFRIDGTFYGLVPLADMVLTQEEKEIGSMLIDLGGETMSVGIYIDGVLRFSRDIPFGCDLITSDLARLLHTPRQSAKEIKERYGVAFPTFLEDEGEIPVPTLDGRSMHNVKKSFILDIIQPRVEELFEEVKKVVDRSGYKDFPVVGVLSGGGSLMPGVTNVCVNTLGLREVRTGMVSREAIIGDEQFFDPKYSTALALVAYASQRGMYEEYNRASFEQKTGLFSKIGKIFKGVDIFGS | Function: Cell division protein that is involved in the assembly of the Z ring. May serve as a membrane anchor for the Z ring.
Subcellular Location: Cell inner membrane
Sequence Length: 416
Sequence Mass (Da): 45299
Location Topology: Peripheral membrane protein
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A0A1E4RM38 | MSRYIDDYTQPNPRENFISLRLPQRVFIWLYSISLFFFTVLTIGFVAVTPIDVIKQTLGTSSSGIKLFIVIIICIVFLVASLFLYFLRLYQNRISLNDIPSKSVYIPFYGDLSKDVCAYIDKKLVECLTDIKVKAGPLHNHDVVINHPGMAPPEYIQKRNKSPSGDGTLLPPNSCYEDVIRSLGDRFSVDGRILTQIDIPKSYSFREMIISLTKLVKAGENPPNFPDVKKMIELYEEFKFSGELINERDLLVFMVEFDKLAFFFQGSFDTKDKSMDQSRPR | Function: Required for growth under high-pressure and low-temperature conditions.
Subcellular Location: Membrane
Sequence Length: 281
Sequence Mass (Da): 32274
Location Topology: Multi-pass membrane protein
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A0A1E4RT98 | MLRKEYQQEEHLQGVRFNWNVFPSTRLEQSQLLTLVGCLYKPFNESETIPTLTSHAISCSSCLNYINPYIKIDRINQMWWCPFCCKRSYFPEGYEFDNITNDISVNPSSSTIDYILPEDISNPIVSVPKCFIYIIDKYQHRDEVDHKSFLIDNVKKNINSLPAGSLVMLISFSDTVEVHNLNGDSVMFTQEELFSKAKNFDLKDTPRLISKKLNLTQLASDWSRSDLVTNGYLNDAHKIKLDKLKTELTNTYKPVRATGMALLICSIILNQSSFKHFVGKVSLLTSGPVTLQPGAIVGSHTGETVRSHHDVLNLKSPYFISSFKFYSLLGQLAIGHTLLNALDIVHSSKTLNIPSDKPRFVVDIYTGSLDQVGVYEMSPLCKISCGNIILSDSFASPHFQRNFQKSTQQFLATKLDAKFSISTSTGAKILRILSGNGSPLPSTYQVNPKLNHMHSEKISDTLDSFDSNVKKVKFTNLWWFNSIEEDTIAIFFEVDTVSSSSKLSGDGIKEIYVQYQMYYKFENSFRLRVTTIRRPTTLSILLKNQDSGMKLINSKTLIMKERDLLNSFDYQAWAVLLARLMINKIDTTLGFGDFETVVKKADLTLVRLLHYFGGISIDKITQSSNPYDSLMSCYRINENFKKLPSLMYNLRRNPQLINIFNSSPDETAVYHKSFMSANTSLSCKMIEPQIHKNYEETTLDYVTLKNLEEGHFLIMDSGFHVIIYYNGKLKLHPSNNDELIFGDSPGELIHVLEFCWKLASDRPIEPKMILTQKGHSQARFLMARLIPEDQETGPPKEPSKKSIGSWFRQLTLSSSSPGLNYALMTEEISLKRFYDELINLVNNYEINDHY | Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules.
Subcellular Location: Cytoplasm
Sequence Length: 850
Sequence Mass (Da): 96943
Location Topology: Peripheral membrane protein
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A0A0M3RI36 | MVLAGIGAGLAAIGAGIGIGKIGASAVEGVARQPEVSSKIQTVMIIAAALIEGVALFAVVVALIAK | 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 catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Subcellular Location: Cell membrane
Sequence Length: 66
Sequence Mass (Da): 6298
Location Topology: Multi-pass membrane protein
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A0A6C1PNC8 | MYHNGMKEPKVSTGGGARSLARFIVFEGLDGAGTTTQSVLLDDRLKREGRRSWLTSEPTTGPIGILCRRVLSGEIPADPDTIAHLFATDRSAHLNGADGIRQHLDDGYIVLCDRYKYSSLVYQGAETDVDFVRALNARFAVPALVVFLDLSPEAADARLAARPTREIYERIEFQHAVRANYLREMEIAGRETRVIMLDGTEEQHALAEKVWEAVADASIL | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
EC: 2.7.4.9
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Length: 220
Sequence Mass (Da): 24373
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A0A6B2BYV5 | MDKESLRKEFSEKHPELYQVELFKEKGFIRKKCKRCGRYFWTLDKNREYCPNQPCSRYEFIKNPSGKKLDYVNMWDKIKNFFVENGHQYVRRYPVVARWRDDLYFTVASIIDFQRVEEGKIIFDFPANPLIVPQMSLRFNDIANVGLTGRHYTSFCMIGQHALANEKGYWKDRTIQLDFDLLTKRLGIPEEEIVFVEDVWLGYGAFGYSLEYFVKNLELGNAVFTEFEGSPSSYTRFSPPVVDMGAGLERFVWLSYGTPTSYEAVFGSILENLRKEIQIAIDEDFASSFYEIAGEMDFSEGATLESLYSKMNVPEDKIEEIMKLKDLFILLDHSRTLLFAMSDGQLPSNVGGGYNLRVVLRRMLDILKKRKWNVTIFDLMKLHAEYLKPMYPELSENIDRLKEVVEVEQQKYEKTLQTAEKILSSYKTKKLDISEAAKLYESNGISPEVLKENGFIDFDPSEVYNYVAGKHINPKTESVKPAFNPQGLPKTEQLYYDRSVTEFEAKVLKVENGYIILDRTAFYPRSGGQEPDHGFLNGVKVLDVIKISDVIGHKVENVSGFKEGETVIGKIDKKRREALMRHHTATHIINAAARAVLGPWVWQHSAFKEEDYARIDITHHSPITEEQLKAIELYANNIVQKNVRVEKLLMPRTVAESQFGFRIYQGGAVPGNTLRIIKIGDYDVEACGGTHCDWTGEIGLIKITNVDRIQDGVDRIEFVAGEAALKYMQRMYSAFQNLRKTLNAPDLDSIQISVAEKIKETENLKNKYEELLRKYAIAIGSHEKKNLVVLEDRTIKKDDAVIIGDTVANNLGKNFLWLNCDQNGCFFLIMVPKNMSKDVQEAIKVLTEKCKGSGGAKNNVGQGFARCDKESMKNILSSLLEKDSNV | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
EC: 6.1.1.7
Catalytic Activity: ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala)
Subcellular Location: Cytoplasm
Sequence Length: 886
Domain: Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.
Sequence Mass (Da): 101502
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A0A662PU39 | MVRIVVVAVPGAGKTTILKKLLEKVPDLKVVNFGDYMFEEARKGFGISDRDEMRRKLKPRDYKLLQERAAEAIARLDGDLIIDTHAVIKTSFGYYPGLPSRVAEILNPDAIVVLEFRPEDILQRRLKDLKAEEGVKRVREIERVEDVQEHQELGREMAMAAANHVCCYLTCLRYLEPQKYPYQHAEEAASALAEIVEKFREAERG | Catalytic Activity: AMP + ATP = 2 ADP
EC: 2.7.4.3
Subcellular Location: Cytoplasm
Sequence Length: 205
Sequence Mass (Da): 23455
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A0A174NKB9 | MAKGPIDIGEENMALNQEDMASNQEPTEPNRQPRDRKAAETEAARLKGQETRRRNYEKRMEKQRLAALAAEEQRLKQRKRDEGFMREALRQAKKAAAIGDVPIGCVIVCGDRIIARGYNRRNADKSVLSHAEIISIKKACKKMGDWRLEDCTMYVTLEPCPMCAGAIVQARIPRIAVGCMNPKAGCAGSVLDMLHVPGFNHQAEVAEGVLEQECSKLMSDFFQNLRERKK | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deamination of adenosine to inosine at the wobble position 34 of tRNA(Arg2).
EC: 3.5.4.33
Catalytic Activity: adenosine(34) in tRNA + H(+) + H2O = inosine(34) in tRNA + NH4(+)
Sequence Length: 230
Sequence Mass (Da): 25828
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A0A8B5WTC3 | MESFTDEAEYHEEVLGRSVLPPGFRAATTTLTFVPSERPTGEPYKMNLATILLNEPSTGIAGVFTRNRFPGAPVVIARERMKAGVLRAVLINNKISNVCSRTGVEDARVLCSTYAAATGIDETHVVPVSTGIIGWRLPIAEMTAAIPALIDSLHEGPAADVAHAIMTTDSFPKVRSATVGSARIVAIAKGAGMIEPNLATMLVFILTDADIDRDELQTKLEDAVRVSFNRISVDSDMSTSDMVLALSSRRTRVDPDEFAAALTAVCSALAEDVVRNGEGAGHVIKARVSGVPEQTLAVALGKAVVNSPLVKTAVYGNDPNVGRIVSSLGDYLGNHDVHLDVGRLEVRIGDDVVFTGGAFDLDKEKETRLAGYIAGAALNPRLKGFPQHNRTVDFNIDFHSGNSSACVIGSDLSDEYVHENADYRS | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic): step 1/1.
Function: Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate.
Catalytic Activity: L-glutamate + N(2)-acetyl-L-ornithine = L-ornithine + N-acetyl-L-glutamate
Subcellular Location: Cytoplasm
Sequence Length: 425
Sequence Mass (Da): 45328
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L8H7H0 | MKRLYQSWPARNRFQCGGRLIAGPDRLYFYLALSFIVVPFIIACGFIWPYLFVRLGWYVVIAPLVGYILLGLASIVFMLLTRYRDPGIIPRGLEFSHNPDNPWDYERKKPPETIKINVHGENLRIKYCDTCHIYRPPRAIHCSVCNNCVERFDHHYILLHPPFASSSLLSSSLLFALYVLTRGLLIP | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 187
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 21686
Location Topology: Multi-pass membrane protein
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A0A6B2BXG6 | MDKLKFELYVYVINELGIDPAKDWKATLILSELLKNKPVKYVLDKASLLLKQRRALVVGAGPSVLDDLDYAKRKGILEGSTILAADGASLAYKDFAKKDPEIIVTDLDGYPEEEVKMVNEGSLAFVHAHGDNIDKLLKYVPQMKFVAGTTQTFETDLVKNYGGFTDGDRAAFIAESFGAKEIFLAGMDFNFSIGKYSNLEKFNGNYDRKRKKLEIGVKMLEALAAISKAPLINLSKGAVKIKGINNIER | Function: Catalyzes the transfer of diphosphate from ATP to 6-hydroxymethyl-7,8-dihydropterin (6-HMD), leading to 6-hydroxymethyl-7,8-dihydropterin diphosphate (6-HMDP).
EC: 2.7.6.3
Catalytic Activity: 6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+)
Sequence Length: 249
Sequence Mass (Da): 27562
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I7LLH3 | MDSYWDGPKPEAQARTIEEMRDVLADPGCTSDQPLYFMYRDLARSDDDRRWLHEHHVRYDITVIPSLTLCGEYVKTKGHYHTVNPAGVLYPEIYEVLAGTGHYLLQTEDAGDVVMIVGSVGDKILIPPGYGHVTINPAGVDLVMANLVSTEFSSNYAPYAERRGAAYYEMEGGALVKNPRYPDAPPVRYCDPVEVPELGIEKEVGLYDLIGRPRAVAFLNHPEQFMEIFADVTGGCLLMR | 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: 240
Sequence Mass (Da): 26828
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A0A1F3BJ50 | MRKNIALLAGGDSSEYVISVQSGEQISQILDKEKFNVYQIHVKGKDWNYFDAEKRTIPINKDDFSLEINHEKVKFDCALILIHGTPGENGILQAYFDLVKIPYTTCSFFTSALTFNKFATKLFVKEYGIITAKSVIVRKNDKINSQDIIKTVGLPCFVKPNNGGSSFATTKVKEEKELAEAISLAIKEDGNEAIIEEFIKGTELTNGVYKIKGEKTVLPITEIVSSKEFFDYEAKYTDGVTQEITPARVSSEIEARCKALSAKIYDILDCKGVTRIDYILRDNELFFLEINTVPGMSKNSIVPQQVRAMGGNMTDFYTQIIENSLK | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
EC: 6.3.2.4
Subcellular Location: Cytoplasm
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Length: 326
Sequence Mass (Da): 36586
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A0A533VEN9 | MNELAIGAIVAALIFDFLNGFHDAANSIATIVGTRVLRPLPAVGIAAFANFVGPFLFGVAVATTIGKGIINPDFVTIDIIIGALAGAITWDIITWLLGLPTSSSHALVGGIIGAGLAGVGSNAIIFDGLTKIGMGIVISPVVGLVAAFSLALLIMTIFAKKKPHAVNSAFGKLQLVSSTYFSLTHGANDGQKTMGVIALILLTQGVITKFQIPSYVILMAA | Function: Potential transporter for phosphate.
Subcellular Location: Membrane
Sequence Length: 221
Sequence Mass (Da): 22628
Location Topology: Multi-pass membrane protein
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A0A2N3G5M7 | MLASGASGGLIWLCDRKRKLLLIDGHGLAYRAFFALPVTMTNDEGQPINAVYGFVSMLLKALETEEPDAIIVALDGPRAQLKRTQEFPEYKAHRPAMPVELKGQIEMIERMLCQMRIPVVTVPGFEADDILGTLALKVSGEGGEAVIVTGDRDILQLVRPGVRVVMTSRGITETESFDRRAVEDKYGVPPSMLPEVAGLKGDASDNIPGVPGIGKKWSVDLLRRYGSLEELYARLDEIEGTKRREALEENREIAFLSRKLATLDTNVPVEIDAGEAILDNWDKREVLECLLALKFKTLARRFQDTYGLSRPARGLSAGQAGLTFEVARAYSLVDPTDDSALSAFELKARETGAAGVSSVLSGAGFCDIGLQALALATGEMALVARVEAPAAFEIARGIIESQEVQKWFHDAKPTLEALDKLEISAARVTFDTKIAAYLENPSLDSYRLFEIYERNVEGDVVITGHENASDPSEQPSLIDLEPSGARHAVEDIEAVRQAAMVFHLKPVIEEKLRALGMKKLADELELPFLFVLKEMEETGIALDAEVLLALAREAASTLGVLEKEIYRLAGHEFKIGSTKQLAHVLFDELGLPPARKTKTGYSTDASVLEALKGSHDIVGKLIEYREYAKLKSTYLDVLPALVCASTGRVHCRFNQTAGATGRISSSNPNLQNIPVRTEFGREIRRAFIPGRGFQKLLVADYSQIELRVLAHMSGDTRLLAAFERDADIHSETASHIFKTCLRDVTPEMRRMAKVVNFGIVYGMGYYGLSSRLGISVEDATAYIDTYFETYEGVSAYRERCVSDAIAKGYSETILGRRRNIPELASPNRHTREFGERVAVNTPLQGTAADIIKKAMVDVSTAIKERGMTTRMILQVHDELVFEAPALEIESLESLVREKMISVVDLLTPLKVDIGVHDNWNA | Function: In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity.
EC: 2.7.7.7
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Length: 921
Sequence Mass (Da): 101399
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R6PI33 | MSRIKIAAPAKINLTLEVLDKREDGFHNLKSIMQAISLYDYLTFDVTDSDKTQITLFGNSDKIPYDNKNLVYKAIEKFLEKTAINNKKIEVYIEKNIPVEAGLAGGSTDAAAAFFALNKLFNNPLCAEEIELLCASLGSDLNFCLHGGTALCKGRGEKTKRIPTKQQYVTLIKPLGFGISAKEAYTKFAQMSDKTVPNNTEKLMNDFSTNFLFNSLELAVINDYQELLEIKTAIPKALMSGSGPTFFVLERYCPHVFDSKRFLVIEDLKFITDGVKEIPHNC | 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-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+)
Sequence Length: 282
Sequence Mass (Da): 31517
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A0A3C0WX83 | MGNVFVISLGGSLVAPSAIDTSFLCELKTSVQAYLSKNSDKIIFIVGGGATARIYQNALRAVNPDTPSASLDEIGIRATHMNAIVVKSLFGCADEVVTDPSAADIKFSGRILVAGGWKPGFSTDMDAVMLAKRFGASTCINLSNIDMVYTKDPKANKDALPIEDATWDRFISEIVGTKWIPGSNYPFDPVASQYARDNNLTVVCANGRKIGNTISILEGGSFIGTRIHP | Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; UDP from UMP (UMPK route): step 1/1.
EC: 2.7.4.22
Catalytic Activity: ATP + UMP = ADP + UDP
Sequence Length: 229
Sequence Mass (Da): 24395
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A0A3B5L095 | IVFHWRPRLAVLARCRSCPLVLADVLLLRDSFGQQHVVEVLTEEMEAGRLRLRPGLTVAFGAFQKTLLRYYLYEGLRYVWLDRKGAFCRVSVLNEDWTCKGLYGFQNGLSPQEQSWRRSMFGANLIDVPVKSYVRLLFEEVLNPFYIFQVFSITLWSIDAYYYYALCIFIISVISISISLYEIRKVSLQWETFIQFDVLI | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
EC: 7.2.2.-
Subcellular Location: Membrane
Sequence Length: 200
Sequence Mass (Da): 23508
Location Topology: Multi-pass membrane protein
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A0A1Y2EPR3 | MVRSVPLFSACSRCVFRTFKRFEKGMDRLTGRVGPVFVGLAIILIGGCAITFFDVVYPSVFLDPETSWLYFLFGTFTSVYLVWMFSFHYYKAVTVRPGSPLDPPRPYIAPRSLSALLPSALRFGPFRNLSTRGKEDTRRARAIREIQAAQLERAAAVGDASASSASSASSMNKESRHARADRRARTCKKCLPVDGVRPPKPERSHHCSVCRTCILKFDHHCPWIKQCVGLHNERYFLLFLIYFSIACGFAAWWGWKPLMMALSFGQEWPHHVPRAFMLLLFILAAVMSVAVGVMAIFQVWLVMLGESAVESHDNDWYRKTAKSRGREFRNPYHLGRRENLNYFFNIGPGRFHWATVLLPLEIPPSSDGWTWKKIEGWEQFSMDYEDELTDEEQASDGEEF | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 400
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 45782
Location Topology: Multi-pass membrane protein
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A0A4R4D2V8 | MAGSRPLAPEPQVPQEAGSNLFEGGALPRRAGAGDRPRSVPPQPGRFVALAKLDPAQYVRDVRTEVAKVTWPSRKETLITTGLVLAMSALAAVFFLVVDQVIALGMRGLFGMG | Function: Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
Subcellular Location: Cell membrane
Sequence Length: 113
Sequence Mass (Da): 11969
Location Topology: Single-pass membrane protein
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L1MGN2 | MISSLRGPVIDIGLNSAVVECGGVGYLFSATPQTLAELSRGEEATVLTLLIVREDSMSLYGFKDAASRDLFSTLLGVSGVGPRLALAVQSVFNTADFAQAVTRGDAKALQRVPGVGKRGAERMIVELKEKVSAFVDAAAEGSDGSADLATANAEPLPYGSAVTEQVVEALMGLGFNEKQATAAVESTLATHAEADNSTLLRAALATLSS | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Subcellular Location: Cytoplasm
Sequence Length: 209
Domain: Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Sequence Mass (Da): 21520
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A0A843BK50 | MRASDLGLSQESTDCIVRYGAETLYEPQAAAVEAGLLEGKSVLVAAPTASGKSLVAILAILAMMEGGGRRAVYLSPLRALVSEKRAEFAAMGKALSRTVKVSASTGDLNARDRLVGNVMCMTNERMDLALRKGESWLEEVDLVIADEIHMVGDPFRGPTLEMVLTLLNDGSRQMVGLSATISNAPEIARWLDCRLVSSVWRPVKLTEGVYDGSRVDMADGTGFEVRSSSRGAAVDLALDSISQGGQALIFVNTRKGAPSQAGRAAAAVSRMLEPDRKKELQAISGKVLKNGENTGLADELAALIGKGVAFHHAGLNEKCRRLVEDGFRAGHIRALAATPTLAAGVNLPARRVVIASLGRYDGRYGRNMPISVMEYKQFCGRAGRPQYDDIGEAISVAEGDPQEAMERYVLGEPERVESALHHRLGVHALSLVVAEPGITADALQRFFNGTLGGAQRGGMEMSGPLRDLERLGMVETYGKRYSATRLGEITNRLYLEPETAVRFLEVVESATGGPHTLTFLHEVMSCSEFFPVLPIRAAQRDAAYELVERYGDQAVWYVDPEDISRSLLGLFGWIGEETEQEISERYGVESGDTHRAVESARWLLRSMADIATYARLPDVHKELETLRIRVVYGVREELVPLVPIRDVGRVRARALYRAGARNPRDVASMPLDRIRSVCRVGPAAARRIQSGR | Function: DNA-dependent ATPase and 3'-5' DNA helicase that may be involved in repair of stalled replication forks.
EC: 3.6.4.12
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 692
Sequence Mass (Da): 75327
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A0A533UBT5 | MSEVQQNAPNTETQRDGPRDSIYIGKKPLMAYVTSTLIQLANQPTVTIKARGLSIGRAVDVSQIILKRMENAGYTIGDVRIGSETLQAEDGRTRNVSTIEIEVKKA | PTM: Acetylated. Deacetylation by the SIR2-homolog deacetylase may regulate its activity.
Function: Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes.
Subcellular Location: Cytoplasm
Sequence Length: 106
Sequence Mass (Da): 11617
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D2Z8T8 | MYQVALSLSDGTSKSCLSTIDGVDIEGELVFTTAYPGYSQSITDPSYHGQILVFAFPCIGIYGLDEVDFQSSRPWVKAVVVQRLQDTEGTFEKWLAKWGVPVITGLDCRSLVLKLREIDTPMARISETREPPIVDTLGGGLVSEVSSSAVRNYGSGSTSVALIDYGTKMDIVRRLVDRGCSVTLLPHSVDPRLVLNGDFDGVLLSNGPGDPSLLPEEIGVVRELLGKIPILGICLGCQILALACGAETVRLPYGHRGGNHPVLDLRTGRAMVTSQNHGYAIDESSLKNTDLDISFRHLSDGTVEGISDPALRISGVQFHPEAGAGPMDGLWIFDDFVDTLRRT | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.
EC: 6.3.5.5
Catalytic Activity: 2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate
Sequence Length: 343
Sequence Mass (Da): 37006
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A0A640VU49 | MVATLSCDEGRIMLNGHHILLIIGGGIAAFKSLDVIRRLRERGASVTPVLTQAAEQFVTPLSVSSLAGRKVYRDLFDLTEEAEMGHIQLSRVADLVVIAPVTADLMAKMASGIANDLASTLLLATDTPVMIAPAMNVRMWEHSATQRNLQTLMEDGVTCVGPNDGDMACGEFGPGRMAEPLELVDAIAAKLRAGPLAGKRILVTSGPTHEPIDPVRYIANRSSGAQGTAIANALTGLGAEVIFVTGPATAPMPQHAKIVPVQTAREMLAAAEDALPVDAAIFTAAVADWRVKSASAQKLKKSKDGLPLLDFEENPDILHHIATLSDKRPGLVIGFAAETNDVVDHATAKRLRKGCDWIVANDVSAGTGVMGGADNTVTVIDDSGVDSWPKMTKAEVARRLAERIAQAMS | Cofactor: Binds 1 FMN per subunit.
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 2/5.
Function: Catalyzes two sequential steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine. In the second step the latter compound is decarboxylated to form 4'-phosphopantotheine.
Catalytic Activity: (R)-4'-phosphopantothenate + CTP + L-cysteine = CMP + diphosphate + H(+) + N-[(R)-4-phosphopantothenoyl]-L-cysteine
Sequence Length: 409
Sequence Mass (Da): 43171
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L8GFC4 | MEKRDVWERLKWNGWGEKGVQYELNQNGNVEHSRTGVELPKIIPFAKDIFGLDDLENTPSEAGGFWIGQGPGKSWHEKRYDLPMLRDLLLEKGLWVDVAETAVSFSNLLLLWKDVKESVLDAFKERNAPGWIGAHISHTYTSGVCIYFHYASVQQLDKKDDVHGEEDLSIYLDAKKAATTAILRNNGALSHHHGVGYEHVPFMSRYIGKSSIKLLSDIKKTLDPASVCNPGKLLPEAGKEDMDNEDHSFYKYGFASLTDQLKQASSVRAKSAL | Pathway: Glycerolipid metabolism; ether lipid biosynthesis.
Function: Catalyzes the exchange of an acyl for a long-chain alkyl group and the formation of the ether bond in the biosynthesis of ether phospholipids.
Catalytic Activity: a 1-acylglycerone 3-phosphate + a long chain fatty alcohol = 1-O-alkylglycerone 3-phosphate + a long-chain fatty acid + H(+)
EC: 2.5.1.26
Subcellular Location: Peroxisome
Sequence Length: 273
Sequence Mass (Da): 30691
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C4FEL1 | MRIVLQRVSHGSVDVLDEETGKRDLTFEPQTIGQGYVLLVGVSDTDGDEQIAWLVHKIANLRVFEDENGKMNLSIGSVGGSILSISQFTLFADVRKGNRPSFVKAGAPDHAKQVWLRFNDALRAEGLDVKEGRFGAHMRVDIANDGPVTIVMDTDELMK | Function: An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo and helps enforce protein L-homochirality.
Catalytic Activity: a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)
EC: 3.1.1.96
Subcellular Location: Cytoplasm
Sequence Length: 159
Domain: A Gly-cisPro motif from one monomer fits into the active site of the other monomer to allow specific chiral rejection of L-amino acids.
Sequence Mass (Da): 17509
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A0A812TF29 | HFGWAISEAFKRPEAQYVIIVEDDLEVAVDFFGYFAAVAPVLRADPTLLAASAYNDMGQRSFVGNPARVLRSDFFPGLGWMLTRHVWAELGPKWPSGYWDDWLREPPQRQGELALGRRQVLHPEVSRTRTFGEKGVSRAQFFHKYLGNIHLNSAKVDWPSQDLRYLQKQSWDASLKQLVAAAKVKSSVQALLAATCPADDLGPALQGDSPATWSGWLPPSTLRDAAALSSRVLKVEYSGFNGPRGYESLAQVSLQLPSRLHLRHSQPHMLCSQQIGVISDVKARVPRTAYKGVVALRHNSCIKLLVPAQWSIDFDSQ | Pathway: Protein modification; protein glycosylation.
Subcellular Location: Membrane
Sequence Length: 317
Sequence Mass (Da): 35344
Location Topology: Single-pass type II membrane protein
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A0A4S8PTP1 | MAETKPFPAVILAGGLSRRMGSDKAMIPFGRGTLAEHIAERLAPKVASVSLNAPLDHPLAGRLPLLPDPIPDRPGPLAGVLAALLAAKDMPDRPTHVLTTACDTPFLPSELVGKLTSVAAENTVIMAASAGRGHPVTALWPVTVAEDLGAWLDDPDHRRVFEFIARHPAKMVEFAPLDGPFGPVDPFFNINTPEDLAVAQAVLDKGDL | 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: Cytoplasm
Sequence Length: 208
Domain: The N-terminal domain determines nucleotide recognition and specific binding, while the C-terminal domain determines the specific binding to the target protein.
Sequence Mass (Da): 21976
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A0A3N5T132 | MTMREGQAIDVLGDFFRIRFVRNPNIIFGFGSELPEFLRPVILVVFPVLAVILLVVFCIRAKDLKDVFRLPLAAIVGGGLGNLVDRMFRPEGVVDFLDFNFYGILGWNRFPTFNIADSSITIGVSLIFIISVYHEIKRIREKNKQA | Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains.
EC: 3.4.23.36
Subcellular Location: Cell membrane
Sequence Length: 146
Sequence Mass (Da): 16593
Location Topology: Multi-pass membrane protein
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A0A6N2DZ49 | MSTDAQADARRPATLQLLKPGRLPYDEGLALQEKLIQDRIDERITDTLVLLEHPPVITLGRSGAETDIVAAPAALEQNGVTVHRIGRGGEATYHGPGQLVGYPIIHLYERARDIRRFVFKLEEVFVRLLSEEYGIAATRDDEHRGVWVENEKVTAVGIAIRNRVTMHGFAFNVNTDLSHFSWIIPCGIRDRGQTSLAKLLGHELDSGVVEGLVERYFREVFGYSVVSGSTTSGSASSAESDSGTSAN | Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]
EC: 2.3.1.181
Subcellular Location: Cytoplasm
Sequence Length: 247
Sequence Mass (Da): 27084
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A0A3B9GGH4 | MTITRWDELSLKTPSLRPSAATIGVFDGVHKGHQELIRRVLAHAPALMPVAVTFSDNPKHITAPERSMGMLQSLEQKLSTLETLGIELCVLIDFSGNFSKLGGNEFVSTLIRSCGVRYFAVGNDFKCGHRLSTNAFGVRDIARSLDADVDIVDPVLVEGERVSSSLIRSELAKGRTDRAYAMLGRPYTLDLRAVEREYSGSTVKLLPRVRGYVLPRNGQYAARILTAQSSRDTTVVVCSNGIKLDRAGDMADAQFLEFIANTGYTE | Pathway: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1.
EC: 2.7.7.2
Catalytic Activity: ATP + FMN + H(+) = diphosphate + FAD
Sequence Length: 266
Sequence Mass (Da): 29182
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A0A0E3ZJ16 | MLTKIKTFLSVVRSADGVRLVTTKEDLLYEGQTMFGLTRVTQDLDGIRTLRFGQHGPRQSVVKKGDLDYLGLPYARSAMIGLAFTQQLDRILVLGVGGGNIPMFLRKYYSAAQIDVVDIDPQIITLAKQYFNFLEDDLLKAYIQDGRAFIENVQKPYDLIFLDAYTAAGIPTHLATREFLLSLKNALKPSGAIIANMWSTPKVNPLYRSMLRTYQEVFKEVYTLRVPTAGNKIVIALPQFRGLPLNSIAQLAQEISVQKRLPFQLSEVLQPGLIKLIDLQESQVLLDGGQWT | Pathway: Amine and polyamine biosynthesis; spermidine biosynthesis; spermidine from putrescine: step 1/1.
Function: Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine.
Catalytic Activity: putrescine + S-adenosyl 3-(methylsulfanyl)propylamine = H(+) + S-methyl-5'-thioadenosine + spermidine
Sequence Length: 292
Sequence Mass (Da): 32767
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A0A812K430 | MAEAPSTTASAEAGDVELGEGAAAPAAAGQASDAALQPVADRRAGEGEQEELAHGSQTPTSLMDAPPPATTYQLWCNKGNIANGVTFAIMVIGIIWVLLADHVAARYVLSLGLFGWAGAVTNWLAVYMLFEKVPGIYGSGVIPGRFKEIRASIKNTIMGTFFDEEYLASYVGSRANKLIASTLPALQAKLSEAVEGGGMDGAIEKGLSDIIAQGGSLSSMLMMASMTLAPTQPPGAAALVPHMKPLLAGLGSQALEALATQVDVGTMLDVHALRSELDELMNTKLKLLMPHHIKAVIREHLGWLVVWGAVFGGLIGVLSQAHFHCSHPFYAPLHSMKFMHYRNLVGVCYTEDEAKVLASEIEVEDGPDDDGEMFERPGKLNDAFPSPYANEEQARSINNGALPPDLSLITKARHDGDNYLFALLTGYKEAPAGVVVNEEAGQYYNPYFPGGKIGMPKQLVDGAVEYGDGTPSTISQMAKDVTTFLSWAAEPHQDERKRAGNKFILFVLVAAGVTGWYKRMRWAPLKNRKISYRV | Cofactor: Binds 1 heme c group covalently per subunit.
Subcellular Location: Membrane
Sequence Length: 534
Sequence Mass (Da): 57276
Location Topology: Single-pass membrane protein
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A0A2N1TQJ1 | MIINLIELAILEDIGPGDITSDAIFNPGHESECLIISKDSGIFCGGEIARLIYQIIDPGINTEILINDGTVVSPGTEILKFTGPTISLLRGERIVLNFLQRLSGIATETNRYARALLGTSIQILDTRKTLPGFRALDKYAVMTGGGKNHRMGLYDMVMIKDNHIKAAGSITAAVRKIRVCHGSQYRVEVEAANLSEVREALESKADVIMLDNMDRETMGQAIQLINEKAEIEISGNVELDTIDSLKDLKVTYISSGALTHSVRAFDLSMKFRTV | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-ribonucleotide from quinolinate: step 1/1.
Function: Involved in the catabolism of quinolinic acid (QA).
EC: 2.4.2.19
Sequence Length: 274
Sequence Mass (Da): 30010
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A0A963VZ36 | MSITAFITVFFVLLFLGLPIGFVMAVTSALYFLLSGNMLYLLMLPERIFSGLDVFVLMSIPFFMLAGEIMNRAGMSDRLVAFSNMIVGRFRGGLAQVNVLASILFAGITGVALGDVAALGKIFIPQMEKQGYTRAFAAAVTAASSLVGPIIPPSTIIVLYGAIMGVSVGAMFAGAIIPGLLIGISDMIVVYYLARKRGYPRQTVEVTPRKFVKGGADASLAIVMPVIIVGGILGGVFTPTEAAAVAVIYALIVGLFVFRTLNLKDGGAILYNAVIDSSRLFFIIAGAATVGWVFAMENIPAVVEQAFLTVSENPIVLVLLINLFFLVMGMWMEPGALIILFAPVIAPLAYKAGLHPVQFGIMLIINGNIGLCTPPVGNVLFAVANIARIGIDKLARELLPFLVLNFSIILLVGYWADLSLWIPRMLGLIR | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 430
Sequence Mass (Da): 45888
Location Topology: Multi-pass membrane protein
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A0A939WM97 | MRQFLCGSFPDDSGKLIVKDRNYRYLVKVLRFSEGDKFDARLPDGQLVQFCVEKVMPSSAVLRLSGSAPSQVAAEFARTDGVTGAKTPGAKTAQGVQAAEVQSLAERTPEIWLFQFLPKPQKMDLIVRQAAECGVKRIIPIAGEYSVKNDAAGRIERWERIIREARQQSGSGVDTEITDVVAVGAAAEMWKEFSADAEKCAQTGGTLGASCENPPASCAASATASCAFLLDENPSVGKSSLTRIDGRSVSAAALAVGCEGGISDNERKVLAEAGFEPLHFTTNVLRAETAAIYGIAVIQQFLSAD | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.193
Subcellular Location: Cytoplasm
Sequence Length: 305
Sequence Mass (Da): 32512
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A0A356EHM0 | MSNLARQAAEFDEACLRQALALAELGAGHVRPNPLVGAVIARDGVVLGRGWHRRCGGPHAEVEAVADARSRGYANLSGSSLYVNLEPCCHQGQTPPCTNLIIDQRISRVVVGGLDPNPAVAGGGLARLRAAGIAVESGLLAADCQRLNRVFFKYIRTQQPYVLLKSALSLDGRIATAGGQSRWISGQDSRRDVHRLRASHAAVLAGIGTVLADDPRLNVRDLPVAMTWPEGWLPADWTPPPPAQPLRVILDSGLRLPPDSQVARSARQQPVWVVCAPQPPEPERRGLERLGLRVVELPADRQGRPDLRRLLPLLGAEGIDSVLIEAGAELAWSALSAGVVDSVRCYYAPLIIGGQRSTGAVGGAGYLELGKALRLQDMRVERIGEDIVMEGTACLPD | Cofactor: Binds 1 zinc ion.
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 2/4.
Function: Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'-phosphate.
Catalytic Activity: 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + H(+) + H2O = 5-amino-6-(5-phospho-D-ribosylamino)uracil + NH4(+)
Sequence Length: 397
Sequence Mass (Da): 42431
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A0A3N5U932 | MKTVIGIDPGLQNTGYGIIAMNGSRYHHIAHGTITTGKENAMEQRLLSLYQQLNQIVKQHQIDEAGIEDIYFAKNAKSAVPVAQAKGVILLVMAQNSIPVAQYSPLEIKRAVGGTGRAEKEQVQELVRMLLGLSEAPKPDHASDALAAAICHLHCMGLKRMIEAAQDAQDKLSAAAKGRLRNV | Cofactor: Binds 2 Mg(2+) ion per subunit.
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous arms, yielding a 5'-phosphate and a 3'-hydroxyl group; requires a central core of homology in the junction. The consensus cleavage sequence is 5'-(A/T)TT(C/G)-3'. Cleavage occurs on the 3'-side of the TT dinucleotide at the point of strand exchange. HJ branch migration catalyzed by RuvA-RuvB allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
EC: 3.1.21.10
Catalytic Activity: Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction).
Subcellular Location: Cytoplasm
Sequence Length: 183
Sequence Mass (Da): 19773
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