ids
stringlengths 6
10
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stringlengths 16
1.02k
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stringlengths 117
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Q8FN95 | MAKPQGAPPVDNTDPEPRAVDKSCGVLPVPADIRTLADTTRVMTKSTNRSPGHLESGEPGSDTKEHIMKTTPLFTGPLPRAVIATLAATGLFALSACASEEDTQNNGTTTDTTTETALETTTATTAGGDTGADTGADTGSEPDLTAAVTTAEGAEVGTAEFREQDGAVSITVGFNDMEPGFYGLHIHQIGVCETDSAAPDNPDNTGDFLSAGSHLGAGESDHPDHPGDLPQLLVKNDGTAVMTVETDRFTLADLEDDDGSALMIHSDADNFANIPERYSPDGADEDTLGTGDAGSRLACGVIG | Cofactor: Binds 1 copper ion per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems. May play a role in favoring mycobacterial survival in phagocytes.
EC: 1.15.1.1
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Length: 303
Sequence Mass (Da): 31073
|
F0R5W0 | MCISLWIYLRGPVQIVACTTESIRIEVYNRTANAKPIARIYVSINSTCPLLDFYPEKLLSLKPNYKVQEKMKKITIAIDGFSSCGKSTMAKDLAKEIGYIYIDSGAMYRAVTLYCIEHNLFGPDGEIKTDELKQDIDKIHISFRLDPVTSLPRTCLNGNDVEERIRTLEVSSKVSPIATLGFVREALVRQQQELGKEKGIVMDGRDIGTTVFPDAELKIFVTASPAIRAQRRYDELRAKGQPASYEDILHNVEERDRIDQSREVSPLRKADDAILLDNSHMTITEQKEWLINQFKRAAQ | Catalytic Activity: ATP + CMP = ADP + CDP
EC: 2.7.4.25
Subcellular Location: Cytoplasm
Sequence Length: 299
Sequence Mass (Da): 33946
|
A0A2T4MX48 | MIQKGVFIAIDGGEGSYKTGAISVINEFISSKGIKTVLTREPGGTPFAEKVRSLLLAIHDEKINENTELLMMYAARSQHVENLIKPSLVDGYCVITDRFSSSTIAYQCFGRGISRAKIDDIERIVLNGFCPDITIIMDVDPEIGLKRARARGVLDRIELENMDFFKRVRQGYLAQANDNPDRFFVVDASGDFDNAKKQILDILKMKFPEGI | 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: 211
Sequence Mass (Da): 23583
|
A0A938F617 | MVERIDPGGKDPLLPTDGSRADGPASLPWVSDPWDDPKVVSESEVEDSRTGGVLDPESRPTVRGLVRTVAWAVVAVVLLAGLAGWWVVRELNPGGNAETVTFTVNADDDLGAVIDRLADQDLIGNSAIFSWYVRSRGGLEPAAGYYRIERGASAGDIVAVLATPPSDTFVNVTFPEGFTIEQMARRLSEKVPNLDAERFVMAATDGSVISALAPGGTGTLEGLLFPDTYQVAGDSTESEVVARLASTMESVASKQVDLAGGAKLLGRTQYEVLIVASMIEKEAKVAADRPKIARVIYNRLEAGMKLQIDATVKYVSDPALPWTDQKATDSKFNSYLHAGLPPTPIANPGRASIAAALAPAPPPKPDDEACVGLPRGTKCDYFFYVLIDEDGRHRFATTLTQHEANTAEAIASGVLR | 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: 416
Sequence Mass (Da): 44274
Location Topology: Single-pass membrane protein
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A0A6P9AFP3 | MSAHRYLNLRPSPSCQSPSRQSPSCQSPSSPAHRLLASVPRDPMTSKFSSDPEVSSMLKDLSQRIASKPTQNGAANGAANGKTTLNGKASLKTATPVADNGAAVDALSVDKPEAKPYQRKIVWFNAIGFLILHLGTLYGIYLGMFEAYLITDIWAFVVGFISAQSVLLGAHRLYTHRSYKATFPLRLLIVLWQTVSSQNCLWVWVRDHRQHHKYSDTNADPHNARRGFFFSHVGWLMVKKHPDVFEAGRKVDMSDIEADWLVMFQKKYYNILYVLLSVLFPTVVPVYLWGETWWNSFFISFLTRTFVVLNVAWLVNSWAHLYGTHPFNQEIMPSESRLVSFLTFGEGWHNFHHTFPWDYRAAEFGQNFNFTCNIIEFFEKIGWAYDLKAAPEELVRKRALRTGDGTHPRYNKEGVPEHLVAEPEPGAEDADLDDEDGEAVLAKVAANKTDSKVAVAVAAERSKEKRG | Subcellular Location: Membrane
Sequence Length: 467
Domain: The histidine box domains are involved in binding the catalytic metal ions.
Sequence Mass (Da): 52773
Location Topology: Multi-pass membrane protein
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B7VHK9 | MSIVVRWAYTALLFLVSPILLWGLYRSKANKPPFGHRWKEHFGFTPPIKNRQSGVIWIHAVSVGEVLASKKLVEQLAIQNPDKRILITTTTSTGAEQVEKMSGSISHRYMPIDFSWCVQRFINRVQPDNMLIIETELWPNTINTVAKNDIPMILVNGRLSEKSASNYQKMSSLICPTISKFSLILTVHSDDKSRFELLGAPSEKVIVTGSIKYDVSIDNNVIAQGEHLKDILGQGRQIVVAASTHAGEDEQIFRAYQQAKIQLPELLLVIVPRHPERFDSVAELAKNQGLVLVRRTEVVEELPLDVDVYLGDTMGELMVMLSASDLVFMGGSLLGKKVGGHNFIEPALLQKYCLTGPSYFNFADLANQLIDSSALSVVADENELALQMNSALSKPKELIEKGRIGYGIVQQNQGALQQTLQLIHHSATNNQSTNIETSP | 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: 439
Sequence Mass (Da): 48755
|
A0A9C8C4E5 | MSELTLILGGVRAGKSDFAEKVAQVGNRIVYIATAEVLDEEMRKRIENHKRRRSPDWETIESPDDLTESIRQIGSNVDVIIIDCLTVYISNLLAKFSEEEILKNVSEMLNVLNNFNGKTIFVSNEVGMGIVPDNKLARDYRDVLGRTNQMVAKAAKEVYLLVAGIPVKIKG | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 5/7.
Function: Catalyzes ATP-dependent phosphorylation of adenosylcobinamide and addition of GMP to adenosylcobinamide phosphate.
EC: 2.7.1.156
Catalytic Activity: adenosylcob(III)inamide + ATP = adenosylcob(III)inamide phosphate + ADP + H(+)
Sequence Length: 171
Sequence Mass (Da): 19108
|
A0A9D0Q289 | MNYKIRLFIPILAVLMLSACSHQAQNVPVAGVNGQYAGSGTANHNNAGNGVNRGRGGSATQGVNYGSSGGVASTATGRQYNNGSTGRDYYHGGNSYGNTGQNSGSGAYQETYRPADLNNPKSLLAERIIYFDYDQVTIKPHYKKVLEAHAELLKRNPTISMRLEGHADERGTREYNVALSEQRAKSVQWYLRGKGISSARTETVAYGEERPLVVGDGEKSWAKNRRVELKYPRY | Function: Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity.
Subcellular Location: Cell outer membrane
Sequence Length: 234
Sequence Mass (Da): 25612
Location Topology: Lipid-anchor
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A0A0S8KUG7 | MKIAVIGAGAIGSVIGGLLSKAGEDVTLIGRKPHVDAVNRKGLVLEGECGRIVIKVKAAENLDFKPDLALLTVKAQDVESSVRKMQPFLSSTQIVTMQNGVQSDDQAAGLLGKENIISGVVTFNGQFLEPGKASYSIPFSKTALLIGEPFGNKGNRLQTLSALLNKAIGTDISEDIRAAHWTKLIWNLQTAVPAATGLSYQDSYQYPKVRELTINLLKEGLKVIKAAGIKTADVPGFPMEPIETMAREALPIASTLLKKKAESLGKVPVLGSTLQSIKRGKSTEVDYSNGEIVNLGKKAGIPTPVNSLMVELVHEAETTGKFLTVDELARRSN | 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: 333
Sequence Mass (Da): 35526
|
A0A7C5CTS9 | MKSSELEPEPSTLLVKNLPTDIELVLQNPYDYQNVPTQDALQDWANVAVYVIQSTTVIAAHIAFTLRIVDQTEGQQLNHEFRGKPNATNVLSFPCFTDESTADDLVFDLDPSLAVSDEDRQDVNNDGAQHYLGDLVICQPVMQQEAAQQGKSLTEHWAHLLIHGLLHLLGYDHQTDEEAAQMEQQEITILQQLGFANPYLIKPER | 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: 205
Sequence Mass (Da): 23049
|
A0A7C5CNN1 | RKVTVQYPEQKTPISPRFRGHHALRRYPNGEERCIACKLCEAVCPALAITIDSAEREDGTRRTTRYDIDMFKCIYCGFCEEACPVDAIVETRVFDYHFEKRGENIISKEQLLAFGDKHETMIAKDKAADAPYR | Cofactor: Binds 2 [4Fe-4S] clusters per subunit.
Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
EC: 7.1.1.-
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
Subcellular Location: Cell membrane
Sequence Length: 133
Sequence Mass (Da): 15336
Location Topology: Peripheral membrane protein
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A0A9D8HE39 | MSEVKIIKDIKTIHNEIALLKKSGAITGFVPTMGFLHKGHTSLIEKSVKECDATVVSIFINPIQFGQAEDFNNYPRDTKRDYNIIRQTGAQYIFMPGESSMYGDNFKTTVSVKKLGKIMCGRYRPGHFDGVCTVVLKLFNIIGPDIAYFGQKDFQQLFIIKKMVEDLNININIKECPTVREEDGLAISSRNIYLSDIERENAPLLFKTLKAAAAMIKRKNTSIKKIKKTSLELLSGNCCIKSIDYFDFRNRSTLEEIKSLKNYFSREGRPGILIAAAIRMKSTRLIDNVVI | 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)-pantothenate + AMP + diphosphate + H(+)
EC: 6.3.2.1
Subcellular Location: Cytoplasm
Sequence Length: 291
Sequence Mass (Da): 32953
|
A0A931QCK1 | MSTKFGYSVRETAQNVRRNLSLTLASVLTVAVSLSLVGGAVLLRYGVNNVTDRWQNGVEFEVFLNSDASPEQSQRIGNELQTSKDVKRVVYISQEEQYKQFKLYFADQPEYLENVTPDKLPPSYRVVPREADPDIIKTIGARFTREPGVREVVFAEEAVRDLLKVSRVIQAVILGLALVLLMSASLLIFNTIRMAIFARRREIEVMKLVGATNWFIRVPFMLEGLFQGLAGTLSAFAVLYVAQEPAQRFIRDARLFEQFAIFDSQVLTTGLFMVVIGSLLGAVGAGVAASRFLDI | Function: Part of the ABC transporter FtsEX involved in cellular division.
Subcellular Location: Membrane
Sequence Length: 295
Sequence Mass (Da): 32922
Location Topology: Multi-pass membrane protein
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A0A932EX80 | MSAVIRWYQTVRAGRPSPCRFTPTCSSYALEALATHGSVRGTWLAARRLLRCRPFGASGWDPVPPARTSLPADRPFAP | Function: Could be involved in insertion of integral membrane proteins into the membrane.
Subcellular Location: Cell membrane
Sequence Length: 78
Sequence Mass (Da): 8571
Location Topology: Peripheral membrane protein
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A0A932EVQ1 | MALTETGPLALPSGDGAGSPRPLGVFARPRTTHGWRSWVTTVDHKKIGIMYGATALFFFLVGGMEALLIRLQLATPNGKLLSADLYNQVFTMHGTTMVFLVVMPLGAGFMNYLVPLQIGARDVAFPRLNAFGFWCFLAGGLVLNSSWLLGHAPDGGWFMYAPNSGVQFSPTHGIDFWNMGLLFTGIASLTGAINLITTVLNMRAPGMSMFKMPVFTWMTLVTQFLLLFAIPVLTAAQFLLMFDRLFGAKFFDVSAGADPLLWENLFWIFGHPEVYIMILPAFGLVSEILPVFSRKPIFGYPFMVFSGIAIGVMGWGVWAHHMFASGIGPYSVAAFSMSTMLIAVPTGIKVFNWIATMWGGQVRFKAPMLYAIGMVAMFTVGGLSGVTHAVSPADTQQTDTYYIVAHFHYVLFGGALFVFVGGFYYYWPKVFGYFLSDAGGKLNFWILFVGFNMTFGPMHILGLRGQPRRVYTYRSNYGYEFWNMVSTIGAIIIGISFLVLMANIAIGYARAKRLSAGGPLTAPPDPWDARSLEWLTANPTPVHNFDRVPTIRFGLDELFYRKYREDEGGRLVRVATAEEVVEKGDRTDVHLPSPSYWPIVVAFGLPFVGWGLIYNLWLALVGGAVVVLGIFGWALEPSVDDEGGPLHPDHGQPPTTGESGAAEAPVEQEAALVD | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B.
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: Cell membrane
Sequence Length: 674
Sequence Mass (Da): 73961
Location Topology: Multi-pass membrane protein
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A0A938E495 | MDPETLLVVACALLGLVIGSFLNVVVWRVPRGESVVHPRSHCPRCDAQLAASENVPVVSWLALRGRCRHCGAPVSLRYPLVEVGCAGLWAAMALRFGAAWELPVYLGFVSALLTLALIDLDTYLLPNRIVYPLAGFLVVGFAAVAFGTGAWSAYGRALASGAAAFAAFFLVHVAAPRGMGFGDVKFAFCLGVALGWISVGTVVLGLFLGFLLGAVVGVILIALHRKGRRDQVPFGPFLAAGTVLALCFGQPLLDLYLGS | 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: 259
Sequence Mass (Da): 27266
Location Topology: Multi-pass membrane protein
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A0A938EBR2 | CDFGIVATKAMHAASAIAATAHAFAAGAVASVMNGVGNEETLAVHAARVIRGTTFPAGKLLEPGVVQWDVKGDTTFGPFEPKPASMDAVERLADACTRAGMPTTAVADARPPQWRKVIFNASTNPIGALTGLTHGRVCERPDLRALVSGLVDEGKAVAAAQGIVLDADPEDLIDHAAKREVAYDHKASMLQDVEARRLTEIDYLNGGIARFGRDLAVPTPLNDTITALIKGVETSWTSQPS | 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: 241
Sequence Mass (Da): 25263
|
A0A965JUK6 | MTISRVVAIDGPAGSGKSTIAKLLAERLEWSFLDTGAMYRAVTALALRENIDPHDTVSISDLASTSKIETIPSVLINGHDVTIEIRQPEVNHAVSIVAANPEVRAAMVDRQRDWSARQPAGTVVEGRDIGTVVFPDALLKVFLTATPEERARRRGDETAESIQRRDDIDSTRDHSPLRADERAVVIDTTNKDIHTADSVDGRIPRQARHCRSGIAQKCATSAERGSSTRAVPRGNQAGGRSSWSALRGCNVYCQPCWRASHSRRPGKYRKGNAERCMVPKARADHGRNWYAHRAAYQ | Catalytic Activity: ATP + CMP = ADP + CDP
EC: 2.7.4.25
Subcellular Location: Cytoplasm
Sequence Length: 297
Sequence Mass (Da): 32668
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A0A7V5C124 | MPESVPVAVVGASGYVGGELVRLVDRHPVFEAAILVGHATAGKTLAEVHPHLSGGGRILSPWDPAAVAASGARLAFLALPHGASAGPALELLDRGLRVVDLGSDFRFDGPDRYREAYGVDHPRPEELGRWAYGLPELFRAEVVGSDRVAAPGCYPTAAVLSVAPLLRDGLVEPSGIVVDAKSGASGAGRAVTEALVFGAVDESVRAYKILEHRHQPEMERALEAIVTDPVRVLFTPHLVPMQRGILSTAWVRTKPGVIEDDLAESLGRAYAKAPFVEVVDRPPETRWVVGSNRALLHVRHDRRGGIAVVVAAIDNLVKGAAGQAVQCANLMFGFDEAAGLPVEGWMP | 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 = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH
EC: 1.2.1.38
Subcellular Location: Cytoplasm
Sequence Length: 347
Sequence Mass (Da): 36737
|
H8GVM9 | MLPVMTPPAPSPLHLVVMGVSGSGKTTVARALAAELGLTFAEADDFHPPANIAKMTAGIPLTDEDRWPWLRALRGWMADRDARGESTVVTCSALKRSYRDLLRGAGARVQFIDLEGRPELLAARMAGRSGHFMPAALLDSQLDALEPPTPDEQAWTYDVARPPTEIVAEVAARVRRELGQHPAWPPVTPFPG | Pathway: Carbohydrate acid metabolism.
EC: 2.7.1.12
Catalytic Activity: ATP + D-gluconate = 6-phospho-D-gluconate + ADP + H(+)
Sequence Length: 192
Sequence Mass (Da): 20792
|
A0A7L3TEM0 | VLQNNDFLRNTVHRHEPPVTAQPIQILVEDDEVVVVDKPSSLPVHPCGRFRHNTVIFILGKEHDLKELHTIHRLDRMTSGVLMFAKTAEVSKRIDEQVRERQLEKEYVCRVVGEFPENEVVCEEPILVVSYKVGVCRVDPKGKSCKTIFQRLSYNGKTSVVKCLPRTGRTHQIRVHLQYLGHPIVNDPIYNMEAWGPARGKGGKIDKTDEELLKALVEEHRSKQSLDILGISEEDLNSGAENKDCGNSSDCTKSARADPINESSCPAEDTEDPERDAKDPERNDVAACPPNSDSDLETLEKNKELGSCENQDGQTGEKSSEEKDPLCAECKITRRDPSPKELVMFLHALRYKGAEFEYCSKMPAWAMEDWEE | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 372
Sequence Mass (Da): 42034
|
E7S0Y7 | MFDISFMEMLIVAIAALVVIGPERLPTVARQAGQWMSRMRRYIEDVKSDFSHQIDLAELKGIKSEVEDSARSLERGLNDARSSFDTLQSSFDTSTAESLPGAEGHGTADGHVGSLEHGGAGSAGQGATQAALDHDTADSESWAYESVPDDAVAPAPERLSPTDWDKVYEDRRTRQRLKDRRIERELERGFKRPRFRVER | 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 site that transiently accommodates folded Tat precursor proteins before their translocation.
Subcellular Location: Cell membrane
Sequence Length: 199
Sequence Mass (Da): 22164
Location Topology: Single-pass membrane protein
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A0A966KZQ8 | MQYRHIMVAPADWAEAECAPPHDLTGKPAVWPTGTAAPNLQRLMDASRDVLAESDLEASQIWLWGQGFQPQMPSFRSLHGKEAGLVTAVDLVRGLGVLTEIDIVDLATATGWYDTDYEGKRDCALRALESGADLFIIHVEATDEAGHAGDVEEKVRALENWDARILADLVPALDDMGPWRLLMLPDHATPLATRTHSSDPVPYLLADSAVDGPGGRYTEEGVADSPIVAGHELMGRLLSPA | Pathway: Carbohydrate degradation.
Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Length: 241
Sequence Mass (Da): 26052
|
A0A966NGW9 | MDAPASAAETPDADIYGRWPLVVFAHGFAASADTYAPLLHSLAASGFVVVAPEFPLSSSTIAAPAVEGDEPEQARDVNFLIDLFSGPAAPAPFDSSIAPGSVGVMGHSDGAQTVLLSGYSPAFLDRRIGAVVAVSGRYSTFGGRWFGDDAPPLLVVQASADELNPFSSGIELVQRDPHTAMLVAVDGVTHLGAVTDPAAVDPVARLVADTFAASLRADSGAQMRLRGDVAVSPLRLVDSHQG | Catalytic Activity: (ethylene terephthalate)(n) + H2O = (ethylene terephthalate)(n-1) + 4-[(2-hydroxyethoxy)carbonyl]benzoate + H(+)
EC: 3.1.1.101
Subcellular Location: Periplasm
Sequence Length: 242
Sequence Mass (Da): 24878
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A0A520WV25 | MELVGVSALPIVGLMSFLIGIVIAQQGAVQLAQFGAETLTVNLVGRITLRELGVLMTAIMVAGRSGSAFAAQLGTMKLTEEIDAMRTIGISPIEALVIPRVLACTFMMVLLGFYSSVVGIIGGAVVGDLMLGIPFTNFLERIQDVVPVHDLWVGLIKAPVFGLIVAIAGCYHGMQVKGNSEEVGLRTTMAVVTGIFTVIVLDAFFAVFFTELGWG | Function: Could be part of an ABC transporter complex.
Subcellular Location: Cell inner membrane
Sequence Length: 215
Sequence Mass (Da): 22704
Location Topology: Multi-pass membrane protein
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A0A960HY80 | MNTRSRIQAPLALVLAVVLLDQATKAWALRTLADGPVRLIGDWADFRLAWNSGSAFSMLSGSTWFLTALGIVLLGVLIYALARATDPINKIALALLLGGALGNLTDRFFRAPGVGQGHVVDFIRVGSWPVFNIADSAITIGVIVVMWRTWTLDSASNTQANAPVQAGAQTAPRSHRGSTTVEGQPTADLGAANSASSGPVDVAGDDVSITDPDSVTS | 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: 217
Sequence Mass (Da): 22637
Location Topology: Multi-pass membrane protein
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A0A2D8I3H0 | MFQRYIIAYVFEYICAVHLEVDFIFNTKYKINDCGLYKAWIKKCACHYGLSSCRLVYSFMNDNSLLELNQKHLSHDAYTDIITFCSSEGKNVIADIAISTERAGENAHKYNVLFENEILRLMAHGLLHCVGFKDKNKVDKRRMTAEENKLIKMFHVEQKARLDV | 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: 164
Sequence Mass (Da): 19141
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A0A6P8YUQ3 | MAVPPPDRISASYLILFVFALLFSASSSQERQLTATKNPGCNENPRCNSSVEVVHVRADGPNDTMHYVWCFHSEPTVLVALTSHEANLSVSWQDFPNASSSVSFTSQPFYSFGVLMSQIYEFNDINDTGLLDPANNSNTYVNKIEMPEVWEMKMLQQNRDFVRLVMDGTWKKNSTSIKNGLIRVELETYRSTDHSPNLPHLLHSSNATLIELSIVNMVTSSGFENSRYAIELTMAANESSSGGIYSRSFKSLDDEHTPGVFTLVDLQTSASKQSGNGGYLQWRPVAYVADERDIINSTETAFYSVKNGSLLQCEGTLLAAFSGFDLNTSLLKAVNVSFGASDDGFYSATNKTIWTFTMGYGHPPDENFSLLIILVMSVCLGLPAVIIVLSGLYVALRRITYRKDDLLLSE | Function: Required to protect lysosomal transporter MFSD1 from lysosomal proteolysis and for MFSD1 lysosomal localization.
Subcellular Location: Lysosome membrane
Sequence Length: 410
Sequence Mass (Da): 45373
Location Topology: Single-pass type I membrane protein
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A0A7C1KPI0 | MSLHISSLLKKSADYLKSRGSTSPRLDAELLLAEALGMRRIDLYINYDRPLNEAEVGRYRELVRARGRGEPVAYILGRAYFRDLTLRVDRNVLIPRPETEHLVEAALGRLADRDWPAPPRVLDVGTGSGAIAIAVAAGYPDTVITAVDRSAAALELARENAHAAGVACRIDFIESDMFAVLDPLATFDVILCNPPYIADDEWDGLPRDVREYEPEAALRGGADGLDFYRLLAREAPPFLRPGGRLMVEIGSAQGPGVQELMRVEAGLAAVETLKDYAGHDRVVVAGRNGNEGL | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
EC: 2.1.1.297
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-homocysteine
Sequence Length: 293
Sequence Mass (Da): 31943
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A0A5B9ELU9 | MVKLAQNRYGKSRVRLLKVTRHEGHHHVDEWTVEVLLQGDFISAHVEGDNSKILPTDTMKNTVYYMAHRSSATSMEQFAEELIDFLLSRNPQVLAAEVTVHSALWKHMKVDGSLHPTAFIRGSDEQQTTHVVRHQPGGFQVTSGLSNLVIMKTAKSGFEDYIVDELTTLKPTSDRIFATACTATWKYIHAAPLHYNQLRERARETMLHTFAGHESKSVQQTLYAMGEAVLEAVTEISEITLTMPNKHALLVDLDRFGMKNNNEIFVPTDEPHGTIQATLVRM | Pathway: Purine metabolism; urate degradation; (S)-allantoin from urate: step 1/3.
Function: Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin.
EC: 1.7.3.3
Catalytic Activity: H2O + O2 + urate = 5-hydroxyisourate + H2O2
Sequence Length: 282
Sequence Mass (Da): 31833
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A0A2M6ZZH7 | MKKKIPSKDRLIVGLLASTMKEATKLVKLLKKDVSMFEVNLPLYTVLGPDVIKMIHHEGGKVFLDLKYHDIPSTAARAVGMATKLKVEMLTVHASGGCDMLTQSVEAACDAAGSKSAKPKILAATVLTSMDSMGDIGIQFEVREQVVRLAKMSQQCGLDGVIASPLEIKPIRTVCKNNFIIATSGVRPLGTAAQDQRRIASPIMAIAAGADYLIIGRPIAQSKHPVEVVQGILKEISG | 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
Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Length: 238
Sequence Mass (Da): 25457
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A0A964ZPZ5 | MTGASGNGVTREVAIVAPTASGKSDVAMAVARETGAHIIAVDAMQVYRGMDIGTAKPTTTDRAEVSHHCIDIADPSERFSVAEFQRHAAAARAECAAAGKSALLVAGTGLYLTALIDDLSLPGEWPAVRDELQREPDTDALFARLESLDPLAATRIERSNRRRIERALEVCIGSGKPFSS | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
EC: 2.5.1.75
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA
Sequence Length: 180
Sequence Mass (Da): 19045
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A0A352B1J8 | MPESESYDYALIGGGIMSATLGVLLKLTNPHVRLVMFERLSEVAAESSNPWNNAGTGHAALCELNYMPDSKDGSLPDPSKAIAINEQFQVSRQFWASLVELGILSTPSSFIRTVPHMTFVQGAKDIDYLKRRHLALENQPLFSGMKFSTDLDEISGWAPLITQQRKKQDIAATFIDQGTDVDYGEMTKQMITWLKGQGMKLEMDTEVKSVYQFESGKWQVWLGASQNRLIHADRVFVGAGGYALKLLQRSGIPEINGYGTFPVSGHFLRTDNPEVVAQHHAKVYSQAQVGAPPMSVPHLDTRIVDGKPSLLFGPFAGLNPKFLKSGSILDLPLSIRPANLLPYLSVAFRNLGLVSYLLKEVTKSRSEKFASLQEFVPDADANDWSYYEAGQRAQVIKPVGRGGVLQFGTEVITSADGSISGLLGASPGASVSVSVMLEVLEKMQPKQFQESKAALAKLIPSFEKKLNDNPALAKKTLKATAKALGLKA | Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; oxaloacetate from (S)-malate (quinone route): step 1/1.
EC: 1.1.5.4
Catalytic Activity: (S)-malate + a quinone = a quinol + oxaloacetate
Sequence Length: 488
Sequence Mass (Da): 53275
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A0A662ZG72 | MNTISKYIFKDVLKTQGAIFGVLMLIFMSQTFIKFIGRASKGSIPAELVSQLLALSVPSMTNFMLPLSLFLAVLFSIGSFCSQSEMVVMRSVGYSHRRLLGVISLLIAVNMVINVACTCFLSPWCESRQIELINKAKSDPTMLSIDSGKFIKLNGSNVVYIDNNGDFDRNYNVMNQIYIFSSDDGNNVPSVTISASAKSEYDSDGLFWLTLYRGTRYEGPDKRGEFKVSLFDEYRALVPEGSGSHDKVKASTKSNAELLESGTSQDYAELQWRIVQPITICILALLVVPLSMVNPRRGRFAKFLPAIIIYISYYLFAFGFKSSIARGNLPVFPGIFIVPVIYLFVFTIPFNLTNTEWFNRMRAGKKKRIEEKK | Function: Part of the ABC transporter complex LptBFG involved in the translocation of lipopolysaccharide (LPS) from the inner membrane to the outer membrane.
Subcellular Location: Cell inner membrane
Sequence Length: 373
Sequence Mass (Da): 41897
Location Topology: Multi-pass membrane protein
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A0A7Z9VPF0 | MRRLFVAIKVPETVQSLLQVHQPDSTTSAHILSPEQFHITLHFIGNVDDKSSQLIDSALTQIKASPFLQYLSAIGAFFRKKGSDILWAGVEKNNNLLALHQSIGETLLACGVTLDKREYFPHITLAKIKGGSEIISNAQAKGINFGTDFKVRGFSLFESRLTDKGVVYKEIKFYRF | 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: 176
Sequence Mass (Da): 19686
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A0A7D5SLT3 | MQYRATSLAGVMILTPRTFSDHRGQFRECFRQDEFEQHCGHYPLVQDNLSRSVGGTLRGLHYQRNRPQGKLVQVISGTIFDVAVDIRPASPTYGQWLGCQLNAECGELIWIPPGFAHGFYVLSDNADVFYRCSDYYRPGDEAVIRWDCPNLAIKWPLSEQWSLLLSDKDRQAPCFVGVS | Pathway: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
Function: Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose.
EC: 5.1.3.13
Catalytic Activity: dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-beta-L-rhamnose
Sequence Length: 179
Sequence Mass (Da): 20405
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A0A960EMU2 | MTSPRFVITGGGTGGHLFPAIAFAEALTRRGMPKDAIHFVGAERGIEATVVPEHGFGVDLLPGRGFPRRIDLENLKNAAVTLKATNRARRILKRQRPDVVVGFGGYASAPAILAARTLKIPTLIHEQNAVPGAVNRLAVRLGARAAVSWPETPLPGAVVVGNPVREDVLGATWQPADPFSVSVVGGSLGAKTLNDATLELLELWQDRDVVVRHVAGPRNYESVNSATIEIRGRQGTPRLDYRLSAFESDMAGLYATSHVVVARAGASTVAELAVVGTPSVLVPLPGAPGDHQTRNARALSDHEGALLLPDAECSGSSLARALSELMEPSAGDQMHRRALAQGHRGAADDLASMALEMTDV | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Catalytic Activity: di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-glucosamine = di-trans-octa-cis-undecaprenyl diphospho-[N-acetyl-alpha-D-glucosaminyl-(1->4)]-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + H(+) + UDP
EC: 2.4.1.227
Subcellular Location: Cell membrane
Sequence Length: 360
Sequence Mass (Da): 37923
Location Topology: Peripheral membrane protein
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A0A960GFK1 | MNQRLVGAAAATFLGPYGTFADTARRSVPELTEAAWVPGDSIPAVFDAIRRGDADVGLVPIENSVEGSVSVTLDELNSESGLTILGEVAIPVRFTLAAATAIPLAEIRAVGTHPHAYAQCRGWLSEHLPQAANVATLSTAAPAEQLAAGTARGFDAAVVSATAAEHYGLVPLVTDIGDNSEAWTRFILVGRSGPPPAPTGNDKTSLVLFIRANRAGALLEILTELAVRGVNLTRVESRPTRRALGDYCFSVDLEGHVAEERIADALMGLQRQCAGVRFLGSYPAAGSAPVRPAEGVRDEDYEAARQWFQAEVLHRDSNAG | Pathway: Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from prephenate: step 1/1.
EC: 4.2.1.51
Catalytic Activity: H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O
Sequence Length: 320
Sequence Mass (Da): 33703
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A0A7V1CJN4 | MMLKTVFDKAKQNNKNVFIPYFPAGYPTISKSKKVFKQLSKSGSDIIEVGIPFSDPLADGPTIQKASTVALDAGLRIEQVFKALGEIKGDLPPTIIMTYYNLLYANGLKNFARKAAKAGVAGVIIPDLPVDESGEWVRLSKDHIETVFLAAPTSSDERIRKIDKATTSFIYCVSVTGVTGALNALPRSLSSFLKRVKGVAKNPLAVGFGVSKKEQVKQINEIADGVIVGSAIIKAYEKAKSEKEALKNVDSLIRKLTS | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
Function: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
EC: 4.2.1.20
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Length: 258
Sequence Mass (Da): 27906
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A0A966MS66 | MSEPRRPVLRTLGIDPGSKRIGLALGVGAVASPHRVVTRTRDLEGDLRSIVADIAEFEIDIVVVGLPISLDGRHGAAARAATELADRLARLTSVPVEMHDERLTTVTAERSLAEAGLDSRRRREVVDKVAAAVMLQAWLDSRGPS | Function: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 145
Sequence Mass (Da): 15592
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A0A194AK75 | MLIDPFTVFVQVLNFLILVLILKRFLFRPITRAMAQREERLARELDEAQKAKEKAEQHLADIKARNARLKDEEARMLQEIKTRAATLEKELTASVKAAVRAREHAFIQSFEREKRRRIETLQQEMATQLFTVANTALHDLAGISLHASMVAHFLDMLEQDPGAHKDRFPNLFTGQDTLTVSTPFELTGETTNRLRAILDRDFGFSGRIVSHLDPGLLAGVSLSGNGHRLDWTIHRYLEDLKTGLLEQES | Function: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
Subcellular Location: Cell membrane
Sequence Length: 249
Sequence Mass (Da): 28412
Location Topology: Single-pass membrane protein
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A0A2S6S5K7 | MFMPILLQSIKKRIDFLRISKVGRKKFTKGFILQKVKRNDSSNTYLNKDFARVGLTVTKKVGTAVVRNKIKRRLRSLSNEILTNVGKKNYDYVIIANKKAAVMKYQELKEDLINAIK | 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 the ribozyme.
EC: 3.1.26.5
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Length: 117
Sequence Mass (Da): 13562
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A0A9D8DXJ6 | MTPEPHPLSAGALALVAAGGAVGGLARYGLGRAFPTAPNAFPTTTLVINVVGAFLLGALLTVLARRSTPDHRLRLVLGVGALGAFTTFSTLAVDVVRLGRSGRPGLALANATVSVVAGIAAVVAGHRVGQIGARARGGTRAP | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 142
Sequence Mass (Da): 14063
Location Topology: Multi-pass membrane protein
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A0A938DQV7 | MFPESIVLDCDDRVLECGRDLLEGHDRAVLLLEHGEDATVCVEEHRSQSVDGEGEWRGLLGPTARSQRRGQQHEHDDRPSEGAVRSDDARNGAPVTASCSAIHPTIVPLRDRRTVAGDRWSRALRSPGRGGAALLEPSGEAETVVLADLRARGLVQDHTDWTALSDRLAVGPTALYCGFDPTADSLHLGNLQGILLLRRFQDAGHIPVALVGGATGMIGDPSGRSVERQFLDTEVLDANREAIGEQLAGLLDVGADGPGMLVDNRTWTEPLTLLEFLRDVGKHVTVNTMLAKDSVRGRIDRETGISFTEFSYMLLQANDFLELHRSHGVDLQVAGSDQWGNITAGVDLIRRRTGDHVHGLTAPLLVRADGSKFGKSEGDNIWLSAERTSPFAMYQYLLNVADDDVTDLLLRLTLVSPEDCVAVRSAHDVDPSQRIGQRRLAAEVTGLVHGVGVLPAVERAGEVLFGSRPITEVDSATLTLLATELPSSARSLADVLEADAVDLLADPVVGLAKSRSEVRRNMKGHSINGVDLEQRSSLVGEADLLDGRYVLLGRGRKARHLVVVSD | Function: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
Catalytic Activity: ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) + L-tyrosyl-tRNA(Tyr)
EC: 6.1.1.1
Subcellular Location: Cytoplasm
Sequence Length: 566
Sequence Mass (Da): 61184
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A0A3D2HH96 | MQATKWRLGITLLAIAIGVGQLMPWEDKPYATYLTQQVKSNKAQFQSVLQAAQTQVKEHKAPNLIQALVRICKEQKLDLSTCFTQLNAADIKNFDKRNQILLQHLLHKSQSVFKQGLDLKGGVAFSLSINPQVLEGKSDWECEKLVQKAIEVITTRIDALGVAEPIVRPYGRNNIEIQLPGISLETHPDIVGALKKPAKLDFRLVNEDADPNGSIPLGYERLVMEQEDEQGQWIQIPLVVKRIPAMTGKAIKEAHPVVDAYGKYEVSLQMTSEGKERFASITRQNLHRRLAIVLDGVVCSAPVIQSEITGGQASISGRFTQRDAIELSNVLNNPLEFELELAEIYEIGPSLATSAKNIAIYASLAGLILLITVMSLYYRLPGMLCSLSLLLNAFFIFVSWAILGATITLTSITALALTLGMAVDANILIFERVREELRAGINLTTALNTGHKKAFIAILDSNLTTLLTAGLLVLLGSGAVKGFGITLAAGILTTLFSVLCFNRALLELLVHTNHFHLPQQAWFQDTKINFLAHLKGGLCISCLLALIGCIAFGIRGKGVLSIDFVGGDELLVQGDRMVDCQKIRDLAKQKQLGTINAVYQKNLSSASHLLKIQTEKGRGMEVFSALQASEPEVHFTCVSKNQIGASISSDVQKHAILSIAFALIGILAYIAVRFEWTYGISSVLALTHDTLITMGLYVAFGHQFTAPMIAAVLLVIGYSINDKIIIFDRVREELAANRSMPLNAVINHSINKTLSRTLMTSLTTFIPTSLLYICCSGIVRDYALVFLLGIVIGTFSSIFVAMPLFYKLNHGNRTQLDHPQTAKHAWEQA | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
Subcellular Location: Cell membrane
Sequence Length: 829
Sequence Mass (Da): 90950
Location Topology: Multi-pass membrane protein
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A0A357I1A9 | MAIGIINYGMGNIASIKNAFEALGADTFLVETPEMLKDAERIILPGVGAFSAAMQHLNEEKWIPAIQHAVYEQKRPLLGICLGMQLLLTSGDEGGTCAGLGLIDGEVKHLQLSDPALRIPHMGWNEVDYTAESPLFKGIPDQSDFYFVHSYAAVTKSDDDVIARTQYGGDFVVAIARDHVFGVQFHPEKSSTAGRKLLQNFLEYMPC | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9.
Function: IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF.
Catalytic Activity: 5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H(+) + L-glutamate
EC: 4.3.2.10
Subcellular Location: Cytoplasm
Sequence Length: 207
Sequence Mass (Da): 22659
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A0A364MTA8 | MTSTPIHSTGRGGAGNIGPDETLYTDGGLVREGVQGEAPEGEFSTGRGGAGNIGKSPRVGPQSDEGRPVDMVPEINQRNAQDEFHTGRGGAGNVYKEKHGGHSHSPDRQGLGEKVKQALHLDKKKEHETSPLAQNETDAEALVHSSDPNHPANHICTLCAKFYNLGWVTGTGGGTSIRHEDKIYIAPSGVQKELMKPTDMFVMDFNSKEYLRKPEVLKPSACTPLFMAAFERGAGCCIHTHSQWAVLVTLLVERDFGRDACFEIEEIEQIKGIPKGRGKQGNLGYYDRLRIPIIENTAHEEDLRESLEEAMEKYPDSYAILVRRHGIYVWGDNVHKAKTQAESIDYILQLAVEMKRLGLPWTK | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 2/6.
Function: Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P).
EC: 4.2.1.109
Subcellular Location: Cytoplasm
Catalytic Activity: S-methyl-5-thio-D-ribulose 1-phosphate = 5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O
Sequence Length: 363
Sequence Mass (Da): 40023
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A0A0J5QLQ7 | MAEQKSVRTDTVVDSASKDAESFDFGSKVRDLLGWQAAMVTALCVLYSVFHLVVLNFVQLDAWVFRVLHVNIAAVIAFALYAPFGKGGERVPAFDFLLSGLAIFASFYIWWNLDELIVRTGVLPTTGDVAAALAGIIVIIEFTRRTAGLALPVLAGIFIVYGFVGPWLPGVLYHRGFGVDEFSTFVYSMEGVFGIATAAAAKYIVLFVLFAAFLQVSKVGDFFMNLAFACFGRMRGGPAKVSLFGSILFGMISGSGVANVVASGTFTIPVMKRVGYKPTSAGGIEAAASTGGQLTPPIMGAGAFIMAEITGIPYTEIIVAALIPCLLYYFAVYIQIDLEARKEGIEGLPSSELPELRPMAKDAFMLAPLALLIIFLFAGFSIISAGSWGIAIAVLVMLQQRIGLDSRLLAVPVATVLITILAAPYLSANTHGSIAMGAGCVALAGAALAARVKGFTGAMRGTVSDILEAFSIGARQCLQLAAVCACAGIVVGVIGLTGLGGRFSAMLLGVAGQSEFLALIFAMVISLILGMGMPTTAAYAIAASVVAPSLQRIGLDVLPVHLFIFYYAVISTITPPIALSAFAGAALAGGDPWKTSFKAVKYGLAAFIVPFLFIHNQGVLMEGSVWEIARTTATAALGVWALATASGGWFAGALGPLWRIGFGVTSLLLIAGDIYTDLAGVAIGAALIALRLVQTGRTGRGIKTV | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 705
Sequence Mass (Da): 73621
Location Topology: Multi-pass membrane protein
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A0A0M2V9V4 | MSYQVLARKWRPKQFAELVGQGHVKTALSNALTSSRLHHAYLFTGTRGVGKTTIARIFAKSLNCETGVTATPCGVCSACLEIDAGNFVDLLEIDAASRTKVEDTRDLLDNVQYAPSRGRFKVYLIDEVHMLSRHSFNALLKTLEEPPPHVKFLLATTDPQKLPVTVLSRCLQFSLKALSPDQIAGHLAQVLTAEQISFDTAALALLAKAANGSVRDSLSLTDQAIAQSNSQLTKEAVRDMLGFLDQQFASAILSAILRHDYPAMQAELQALISQHSDYSRVLDDMLSLLHQGALTQLEPAAAQLSEQPEFVAELAASQSPEALQLYYQLLISGKRELNFAPDQRTGLEMALLRALAFVPAPAAIQATTNVATPQPEAARVAGAAKVVAAAPAAVEPPPERLVSGTVSSVAMAPAPPADLAETASSDTTRSLPGSIDALTASIIKRRGLTSDAEAPPPKKSEHRPVPVPAEPAKGVAVSYPDEAEAEPEQLYPEDPANIAMLNSLWQQSHQQAEPAKEFSGEINEQNFSIRYAAEVDSWAALIEKMPVGGLMRLFLLNSAMQLQQQQLTLLVHQSQQHLDKADFRQELLRLLSDAIGEPLQLQVSYSHEVLQCPLAIQQRIEQERISYVSRLMQDDPKIQQLQQQFAASLLLDTLQVN | Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity.
EC: 2.7.7.7
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Length: 657
Sequence Mass (Da): 71505
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A0A2P5C1S6 | MSKSWIRQGYTKVARILGKRDPKSRNFPVLEGHPAAQQHAEVAVEAHESIKERAEELIKEFKIYRGNPDHPNNLTYLQSYFVDLSNCGPMVFDALQKIKEEEHSTLSDRRSCREGICGSCSMNIDGTNTVACLRPIDADTSKATYITPLPHMFVIKDLVADLTHFYNQYRMIEPWLKTTKAVEDGREYRQSPADK | Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; fumarate from succinate (eukaryal route): step 1/1.
Function: Iron-sulfur protein (IP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
EC: 1.3.5.1
Sequence Length: 195
Sequence Mass (Da): 22304
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A0A9E5KHY8 | IEGGIKRAQDSQDEATALLESYKAQLADARTEAAAIRNQAQAEKATIIEQAKSEAATAAAAVTERASASIEAERAQAVASLRRDVSDLALTLAGKVVGETLQDDAKARATVDRFIAELEAQAAK | 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: 124
Sequence Mass (Da): 12966
Location Topology: Single-pass membrane protein
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A0A9E5LJH7 | MLDVDSTLIDQEVIDELAKIAGLGEQVSEITSRAMAGELDFENALRQRVQLLKGHSKEILTQVRAKITLTHGAEELISTLHSLGVKVGIVSGGFEEVIAPLAGELKLDFFRANRLAIDNGVITGEVSGRIIGRHEKAEALRDFAKDSGVDISQTVAVGDGANDIEMIKSAGLGIAFCAKAVLRSEASVAIDVRDLRQVLDYFI | Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 3/3.
EC: 3.1.3.3
Catalytic Activity: H2O + O-phospho-D-serine = D-serine + phosphate
Sequence Length: 203
Sequence Mass (Da): 21797
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A0A0Q8MM43 | MPIKLALNSPAAQQLATEGVDIIEHAVAVRQDIRPLRIALLNLMPNKVNTEIQLARLLSSTPLQVELTLLSPASHSSKNTSPEYLREFYKTPDAVLREKFDGLIVTGAPVEHIPFTEVAYWNELRDFMDAAKSLSFRQMYICWGAQAALWHKYGVERDLHDHKLFGVYEQSVRTPNTSVLRGFPDQFNAPVSRYAMISEAACARHPDLRVLAASPITGASIIESSDKELFVLDHYEYDTDTLKDEYVRDAAKSLETPLPENYFKQGDAANGAANSWRPGGYLLFYNWIYRMYEDVPYNLAAVGTPAAS | Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; O-acetyl-L-homoserine from L-homoserine: step 1/1.
Function: Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine.
Catalytic Activity: acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine
EC: 2.3.1.31
Subcellular Location: Cytoplasm
Sequence Length: 308
Sequence Mass (Da): 34600
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A0A2G4F9Z2 | MGEAVPLRPKPGVHDLRIVESDHRGFKVAGIPAGASARLRLPKVTEAGHAGEVLAAELSPAGPIFLALGFILLLCGLSAGRKRRLLDDTPLSKTLGVFIGEVEVVGACVTSTPFQAYLSGRPCVLYNWSIDEQWERWETETYTDDKGRTRTRRVLRSGWTTVAGNDYTQGFYLKDEFGFLWVHPRGAALETLELFSENASRDDDLYYAKGPRAAIANSTGYRMFRESGLPVGTQLFVRGRASERSDIVAPQIVQDPKAEMFIITPRKESEVSAGKNTTYWLCNIFGLFAVLVACQFFFISLAHLAVFVLAAGYLFAWAAGWVWMVFNSLVGLRNRVRQGHSLIDVQLKRRADLIPPLVACLQGYRNHEAALQTTIATLRAQAGAAPVSAVASSLLAVVESYPELKADQSFNSLMKHLTETEDRIALARAYANDITMFYNTRLERIPDTYVAGIISMERAELFQAQGFERKAADVKFQA | Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
EC: 2.3.2.27
Subcellular Location: Membrane
Sequence Length: 478
Sequence Mass (Da): 52879
Location Topology: Multi-pass membrane protein
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A0A2A4SCJ2 | MNRMLSNNVQQLLKWLALLVVFATGLWAATSWMNNPKTLPIKFVRIEGELKHINKVDVSTAISDLVKSGFFAVKTQQIITEIEKIEWVKTVRISRVWPDAISLQLTEQQPAAVWNKTFLLNQEGHIFRPKNIDIFSSLPRLEGDDAKSVLVLESLNKSNVLLKKIGFAIKALSMTVHGSWMATSSSGVVIKIGNNEPVQTINKSFRLLSVLNIDALNRITSVDMRYPNGMAVVWKEGKELMGYELTGSPLKPTNKKLNV | Function: Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic. May control correct divisome assembly.
Subcellular Location: Cell inner membrane
Sequence Length: 259
Sequence Mass (Da): 29055
Location Topology: Single-pass type II membrane protein
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A0A349NC53 | MQTTQSVEPLIGKTVEELQTLLGSTDKLTRFEPELAQLTGEIKDEDTANVVFQALFAPHLQEHEGESPVPVVAALFSAIQASNSGQPLIGKTVEELQALIGTDTPVEQPTLTGKVEYGTVCMANSGPSTNGSQFFIVTNTDGASWLNGKHTVFGKVIEGMDVALAIQEVETGAGDKPVDDVQILGVLIERI | 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: 191
Sequence Mass (Da): 20304
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R4VL95 | MSEPGARHWRPRGVPTATPVPRRLKPWIDEPGSLTRRLRDLAGEGFAVRVIREDWSRGWPDERLRLQSGSRGALWLREVLLCGANQPLIYARSVIPATSLRGPLRRLRSLGRQPLGSLLFGRYPVRRGAIEIAPVGLHSRLGRRAANCGGTPVWARRSVFRIAGRPLLVTEVFLSELLEELGDGNSHR | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway.
Catalytic Activity: chorismate = 4-hydroxybenzoate + pyruvate
EC: 4.1.3.40
Subcellular Location: Cytoplasm
Sequence Length: 188
Sequence Mass (Da): 21057
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T0LN91 | MASFNNTQWQLTEVKSPNLDQPVPVVAVLNLPYVNNGHRFQTLNIYLPKTNQTKNLVGQPVANLPSYSPADGVPCWQVHIHGGAWRDPELTSTSIEPAAAHAFAGSDTKHPITAIISMNYTLSPFPTHPTLPYDPTKGDSSDPSRDGHHPDHIRDVLQGFAFLRTLGLHDDSYVLSGHSAGACLAFQSTLRSPQAWGLDAAMEPPRPVAVVGMNGLYDLPGLVHDLGSSHASLKEVYQGFQSITFGPDQAKWEAPSPSHVPVDELERRVKSGKVPRLIMIDQSAEDQLVPTNQADKLEARLNGIAGLHVIRGTRCEGRHAAPWEEGYMIWNNVQDILKHLG | Pathway: Amino-acid degradation; L-tryptophan degradation via kynurenine pathway; L-kynurenine from L-tryptophan: step 2/2.
Function: Catalyzes the hydrolysis of N-formyl-L-kynurenine to L-kynurenine, the second step in the kynurenine pathway of tryptophan degradation. Kynurenine may be further oxidized to nicotinic acid, NAD(H) and NADP(H). Required for elimination of toxic metabolites.
EC: 3.5.1.9
Catalytic Activity: H2O + N-formyl-L-kynurenine = formate + H(+) + L-kynurenine
Sequence Length: 341
Domain: The main chain amide nitrogen atoms of the second glycine and its adjacent residue in the HGGXW motif define the oxyanion hole, and stabilize the oxyanion that forms during the nucleophilic attack by the catalytic serine during substrate cleavage.
Sequence Mass (Da): 37304
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K7P763 | PGTMLGDDHFYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLSSAFVEQGVGTGWTVYPPLSGIQTHSGGAVDMAIFSLHLAGASSILGAMNFITTIFNMRAPGLTMDRLPLFVWSILITAFLLLLSLP | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 157
Sequence Mass (Da): 17026
Location Topology: Multi-pass membrane protein
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A0A8E0VG10 | CSEVLPFWITHAKTFTTELNCSLSANEISGLSDILVQRLEAIGCNKLFPVQACAVPFILRSYQSSKRRPVVRPRDLCISAPTGSGKTLAYVIPSVQLLLNRKNVFVRVLVILPVRDLAAQVYNVFKQLIQGTGLQVFWFYCDLIYSRSRYFVVQRVSSKSKLISWTRESAVPFQCRADIVVATPGRLVDHLYNTPGFSMERLRILVIDEADRVVVEEKQDWYRVLEDAVYHPEAFQFDPEHSSNVIRPLIRRKRPLLNFMHQYDTTHDITLQKILVSATLTHDPGPLKRFNLYYPRLLCSSVNSSDTDWGSVHQANAETSTYPQPVDIPIQPMVENSGGVGVFTTPPGLKECLVPVTPETRALFIIHLVRHQNVRRILCFTNARITAVRLAILLKHIRGVQASQLSAQMPPDKRQRILNAFSRGGLNVLVCTDAMARGMDIKDVECVVSYDMPPNVTTYVHRIGRTARAGQTGVAYTLLMRNQFFHFKNDLKRVGKSKIKEIGFHASQVNDVRPDYKAALKKLESAIKELLTLVWLCLHIPLSHAQSKDSNPIDLYGKQIKCEASQRGFHVEVRCQFFGFENSVWDGCVLKLRLSQGGSISFS | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 603
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence Mass (Da): 68226
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A0A2M7IHI2 | MQKSKFQFKIKKYPNFLEEIKCWKRGYKIVVGLDEAGRGPLAGPVIAAAVCTSVNLKFKTKNLKLENIKDSKKLSAIKREEWYKLLTRHSDIKWGVGIVSHRIIDRINIFQATKLAMMKAIEDLKRRDSRNYDRNLLKPLDFLILDGNIKLDLIIPQKAIVKADEKIFSCAAASIIAKVTRDRIMRRYGKKYPQYGFERHKGYGTQLHREVLKKHGPCRIHRLSFRPICKKN | 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: 232
Sequence Mass (Da): 27009
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A0A2E6TIS9 | MIESLIESGSSYSGDIDFLFTLITVIVGIWFIISEVVLFYFLFRYRKRDGVKAEYLSGEKKSHKKWISIPHWLIIACDIVLIVGAVQVWHHIKQKMPPAEETIRIIAQQWAWTFVHPGKDGLLDTDDDITIVDELHLKENTTYHYELSSRDVLHCFSIPIFRLKQDTIPGRKISGWFRPTTTGVHDVQCAEMCGAGHGLMPAILTIHTEEEYAEWLENQTPNLDPDPLKNEQFRGKEIGELAAD | EC: 7.1.1.9
Subcellular Location: Membrane
Sequence Length: 244
Sequence Mass (Da): 27993
Location Topology: Multi-pass membrane protein
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O47381 | FLFAYAILRSIPNKLGGVMALVLSIAILMIIPLLHTAKQRSMMFRPMSQCMXWILVADLATLTWIGGQPVEHPFVXIGQLASMIYFLLILLIMPIXSXI | Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
Subcellular Location: Membrane
Sequence Length: 99
Sequence Mass (Da): 11074
Location Topology: Multi-pass membrane protein
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A0A963WR16 | GDTCTRACRFCNIKTGMPMPVDPLEPEHTAVAAAEMGLEHIVITSVDRDDLPDRGAGQFVKVINALRRETPDTTIEILTPDFKGRMKQSIEEICEAGPDVFNHNLETIPRLYPTIRPGARYYASLRLLEEVKAHNPLIFTKSGIMLGLGEQRLEVHQVMDDMRSADIDFITMGQYLQPTPKHAKVEEFVTPKAFAAYGSIARAKGFLQVASTPLTRSSYHAGDDFAEMKAAREAKLARAQGDAKA | Cofactor: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 2/2.
Function: Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
EC: 2.8.1.8
Subcellular Location: Cytoplasm
Catalytic Activity: [[Fe-S] cluster scaffold protein carrying a second [4Fe-4S](2+) cluster] + 4 H(+) + N(6)-octanoyl-L-lysyl-[protein] + 2 oxidized [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + 2 5'-deoxyadenosine + [[Fe-S] cluster scaffold protein] + 4 Fe(3+) + 2 hydrogen sulfide + 2 L-methionine + 2 reduced [2Fe-2S]-[ferredoxin]
Sequence Length: 245
Sequence Mass (Da): 27087
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A0A5C7TT82 | MLNSTDDLRIVEITALTPPSRIIDEIPRDEAVTATVTGARNAVHNILRDEDDRLIVVIGPCSIHDPVAALDYAARLKEQRDRLAGDLEIIMRVYFEKPRTT | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 1/7.
Function: Stereospecific condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP).
EC: 2.5.1.54
Catalytic Activity: D-erythrose 4-phosphate + H2O + phosphoenolpyruvate = 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate + phosphate
Sequence Length: 101
Sequence Mass (Da): 11337
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A0A6P8ZVV7 | MQIFIRRIFRWSSIGIASPLKISTMHHKADVSSQAKHVHLSANPMELSFFSWICSVAPAFPVRAQNIKILSEPSEFYDALLRKSSTAKHRIVVSSLYLGTGHLEKALVESIRHRMVDLQGQLKVTFLLDHCRGSRGNINSRSMIAPLLEEQPDSVQVSLYHTIALRGLLRSILPQRFNEVVGLQHMKLYIFDNTIIISGANLSHDYFTNRQDRYVIIEDCEDLANFYVNLVHKVCEFSFQLLPNGSTELHSAWPPDCHPYNGDKNKFIDNAQRQIEKIIKPTTIESKNIPKNTSDTWVYPLVQMGQLKIHQDSEVTLDLLQRSPPGSQIHLATGYFNLPKQYMDIILNKSEATYHILTAHPTANGFLNAPGLAGGIPALYTQLAKDFFLRSCALKQHNRVQIQEYIQPGWTYHGKGLWLTLPGQQFPSLTLIGSPNFGSRSVDRDLETQIAIVTSNEELQSRLADERNRLYGKGHEVNKATFTRNDRQVPLWVFCISRFFRRLF | Pathway: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
Function: Functions in the biosynthesis of the anionic phospholipids phosphatidylglycerol and cardiolipin.
Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + sn-glycerol 3-phosphate = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + CMP + H(+)
EC: 2.7.8.5
Subcellular Location: Mitochondrion
Sequence Length: 504
Sequence Mass (Da): 57478
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A0A966Q8D8 | MIEQTLLRHGISRIVGVDEAGRGACAGPLVVAAVMLKDPLSSMWEGIRDSKELTPSQREEQFSIIASGAIEYSIIEISADDIDSLGLHRANLEGMRRAVLSIAGEIDYVLTDGYAVSGLSIPNLAVVKGDQV | 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.
Sequence Length: 132
Sequence Mass (Da): 14080
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F6GPI7 | MSFWYSKSKLATKMFTIFNTVMFSFSNVILAFMCLSLWTFMMGYSHPLRSVLEMQSTEPKPLSGWTSVMAMSIRIVGFSSVMSLYPMVHGYTVSIIFNVLGALLIVNMLWISSFTYDNNKFFSKVNVLTDSKLFSLFLACIEFVSFFIRPITLAIRLSANIIAGHVIFALIMFLPEPYLLFMSVFFLYFEYFVALIQAYIFVTLLNLYSQ | Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. 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. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Subcellular Location: Membrane
Sequence Length: 210
Sequence Mass (Da): 24208
Location Topology: Multi-pass membrane protein
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A0A160MWW0 | MNYRHAYHAGNFADVLKHVVLLALVEALEAKPTPFAYIDTHAGSGCYALEGKEAGKTGEYRDGIRRLLFPDLGAGNGQAATLPPLLRRWLDCILALPGNEDGLKLYPGSPLQAARAMREGDSAHLCELHPEEAARLRELFARDARVHVHHRDGYEALKALVPPPEKRGLVLIDPPYEAQDAEYRVIERALKASLARWPTGVYAVWYPIKLRSQVQPFLRGLQHGMARRVLRAELLVHADDSPLRLNGSGMVILNAPWNLDEVLREPLRAMARLLGQGQPARWNLDWLVNDSGDTPPPPRSPAPRSPRPR | Function: Specifically methylates the adenine in position 2030 of 23S rRNA.
EC: 2.1.1.266
Catalytic Activity: adenosine(2030) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(6)-methyladenosine(2030) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Length: 309
Sequence Mass (Da): 34418
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A0A286KML2 | RTSMKLYVNNDQFYNSIVTAHAFIMIFYTVMPIMIGGIDKWLVPLMLGAPDMAFPRLNNMSFWLLPPSLTLLIMGLYKEGAGTGWTVYPPLSTFYHAGISVDLTIFSLHLAGVSSILGALNFITTILNLKNKNLSSEKLSLFVWSVMLTASLLLLSLPVLAGAITMLLTDRNLNTS | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 176
Sequence Mass (Da): 19420
Location Topology: Multi-pass membrane protein
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A0A7W8P9I9 | MSSDETCSINPDAAMAAAPYRGEVSHLMIGLSRLGYRSPARSGRCRVKKWSDGSGNMAWQLLACLPRAKPYLGFALRERAEAALLGQNNALRASTIMTCTLFLGSNNMIVRSLNDVEATDHFVDWGNGTSHRLLTAKDGMGFSLCHTVVRANTVSFLQYRNHLEACYCIAGEGEVEDMEGNVFVLRKGDMYVLDKHDKHLLRGGRDKDMILVSIFNPPLNGTECHNLNDPTGSAY | Pathway: Amine and polyamine biosynthesis; ectoine biosynthesis; L-ectoine from L-aspartate 4-semialdehyde: step 3/3.
Function: Catalyzes the circularization of gamma-N-acetyl-alpha,gamma-diaminobutyric acid (ADABA) to ectoine (1,4,5,6-tetrahydro-2-methyl-4-pyrimidine carboxylic acid), which is an excellent osmoprotectant.
EC: 4.2.1.108
Catalytic Activity: (2S)-4-acetamido-2-aminobutanoate = H2O + L-ectoine
Sequence Length: 235
Sequence Mass (Da): 25874
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G3JRY1 | MPFTNWLWRAIIAYSLSDGAFVIPDTIPYGEIYFLTKGHYVGTGATSFVDRLESGHIIKYPKPNPYCPEEENLCRQQMEIEAEAYKRIGDSPRVPKLIHWDASECSLVLEFLAEGDLPSYLERCNNQAVTAEQRRVWMKHAAEAVAVVHSATIIHCDVTPRNFLLNEALELHLADFAGSSVAGSRPSITTSARFQRPGWSWEPAYADDLFALGSVLYYIQTGREPYHDIPENEVRDLFQAAAFPDVSTLDYGSVIRKCWTGEFGNAEQIIDAL | Function: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. BUD32 has ATPase activity in the context of the EKC/KEOPS complex and likely plays a supporting role to the catalytic subunit KAE1. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.1
Subcellular Location: Chromosome
Sequence Length: 273
Sequence Mass (Da): 30726
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A0A2M7A094 | MYSISKSFNFCYGHRLMGDSGRCKHLHGHTAKVVINIRKDALEETGMVCHFDELKDLAGKWIADNLDHSMLLSKHDPLAKLLKESGERVFVMDGNPTAENIAELIFKNLKQKGLDLFSVQVWESDTARAEYTA | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 4.-.-.-
Catalytic Activity: 7,8-dihydroneopterin 3'-triphosphate + H2O = 6-carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + 2 H(+) + triphosphate
Sequence Length: 133
Sequence Mass (Da): 15039
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A0A2D8I4D8 | MSSIKAIAAVSQNGVIGVNGDLPWRIPGELKWFKKITMGSIIVMGRKTWESLPGPLPGRENWVLSKSLHENTNIKVFSSFQKVLHAANGRTVFIIGGGQIYAELISNCDELYITEVHQTIENGDVFFPEFRDKFTCIETLEENKDFTIRKWKKSVKPSNKAAA | 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: 163
Sequence Mass (Da): 18298
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A0A351HCY9 | LAAAGLDRLEISQFEGLVFEMLSFEEMVPAPGQAAIAIQCREEALETYAHLFCERTKIAVSLEKGFLKRLGSGCQIPVGAYYHEDTFHIFHPETGYRAFNLDIQKPEDIEPTLDRILKDLQL | Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
EC: 2.5.1.61
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Length: 122
Sequence Mass (Da): 13786
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A0A2B7Y8C3 | MAKPFLARHTWRQLACRKTTTPIIRRRQGIHNVSKQPRRSMTGTTLNPRQEDSSSEPQEQEQLRHRRHGLGKLPLVPLLRSILMQTLMSQVYVVDTASALIKRNMKLLTGNTLFKCVGNKTFYAQFCAGETESEIQRTLANLRSLGYKGAILTYAKEVEETRTMHNSSVAQTQASHQAHVDEWLKGTLRTIQYTGAGGFVGIKYTGAGPECVRLLGSGSKPDGVIANALDQICATAEKHGARLLVDAEHHVQQKAIDSWTLELMKRCNRDGKLVVYNTYQMYLKESTAILDAHLQFAEENGFNLGIKLVRGAYIGSDPRQLIHDTKESTDNAYDTAARMLATRHVENPSCTKIGLVLATHNAESIKKMRDLRQQQLRSGLRLTDLVYAQLMGMADELSLSLTEKRSDLPEEDIQVVKYVVWGSMKECMMYLLRRAEENRDAVGRTREAQRALWQELWGRILPNNVSKTIR | Function: Converts proline to delta-1-pyrroline-5-carboxylate.
EC: 1.5.5.2
Catalytic Activity: a quinone + L-proline = (S)-1-pyrroline-5-carboxylate + a quinol + H(+)
Sequence Length: 470
Sequence Mass (Da): 53091
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A0A835F473 | MGAHRYNRYRSAPTEGPKAARHVGKPVCSERVRLALSFKGIRYEYVEEDISNKSDLLLSSNPVHKKVPVLIHNGKHVCESQIIVQYLDEVYIGRHGLSLLPIDTYERARARFWAAFIDDKMSGVDVCPATGELPSVASLDDYMDRQTTTIFQDASGANEPHPLSPTPASVPATCAAMDGAAESAFTECSKGKPFFGGDDVGYLDVMLGGLVAWVHASEARASWIEPL | Function: Is involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
Catalytic Activity: glutathione + RX = a halide anion + an S-substituted glutathione + H(+)
EC: 2.5.1.18
Subcellular Location: Cytoplasm
Sequence Length: 227
Sequence Mass (Da): 24810
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A0A2K9LNG4 | MDIELWTQNIVNATASFWNKIAAFLPNLAATIVILVVGIVLAKLLSRWSGKLLAKIGIDALCQRIGITESMAKAGMEKAPSDLLAKFIYFFILLVVTLSAAETLGLERITAILDDFVLYLPKVLGALFVILVGMFIAHVVKQSIHAAVDKMGMDYASSVSRLAQIIIFITTFSLAVGQLEIETQMLNIVFAIVLGCLGGAAAISLGLGTRAVSNNIISGVYVREQLQPGDEVTIGDFTGSVLSVGTVNTILENAEGECLSVPNQQLISRSFKFQSWSEDEG | 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 conductance with a slight preference for anions.
Subcellular Location: Cell inner membrane
Sequence Length: 281
Sequence Mass (Da): 30183
Location Topology: Multi-pass membrane protein
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A0A967XZN0 | EADFVKRVLDDAGFELDFWRVKMRPGSPVSFGWLPRGQRRQAVFGLPGNPSSAFVTFEVFVRPFLL | 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: 66
Sequence Mass (Da): 7545
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A0A2S1CXL5 | PWGLMSFWGATVITNLLSAVPYIGTTLVEWIWGGFSVDNATLTRFFTFHFLLPFAIIGVSMIHLLFLHETGSNNPTGLESNTDKIPFHPYFSYKDILGALLLIIILLLLALIFT | Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
Subcellular Location: Membrane
Sequence Length: 114
Sequence Mass (Da): 12759
Location Topology: Multi-pass membrane protein
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A0A2P5AHW2 | MPILNLHSFNFRLAMEKDVKLLGFWPQSFSTRVNGFFSATPFIRRSLCSIVHGGKAIAESLIILEYIEETWSEISPLLPKDANQRDLARFWLRFAAEKDRTLNSLLKSSSERELEKAAKEVRKCLKSWKRKALDITIISLEEKL | Function: Is involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
Catalytic Activity: glutathione + RX = a halide anion + an S-substituted glutathione + H(+)
EC: 2.5.1.18
Subcellular Location: Cytoplasm
Sequence Length: 144
Sequence Mass (Da): 16670
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A0A835FAD9 | MNPSSSSSSSSFSSSSDGYQSAASPHPRGRGRGSGGRWGGRGGRDGRDQIDAFGSSSPTGGYHSVASAFSSLQLSDDADTQRRGGGAGGGWRGGRGGSERIDAFGSSSISTSAGYHSSDASGSSSRVLRHMAAELGLDMRTDGYVRVRDLLRLNVRSYAEVPLKSHTVDEIREAVRRDNKGRFSLLEEDGELLIRANQGHSVTLVTSESLLKPILSADEVSDGMKLYISDNKVILTEGFDGIVPVKYFEKIETWPKRTLVPFEK | Function: Catalyzes the last step of tRNA splicing, the transfer of the splice junction 2'-phosphate from ligated tRNA to NAD to produce ADP-ribose 1''-2'' cyclic phosphate.
EC: 2.7.1.160
Catalytic Activity: 2'-phospho-[ligated tRNA] + NAD(+) = ADP-alpha-D-ribose 1'',2''-cyclic phosphate + mature tRNA + nicotinamide
Sequence Length: 264
Sequence Mass (Da): 28240
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A0A2D8VCR7 | MRKALATVALLALTPGCADLDEYLDDNWGSLILFSISGIVSCWCFRCANESNKMFXRMESTPISPVAEVQEGATEIKGRVKAKDDILVSPWGRKKCVYYKFKVEEEKSSGEGGTYTTTFVKEEECVPFVVRDETGEASVDNKDATYELKLDKHNRSGVFKSPTPELKQLLKTRYGKKTRGLIFRKALTYHETALEIDDEVYVFGTATAENPARNEGYLLQNGEMPLIXTDKGGSSVELGYQKDGMTLMVIGGVASCFALLGFILLVT | Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
EC: 2.3.2.27
Subcellular Location: Membrane
Sequence Length: 267
Sequence Mass (Da): 29557
Location Topology: Multi-pass membrane protein
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A0A4Q7DK89 | TFNFAMQAIDQIVNSSAKTYYMSGGQVSCPIVFRGPNGAAARVGAQHSQCYASWYSHIPGLIVIAPYTAHDHKMLLKAAIRETNPVIFLENEILYGESHEIPEGVDADLVPSIGKSVVLRHGTDVTITAFSLQVKKALEAAIKLAEIGIKAEVMDLRVLQPLDAETIIKSVKKTKRLVTVEEGWSFSGIGAEIAAIVQEQAFDYLDAPIKRVTAKDVPLPYAANLETASIPQVQDIIDAVKEACFRTR | Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
EC: 1.2.4.1
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + H(+) + pyruvate = (R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + CO2
Sequence Length: 248
Sequence Mass (Da): 27008
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A0A653KYY8 | MKKPESFTVTLPWPPSTNRIWRNVAVHGKPRTLLSEEGRRFRTTAAQLCMLGGVNNRQLAGRLAVSLVACPPDRRARDLDNVLKATLDALTHAGVWLDDSQIDLLSVERGQVVKGGELRVTISVKEAA | Function: Endonuclease that resolves Holliday junction intermediates made during homologous genetic recombination and DNA repair. Exhibits sequence and structure-selective cleavage of four-way DNA junctions, where it introduces symmetrical nicks in two strands of the same polarity at the 5' side of CC dinucleotides. Corrects the defects in genetic recombination and DNA repair associated with inactivation of RuvAB or RuvC.
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).
Sequence Length: 128
Sequence Mass (Da): 14081
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A0A6P9A331 | MCSELTYNSVRIAHQVREHEEKKSSERKKHLLCIVMQYLRDEGYLESARLTAKESGLGDQYEVCDNIDLPTIVKEFEDYYYVRFQKHPKLCKKSENLSDAANGPTRVQPRRKAIVKKTSSDAASSQSASNGCPGGGPSPPFAEPLELTVVPYPQAGPAASKAEGGDDAQVSSPERLLRPLGSLSKDPEWRQFAEIISKDIFMHNPNVRWTDIKGLQEAKRLLREAVVYPTKYPELFSGILAPWKGLLLYGPSGTGKTLLAKAVATECGTTFFNVSASTLVSKWRGDSEKLVRVLFELARLHAPATVFLDEVDALASRRGLAGEHEASRRLQAELLVQLDGLNGHAENVFLLVTSNLPWDLDEALLRRLEKRILVDLPDQDAREQILRHYLPPSPAPAPRPRGPPRPALGPAMHCQLDYAQLAQETTAYSGADLRLVCKEAAMQAVRSVFSHLESGRPDYSTLQLDVVTTDSVRSALAKTKPCGARNAERYRSWQQQFGAS | Function: Severs microtubules in vitro in an ATP-dependent manner. This activity may promote rapid reorganization of cellular microtubule arrays.
Catalytic Activity: n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers.
EC: 5.6.1.1
Subcellular Location: Cytoplasm
Sequence Length: 500
Sequence Mass (Da): 55428
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A0A835CB25 | MSATNVDLESSSADNNSAAETPRERILRVPQDYIGSVDKCTRETWVCEGTSMAHREVTYVPGLHKIFDEILTYAADNKQRDPSMDSLRVAVDVDRCRISVYYNGRGVPIELHPEEGLYVPEMIFGDLSNYQEITGVKLANLFSTEFVIETVDRSLERKYKQVFSENLGNKSEPEITACLQGVNWTRITFKPDLAKFHMTHLDDDAMALMKKRVVDIDGFLGVTVQVSFVNKFATIDGGTHVDYVSNHIAACIAKFCSRHFEVEECEVNKHLWVFVNTFMENPTFDSPTRDALTSPQESFGSSCELSDHFVKSVFQCIISKLSPWNSSKDTPSKRRC | Function: Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks.
EC: 5.6.2.2
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Sequence Length: 336
Sequence Mass (Da): 37997
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A0A6P8ZYQ8 | MLFLAEVQFEVRSYALRNRGYSTAVASNLPGAGIICFSLLVPWCEDFKISFVEDVRAISFKLRLFLVLVMLSSLLWSGREVYATVCGLQQCVRWSMRRGVPSSCSLKRVATTIAASALAALILIVIMVTKFIRDGKIGSVDARIELLAAWIISVIGSALACQIATLWALGTDLYVDVLHLVQDTAAHPKRACAHRWRELRLRLLTIHDLKVCVCASCGVPVVAFILADLLDCTFSLYTNMSLAFASRQCVTDSIWAVVMALRLVLIFGLCQRISETYEELSHILNGLLLNSKPVASEEEVKGCIIQICLGNNTCTAAGVLPMDLNSMISATLFIMSYCTVLVEFDRVTCSLKELPRES | Function: Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates.
Subcellular Location: Cell membrane
Sequence Length: 358
Sequence Mass (Da): 39458
Location Topology: Multi-pass membrane protein
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A0A088FGT3 | ALSLXIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALTLLLASGAVESGVGTGWTVYPPLAGNLAHAGGS | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 111
Sequence Mass (Da): 11651
Location Topology: Multi-pass membrane protein
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A0A6P8YJ86 | MGRLSFFVVFLAGVACAVFIASVSHLIGFQAESVWKTKFKHKTFSAIPDDDQIRVSEDIHLEVALRAGSDVNVADINRNSAAETEAEGSLHAALEMKRQGKVDKALKLFEHAYILAPLHPDVLNHYGEFLEDTQKDIIKADQLYFQAITFSPGNSRALVNRQRTAHVVERLDLAVLQRVDSKRDEVSAIPDHAPGLRRAKKEAYFQHIYHTVGIEGNTMTLSQTRSILETRMAVGGKSLVEHNEILGLDAAMKFINSTLVNRLGMITIEDILEIHRRVLGYVDPIEGGSFRRTQVYVGGHIPPSPTDIYPLMEEFIVWLNSEQAARMHPVRYAALAHYKLVAIHPFSDGNGRTSRLLMNSILMQAGFPPVIILKQDRSHYYKHLEMANRGDVRPFVRFIAECTERTLDLFLWATTEYEHEFPALETNKDSSRTIFVNDDDAPIHSEEDSTSSPDQVDSSSCLNLSD | Catalytic Activity: 3-O-(5'-adenylyl)-L-threonyl-[protein] + H2O = AMP + H(+) + L-threonyl-[protein]
EC: 2.7.7.108
Subcellular Location: Membrane
Sequence Length: 466
Sequence Mass (Da): 52410
Location Topology: Single-pass membrane protein
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A0A952A4D7 | PEFAAALGAVLAVAAQVGDFFESHLKRRAGVKDSGSILPGHGGVMDRLDGVVPVSVLVAVAIGLAR | Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-diacyl-sn-glycerol + diphosphate
EC: 2.7.7.41
Subcellular Location: Membrane
Sequence Length: 66
Sequence Mass (Da): 6637
Location Topology: Multi-pass membrane protein
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A0A835B7S0 | MSPVKLITAFGSPFAHRAEVALALKGVPFELITEDLYNKSELLLRHNPIHKTVPVLLHDDRTVSESLLIVEYVDEAFDGPRILPADPYDRAMARFWAHFVENKVSKPFWMSFWTEGEVREGFVKEAREMLAVLEAQLDGKRFFGGESLGLVDIAAIGLMGSDDEFPALRRWVKEYTSHEAVKKCTPDAQKLIAYFVENEEKYQQIAKATL | Function: Is involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
Catalytic Activity: glutathione + RX = a halide anion + an S-substituted glutathione + H(+)
EC: 2.5.1.18
Subcellular Location: Cytoplasm
Sequence Length: 210
Sequence Mass (Da): 23872
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A0A7Z9WTU9 | MKLLFDIGNSALKWGWLDAETQFHFGGWLDWPAQADAVVQQIETALPGLEEATCWVANVGPRAALYPLLQALAA | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
EC: 2.7.1.33
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Length: 74
Sequence Mass (Da): 8096
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A0A8T1XD65 | FRTNDLRLSAIEHEDGEGLKGPRLMLFKDGDFNSLVIITKNKEEQVIVSQKMTVSSDEKGQILPTVNQLTNKTDFKPLYLRVKRSSQGEAMENLLYKASRAGKIVFHVVTDSLNYPAISMWFLLNIQSRATIQILNIDDMDVLPPDYDQLLMKQNSNDPRFISPLNHARFYLPDIFPGLKKIVLFDHDVVVQRDLSRLWSIDMKGKVVGAVETCLEVLELAHGRSVMNLIDLEEWRIRKLTSTYIKYFNLGTKRPLWKAGSLPIGRESGVKAVDIEQAAVIHYDGVMKPWLDIGKENYKRYWNTHVPYHHTYLQQCNLQA | Pathway: Glycan metabolism; pectin biosynthesis.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 320
Sequence Mass (Da): 36847
Location Topology: Single-pass type II membrane protein
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A0A4V2E075 | MFERIGALDTFIVICYFVGCLAVAFWKSHKIKTIREYTLGGGSISTTVLVCTIFATAIGAGSTMGVVGKVYTLGFLFIVISLLSPVFWLMTSYIFSDIRQFRGCMSVSDIMYVLYGESGRWVTNTAAIVFSVGVVGAQAVAIGEILHYFFDVGTFVGAVIGVGVLTFYSAFGGIRAVALTDVFQFFVFYIAIPLAFATALHELGGLSTLWTSLPESHKVLDLSGANLYLFLSLLVFRLIPETAGTYMQRFLMSGNPVQLRKSLIVVSLISIPLTLIICLIGVIMKVKEPDLSPDTVFIAFIAHHLSDGLKGFMIAAIAAVIMSSADSWLNTASVLIAHDVCKRVWSKMSDRTELMIARTATLIIGVMSINIALIGKGILEIVWAINNFWSPLVVIQIVAGFLKFRTNEFSYLCSVALGCIGVSVTAYLNSDFGTFSLSAGLIGSAIGLFGSHFLQLCFGVSMPRREERLKEKAEEMRLRPKRSSIGVMFGSVVRNMWLSNLLNLAQQHTKLYKPRYELSGIGMLLCLSVAFLADSKISYITYHVISLKLILVYGIASLLVCFQEELTHRWKTKYLPLYWYITMLFAFPVTSIHMLLLTHGSIFWSVHFVVSTFIMSVFVDYGVFVALSLIGMLIGGALAYLLPPLQSVPLLSIESAYGFSVAMLGFVAISIVKRMQDSNLGDVELVNGRIVHELRSPLSVVISASELLDTIMADAVLRAENKAVTLSNDEVGEIKELSDAIKETSTRGLNTVSVFLARVKHKPEDNGKYMMRKCITSALNEYKVDQKSYKRIHFQGGEDFTFEGSWLLVKNVILNVVGNALRYSGADVKIEIRTANNRVHIKDYGKGISATMLPYIFDHEYTGEVGGTGIGLALCKEIMEELGGGIYCMSEVGDYTEFVLVFPNVS | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 906
Sequence Mass (Da): 99672
Location Topology: Multi-pass membrane protein
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A0A7V0NML3 | MARNTTVARYDLVDAAYDAPGSPKIARSVVICSTPRSGSTLLAESLLSCGTFGTPMEYFDWEGSAAILRGRWLTQDFDAYVSALHAHRTASNGVFSLKIHWNQLVGAAQRASYKPNQAPLKNLLGRIAPNPVLVHITRDDRVAQAISLYRAATTNSWSSLSDHADDIEPPYSFAAIDGYVKALSAWEKNWEILLTTAHLPYATIRYEDLVGSEGPVVDEIARFAGIPQLGPASIAPRLRRQANEWSKETAARYRDDAGADSANRFTDG | Pathway: Glycolipid metabolism.
Function: Catalyzes the sulfuryl group transfer from 3'-phosphoadenosine-5'-phosphosulfate (PAPS) to trehalose, leading to trehalose-2-sulfate (T2S).
Catalytic Activity: 3'-phosphoadenylyl sulfate + alpha,alpha-trehalose = 2-O-sulfo-alpha,alpha-trehalose + adenosine 3',5'-bisphosphate + H(+)
Sequence Length: 268
Sequence Mass (Da): 29326
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A0A6P8ZZH1 | MAYLAIQVLAALALLAAAADAARILAVMPMPARSHHIAFGGVTKALADRGHDVTLISGLPKGNKINPANNKVIYLPNPFEDMANDVLKDFWEQKQKPYEQLQFLMNWGEKLTNTTLSSPIFLAEINKPGQKYDLILAELFFFQEAMVGLGHKFNCPVVAVNPFGTSSMVNDAMGNPVNPAWVPSPFLGFSDRMSFTERAMNSLLHVSMHAYYNYFYMPKMQALSDIHFPGAPPVQDMLRSYLGLTLVNNHFSLAYPAPMSPNVVEIGGIHIPDKPKALPKDLQDFMDSAKDGVVYFSMGSNLKVEFMPESAKQAILGALFALKERVLLKWDGPLPKNMPANVKHIEWAPQGDLLAHPNMRVFFTHGGLLSTQESVYYGVPLVGMPMFGDQQFNMLLAANKGFCVKLEIRELTRQKVDEALREVLQKPKYKEAATRLSRLFRAKPLTPAQSAVFAVETVLEHGADHLRPASVGMPLYQLLLLDVVLAAAVPFLLLFLCCRALCCGSKKAAQEDRSAAARKKRN | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 522
Sequence Mass (Da): 57773
Location Topology: Single-pass membrane protein
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A0A7Z9WVU2 | MGYAHYWSRSRRKIWMKGETSGNFQR | 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: 26
Sequence Mass (Da): 3234
|
A0A835ACE3 | MARCADATLLLVVAAYALLPATTDAALQEGFYKSNTNCSVDVEATVASVVQRYISADRGVGAGLIRLHFHDCFVKVRYAPKLVNLLCSKQFNMKSNQFILTMSTATQQSLFVACATYVCQGCDGSVLIDPSPINPDPEKGSPSNGGLRGLEAIQEAKQQLESTCPGAVSCADILAFAARDASNILSAGAINYGVPSGRRDGLTSAASDATQSLPPPFAQLDRLTELFVAKGFSQDELVTLSGAHSVGRAHCGSFSERIRPNVSDTMDAEYGARLQQQCEDDGDGVAVDQDQGTPVDLDNVYYRNVLAGKVLFNSDWALVSDNATRQMVEDNAADQAQWAAKFIDAMRKMGELEVLTGDEGEIRRFCNVTNSG | 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 + H2O2 = 2 a phenolic radical donor + 2 H2O
Subcellular Location: Secreted
Sequence Length: 372
Sequence Mass (Da): 39775
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U4LM73 | MSAENHSATLSAHPDEFPAFDNQDRHTDATIEDDLETPRASFYSEVAEGELSLDEDYFSSPPPSRNAMTTPSELLSHKAAAITSSNNAPQTHSRATVAVSLPEGVYAQQQDAMSGSGSVTTAPSFSDSMSIRSTAPTLKSLGDADVESMLGEILSETESRFCASSIQESIEESVEDEDTDDEIDEEILTDEEQLARWRAKKKHFFILSEAGKPVYSRYGSETIISSYIGVLQAIISFFTDTSDTLQSFQSGSHLFVVISSGPLYLVAISCTGETPAQLRLQLDSLYQQILSTLTLSQLTKAFSGRFNFDLRRLLGGTEVFLDGLVDSILRGSPAILLSALECITLRKTHRTQINQLLLTHRTSTLLYGLIITDSRLVSVIRPKRHSLHPPDLQLLFSMLFTASTFRDGNEHWTPLCMPRFNSKGFLHAYIHFFTADSAIVLISADKDAFFELREMAEKVVAGLQETGLRERIGEGVKRPKPVDIMPGTVIRHWVYKSRGNVQFISSSWEGVERKRTMVVYQRLHAVVHGRGRVKVAFETAGSGASQGVGDGGDNGGKRSLGQDGMAWVGNGWEVYAVAKRGTKREAMVRGVQGIVKWVKEREERVFVIGGATF | Function: Required for multiple vacuole delivery pathways including the cytoplasm to vacuole transport (Cvt), autophagy, pexophagy and endocytosis.
Subcellular Location: Endosome
Sequence Length: 613
Sequence Mass (Da): 67537
Location Topology: Peripheral membrane protein
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