ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A6S4QS93 | MRKTTIASNIKPISNIIAITGPTACGKTALVQKIARKEDIIINADSRQLYKHLNIGVAKPSTPEQIAYPYRLIDHQPLHKPFTAYDFLEHVKTTVLEQQHNPHSSRIFIVGGTLFYFSALENGLIDLKVDDSLSEQLNREYMSYGLPKLRAELKERDLDHFNQIDKNNPRRIIRALALLRTHQQPLKTLQRKRLPFPYRLHKIILIPPKQTLWKTIETRAENMFINDRLIHEVKQILKQGISKSVLLKHKTIGYLEITEYLNGFYSRETALAKIIKRTKLLAKHQITWLKKQQHAHFIFLGAPTDFITPHHTANTPHHTS... | 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)-dimethylall... |
A0A6G0AFZ1 | MVTQNGFSILAHLSDIELYYTPAELIRDDKLILSGDEFHHSTNVMRNKIGDTLYVTDGQGIIYTSKIISIQKSELSALIVDSKKQLNESGNIWFCIPSLKKPDRLKFAFEKCVELGIINFILFTSRNAVSTKVIPHKFQKTVLAAMKQSLRAFIPQILSSSFGEIMNLDGNKFLFDQSAGKKYDGTVNNKETTYFLFGPEGGFHKSEIEKVNSENQFTLSPHRLRSETAVVKCASLLNLT | 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
S... |
A0A972R7J3 | MKRNNNYQKYLNLRQEFDFFEYQSYKINLIDGVLKIEFSFNMSDKYFFKPKMELRLPDGIKLESTKMLNSAVFNIGMVELISYWKTACPPNIIVKPHKLDDEQAGWWKKLYFNGLGEFFYLNCIDVPIDGFVDIESCGQAAEAVKAEMNFEKVIVPVGGGKDSVVSLEILKRASVDVIPMMLNPNPARIRTIENADLKIGDSLVVNRFLDKTLLELNDKGFLNGHTPFSALLGFTNVLLSLLTGVGYIALSNENSANESTVPGTDINHQYSKSYEFERDFNFYVKKHINNSISYFSFLRPLNEIQIGLLFSRFSRHFMSF... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Catalyzes epimerization of the terminal L-glutamate in UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-L-glutamate.
EC: 5.1.1.23
Catalytic Activity: ATP + H2O + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-L-glutamate = AMP + diphosphate + H(+) ... |
A0A316Z7V1 | FDDGPYDWHAEIAQMFHDNQMKTTYFVNGNNWRCIYDEPQVTAMQTALATGSVMYASHSWSHPNFTQLTMDEIDTQVSLLEDALFATIGRVPRLIRPPFGETNLKINQHLKDRWGLEVVQWKQDAGDGLGATVAQEKAQYKSFKKGDDILILQHETHETSIHQVIPYALKQFKKKGIKSVTAAKCLTKQPSPYKVTAKPGTRNDNWTCVGKPQPGSN | Catalytic Activity: [(1->4)-N-acetyl-beta-D-glucosaminyl](n) + n H2O = n acetate + chitosan
EC: 3.5.1.41
Subcellular Location: Cell membrane
Sequence Length: 217
Sequence Mass (Da): 24537
Location Topology: Lipid-anchor
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A0A841R3Z1 | MARLFGTDGVRGVVNETLTPELAFHLGRAAAVFFVRGDDACARPRFLIGFDTRISGTMLAAALAAGVCSAGGDVDIVGVIPTPGVAYLTRTGDYKAGVVISASHNPYPDNGIKFFDCDGFKLTDAAEDEIEAMLRGDALDNNARPTADAVGRIQLIPEAAQRYADYIAASAPCRLDGLKIIVDAAHGAASAVTPAVLRKLGAEVIAIASEPNGVNINSGVGSTHPELLRERVLAEGADAGVANDGDSDRCLLIDETGAVLDGDHILLLAAQQLKSQNKLKNDTVVATVMSNIGFKKALEKMGLKAVFTSVGDRYVLEEMR... | PTM: Activated by phosphorylation.
Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate.
EC: 5.4.2.10
Catalytic Activity: alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate
Sequence Length: 453
Sequence Mass (Da): 48266
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K2D7D7 | MTASYFQKFKKFRPLFFSLMAISFIAITVGAIKKAGYHITYSATPSMPQGFYLVVPTKKIERYDVVEFIPPKPVLNFLKERKWVPQSGLIIKYVFAVPGDDVCVRDEAVWVNGKRVGDVYRFYAPEKILPRTKICGKLNADQYLLLSTKRRRSFDGRYFGAISSSDILGRAVPVFITDVGL | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Membrane
Sequence Length: 181
Sequence Mass (Da): 20590
Location Topology: Single-pass type II membrane protein
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A0A9E7I3G0 | MGIPKNRTALKEFEEFKEEGEAKYVISSCYGISPAFPGRSSPTRPLLLPWPTAVQVALLLSLFFSLRVPRPDLASHLGAKSHDGQRFRARARSLRGMRLLFHPTTLCRDQIGILRDRSFQKSIGRMAARKPGVFDVDGTLTAPRKVFRFDFRDHAANAGVHAATQGGNQIQIFNLYTTMIIKWPSCSQKWGINWSTACDPIVSMMEQLSHDEMIAYLIFLKSLKSFLGEDKLKEFINFTLHYIAGLDISIKRGTFIELRSGMLNVSPIGQNCSQEEHDEFEKYDKACSCFGFPMRLGQDLQFKIPWGGMTMKFMNQNELL... | Pathway: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2.
Function: Catalyzes the interconversion of mannose-6-phosphate to mannose-1-phosphate, the precursor for the synthesis of GDP-mannose. GDP-mannose is an essential sugar nucleotide... |
F6W9C3 | MLGPLWNFLKRHRRKCIFVGTFLGGVYLLGKYGQKKIKEIQEREAAEYIAQARRQYHFESNQRTCNMTVLSMLPALRDALMQQLNSESLTALLKSRPSNKLEIWDDLKIISFTRSIVAVYSTCMLVVLLRVQLNIIGGYIYLDNAAVGKNGTMLLAPPDVQQQYLSSIHHLLGDGLTELITVVKQAVQKILGSVSLKHSMSLLDLEQKVKEIRKITEEQKPPSWVDTTGPRSLLCHYMMPDEETPLATQACGLTAGDVTTIKLLNETRDMLESPDFSTVLNTCLNRGFSRLLDNMAEFFRPTEQDLQRKDSMNSLSSVSL... | Function: Involved in peroxisome biosynthesis and integrity. Assembles membrane vesicles before the matrix proteins are translocated. As a docking factor for PEX19, is necessary for the import of peroxisomal membrane proteins in the peroxisomes.
Subcellular Location: Peroxisome membrane
Sequence Length: 373
Sequence Ma... |
A0A920AAI7 | MPKIPHQSSATGMQAIPTTGVAMGVQYLEQQNIAEEFGKNKPVVVCSIGDAAMTEGEISEALHMAALKQFPILYFVQDNEWDISAHASEIRANDVSQYIQGFKGIELRTIEGNNFIESYTTIKEVLETIRKERRPFMIHAKVPLWGIILQGT | 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... |
A0A660T6S2 | MNCIVTEFSGFCHGVKNTISTIEKLLKDESQPVSCIGLPVHNSQITEKLITQGLNVVDKVEDIQSGILIIRAHGLPPERIEYAKKRGLKIVDTTCNIVVRVQNIAKTLHSEGYTVLITGEHEHPEVRAIYGCTQEEGIVCSSVNDVRALKLDGKVGVVSQTTFSESIFRKIVTALIERNFSELRVFDTICSTLAKRNTAAQITASQVDMMLVVGGKMSSNTKRLYEACKKINPNTYHIETKEEFSDEWFTGVETVGITAGASTPQWIIHDICNAVKAR | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Pathway: Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from (2E)-4-hydroxy-3-methylbutenyl diphosphate: step 1/1.
Function: Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of is... |
A0A9E7KFL0 | AGVNGDGFIAQDIGFENTAGPEKHQAVALRSSADRSVFYRCSFKGYQDTLYIHTNRQWYRNCDIYGTVDIIFGDAAVVLQNPNIYVRKPMDKQKNTVTSHGRDDFHENTGIVMHAAFVMAAPDLKPVQGSFQTFLGRPWRQYSRTVYLLSRLDDLIDPAGWHAWNETMSVSNLYYAEFQSKGDRADTSKRVNWPGYHVLTTDQEAEPFTAGNFLSGDSWVLATGVPYASGLYGYDVGGNN | Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
EC: 3.1.1.11
Catalytic Activity: [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol
Sequence Length: 240
Sequence Mass (Da): 26888
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A0A9E7F0X3 | MAGRYDSDPFQEEDVNPFAETGRRGKVAGSNYGGGPLSSAVRDLKKKERELQVKEAELDKREKLALLWMTKIGHLFFPIIHHDIASEIPVHLQRLQYLAFASLLGLTACLFWNVIVVTTAWIKREGFKIWFLAIIYFISGVPGDALDGVNFTIISSQKVYSYFRGSGKTAETKREAARGAMRAAI | Function: Probably involved in membrane trafficking.
Subcellular Location: Cell membrane
Sequence Length: 185
Sequence Mass (Da): 20725
Location Topology: Multi-pass membrane protein
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A0A660T6F2 | MNVEIYSYSVFTTVIGMTVVFLFLWFLSLLMSFLKILFKEKKKGMEQEAVLEDERVIVESEKRTDWIVAAVSAYLTAEEEELYPHSAKSWKPVSNEKFDPWVIGGKLLKRWSGV | Function: Catalyzes the decarboxylation of oxaloacetate coupled to Na(+) translocation.
Catalytic Activity: H(+) + 2 Na(+)(in) + oxaloacetate = CO2 + 2 Na(+)(out) + pyruvate
EC: 7.2.4.2
Subcellular Location: Cell membrane
Sequence Length: 114
Sequence Mass (Da): 13257
Location Topology: Single-pass membrane protein
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A0A345UJI5 | MLNSTKTITAKDVATSYVEVSKSALQQNVRTLTELAGDRIKTMAIVKANAYGHGAAIVAEALEGKVTALGVATVEEAINLRKSGIIAPILVFAPVRKETVGDYKSFNLVATVGSFEELGMITPSMSFHLEFDTGMGRLGFYPEDWPEIRDFVTANMLKPSGIMTHFACADSPSHPMTIRQNAAFEDLLRTMDTFTRGKVIHASNSGGLLFYPQARYSMVRFGLSLYGYSPSPTYALPGLKPVLSWKTRICASRAIHAGATVSYEATWSAPEDGWLLVLPVGYADGIPRALSNQIVMRCNGQLLPQAGTVTMDYTMLFCRN... | Pathway: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1.
Function: Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
EC: 5.1.1.1
Catalytic Activity: L-alanine = D-alanine
Sequence Length: 366
Sequence Mass (Da): 39866
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A0A920DSG6 | MTRLVFESKMEAKKSINFDSNFTKGWFVNSAISFLSKRKRAYIFSSLLIVLGIASLSTRGLNQGVDFVGGRTYVVRFDQDVVTQDVRSSLAAPLETAPEVKTFGKANQVKITTKFMIDEKGSDELVNVKLNEGLKALGINYEVMSSQLVGPTIADDIKQSAVWAVLFSLVVIFLYILIRFRKMSYSIGAVAAVFHDVLIVLALFSILYGRLPFSLEIDQAFIAAILTVIGYSLNDTVVVFDRVREYFGVKSGSREEIVNTALNSTLSRTINTSLTTFFVLLIIFLFGGEVIRGFMFALMIGVVVGTYSSLFIATPIMVDT... | 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: 327
Sequence Mass (Da): 36216
Location... |
A0A923XL85 | MQMLVTGLSFKTAAVGIREAVSFSESDLSESLLKLSFYEAINEVVILSTCNRTEFYVITNDLDIAQKSIISFIEKEKKINFAQLESCFYNYYNKFAAEHLYRVISGIDSLIVGEGEILSQMKNAYAKAHEVGSSGKIFNALFRFVIETGKKVRTDTTIAQRPTSTGSVVAKLTKQTFGDLSTKTALLIGTGKIGTITAKNLRANNIGKLIVINRTHQKAKDLAEELGGIAFEFEHLDSVIEQADVTIVCTGSQGYLITNNNCPSKKEVLMIDLSIPRNIDSEITKNKNIKLYDIDSLESVVELNKEERTEIIGEVEMIIK... | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
EC: 1.2.1.70
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tR... |
K8Z8P0 | MEVEVNTQPNYQVKIENHLFQTIGKEIRHYWTPRKVMVVTDYTVQALYYDELQEQLQKEGFEVFLFSFPEGERNKSLEIAEQLYEGLAEQGFNRGDGIIALGGGVVGDLTGFVAATYMRGIPFLQIPTTLLAQVDSSIGGKTAVNLPFGKNLVGAFYQPDAVFIDPIMLQTLEWPYLAEGLAEVIKMAMIGDKELWEHLQTLPLEKEAFFAQLPYIITRACQQKADIVRQDPYDYGLRRKLNFGHTIAHALEAIDDYKGLRHGAAVAIGMVAILQLAYKEQWIENETMIEELIQLLEKFHLPTEYDEVGMDEIFEYIVRD... | Cofactor: Binds 1 divalent metal cation per subunit. Can use either Co(2+) or Zn(2+).
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7.
Function: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP)... |
A0A059XEQ3 | MNRGKYIVIEGAEGVGKTTMVQLIAGHLQSAGLPVKIMREPDSQNDVTARSIRRLTQDPRFPMNTRTEVLLYNAARSQSLEVIRGLVEQGVICLVDRSYLTTLAIQYYGRGDVTDYERINDIIDFAVGDMQPDLMLVLDAPVSTLRERVRGRYQGERFDNLDEAFLERVRAGYLWEAKQRELPVIYANEDIDDVFKQVWQHITAILSSRSKDASTGPQSVAEVLAAKPPIKSAPVVQPAATQPELPPAETNGQPDTALRYIVPKRVTGKLAREYRRSLDAILDTRAVLMEAVEEDDPARDIITRALLPVAAYGATDTAAA... | 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: 545
Sequence Mass (Da): 60658
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A0A9E7INM0 | MRMTSFAATELGRLFPSLLATPRNPRPVLSPLGRSPETLVSFSSSIRAAPAALELCVRNGRAPVVAAGTKHLIGSLTKTEGLKFAVVVARFNEIITNLLLEGALETFGRYSVDDDDITVVKVPGSFEVPVVAQCLGKSGKFDAILCIGAVIRGDTSHYDAVANSAASGVLNAGLSSGVPCIFGVLTCDDMEQALNRAGGKSGNKGAEAAVTARRETGEVGNGEAVARREQRGTDDGQGSRPWPSNLRLARSPSDPVAESNPTHRKRPFLFGTCTLSSIAPEEDAMHPPPTASALSLLLSLFFSARPPPKPRTSSLFFPVG... | Pathway: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2.
EC: 2.5.1.78
Catalytic Activity: (2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphat... |
A0A369A779 | MKFLLLAGEPSGDLHGANLLRHLKKFFPDGAFYCFGGDKMAANGAHLLLHYREMAFMGFWEVISNLPKILKNLRFCKNWISKNRPDVVIFIDFPGFNLRVAEFSKKQGCRNIYYISPQIWAWKESRVYQIIRNIDLMITILPFERDFYRKYNYEVKFAGHPLLDALYLDKQSVEKSDADKDIDVVLLPGSRLQEVRHILPVMTEVAVHFPDRKFVVAAAPNLPDEIFQLCIKGKSNVEIIKEKTYELIRRSKAAIVTSGTATLETALLGTPLIVVYKGNSISYWIARQLVKVKYISLINLILDHPAVPELIQYQVTPSKI... | Function: Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
EC: 2.4.1.182
Catalytic Activity: a lipid X + a UDP-2-N,3-O-bis[(3R)-3-hydrox... |
A0A6P3DQM0 | MARYAEDVYYEFAIKLTHDAAQILKAAINGAKNVDEKQDNWDLVTEYDRKIEEVVIGQLKSKFPGHRFIGEESTGKDLPELTDDPTWIIDPIDGTTNFIHGLPLTCVVIGLAINKEMVIGIVYNPVLEQLFTARKGRGAFLNNKPIKVSNVQDLSKALVCMESGFIKVHHMREKTIERMRTIALEAQGIRTLGVAALTLCYVAMGTVEAYYIEGPGISTWDIAAASLIISEAGGVVVDRETGEKINIMQPRAIGACNEKIADKLVKLIHEADQRAK | Pathway: Polyol metabolism; myo-inositol biosynthesis; myo-inositol from D-glucose 6-phosphate: step 2/2.
EC: 3.1.3.25
Catalytic Activity: a myo-inositol phosphate + H2O = myo-inositol + phosphate
Sequence Length: 276
Sequence Mass (Da): 30511
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A0A257ACG5 | MKVGVIAFQGAIEEHKIALERAIKKMGKKGEVFLIRERLKEIDALVIPGGESTTISNLMKKTGIFDEIKRIADEIPIMGTCAGCILLAKEVRDKVETLKIMDMEVERNAFGRQKESFECPLSIKGFEKPFPGVFIRAPIIKRTWGNCKPLAKIGEGIVMAKQGNKIALAFHPELTDDLRIHQYFLEMI | Pathway: Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis.
Function: Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.
EC: 4.3.3.6
Catalytic Activity: H2O + L-glutamine =... |
A0A257A514 | MKRRDIQKLLKEAEAEEGDLIEIRKGNEIYKGILMPHHSFSSEDVIIIKLENGYNIGIKIDDECEIHLIKKRKEKEKRKKKISFNKKKPIVSLIGTGGTIASYVDYLTGAVHPATSAEELALSVPEIFDICNVKAKILFQTFSENITPEHWKAMAKEVAEELNKDAEGVIISHGTDTLAYTSAALSFMLKNLSGAVVLVGSQRSSDRPSSDSFHNLLGAARVAISDIGEVVVVMHSNISPPLCTIHRGTKVRKMHSSRRDAFQTINENPIGFVDKGLKIIGKYRKKTDGMTEADVSIDSNVSLVYHHPALTPDDFMSIVE... | Function: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). The GatDE system is specific for g... |
A0A151F606 | MDGTVIEFYKMNGAGNDFVVIDNREDIIPERCKSEFAENVCRRRVSVGADGILLVEPSEKATFKMRHFNADGSEGEMCGNGARCIARFAFLKGIADKKMSIETMSGIIKAEIVNSHVKINVNPVTEKELHKKITVDGDEISVYYLEEGTPGLPHTVVFKDDLTMEEDIEDVGRKIRYHSAFSKGTNVNFCRVKGRDTIVNRTYERGVERETLACGTGSAAAACVAYLLGKCGKKVNVETKGGILEVSILDENLENIYLTGDAEIVYKSTLEERQVF | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.
Function: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine.
Catalytic Activity: (2S,6S)-2,6-diamin... |
A0A8E3YDR0 | SLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTILNMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGQP | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A6I8NFZ3 | MPIVDKLKEALKPGRKDSADDAELGKLLASSAKKVLLQKIEFEPASKSFSYQLEALKSKYVLLNPKSEGAGRHKTWEDAPVRRQGSDHGLGSSSGGDGVPAPQKVLFPTERLSLRWERVYRVGAGLHNLGNTCFLNSTIQCLTYTPPLANYLLSKEHSRSCAPGGFCMLCVMQNHMIQTFANSGNAIKPFSFIRDLKKIARHFRFGSQEDAHEFLRYTIDAMQKACLNGHAKLDRQTQATTLVHQIFGGYLRSRVKCSLCKSVSDTYDPYLDVALEIRQTANIVRALELFVKPDVLSGENAYMCAKCKKKVPASKRFSIH... | Function: Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes.
EC: 3.4.19.12
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attac... |
K1XNQ5 | MNHFSANIKEPDIVKLKHDLKQKSFEFKELPYGHFQAINSSLKITINVYHSLKCLIQGKGTEEFVRYYFEPEILKTFDLDYGHLNFKEKIGMDESGKGDYFGPLVVASAYVSNENFHQLKKNGVVDSKKINDKRIHVIAETIKKICPIHFISISPEKYNELYAKFNNLNSLLAWAHSACLKEILTKCNTTNATIDKFAQSAVLNKYLKIKNITIDVEQIVRGEQDIAVAAASIIARSNFLNQIENLSKKYGIQLPKGGGESTHSAGKEFIAKHGIENLGKVAKLHFKNTEKIQN | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Subce... |
A0A5P9NPC7 | MAKLIVIMGPAGCGKSVVAARIAAARSATALDADDFHSRENIAHMAGGNPLTDAQREPWIAAMEKELHARLGNNENIVLAYSGLRRAHRARIRACAQRSLFIKLQVPIAQLQERVAKRQNHFMSAQMLPSQLAAMESPASEETIVQIAAHGSLDDVVESTLNAIRETFS | Pathway: Carbohydrate acid metabolism.
EC: 2.7.1.12
Catalytic Activity: ATP + D-gluconate = 6-phospho-D-gluconate + ADP + H(+)
Sequence Length: 169
Sequence Mass (Da): 18350
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A0A1B1YW16 | MSAVCALRWQGGALELLDQRLLPAQQLWLRCASAAEVADAIRDMVVRGAPAIGIAAAYGAVLAARAAYAGHGTGWRDVIVADLDLIAAARPTAVNLAWAVQRMAGCLAELAGDPEPALLAAARAIHDQDIAANHAMAAYGAALIEPGSRVLTHCNTGALATGGHGTALGVIRTAHAQGRIREVFVDETRPWLQGARLTAWELQQDGIPARLVVDGAAAWLFARLRPAWLIVGADRIAANGDTANKIGTYTAALAARAHGARVMVVAPLSTFDPATPDGSAIEVEERPAQELTCLAGQAIAPAGFAAWNPVFDVTPADLID... | Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 1/6.
Function: Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
EC: 5.3.1.23
Catalytic Activity: S-me... |
A0A651GKV7 | MISPQEALEYIRKATPATAAEHKSPGEAHLQTLAEDVAAPHHHPFFDQSAMDGYAARFEDLVSGQALRIAAHLPAGSTTLPTIQPGEAARIFTGSAIPPGADTVIMQEHCSTENDLLVVERLPEKPGTHIRRCGEQIARGEVALPKGKVLNSSAIGFLASIGVQRVSVWKRPTAAIITTGSEFIRPGEELMPGKIFESNGIMLQTALQEQGIASERHICEDDPEKLTALINQLAEKTDLLLLTGGVSVGDHDHTPSALSSAGFNILFHKVNQKPGKPLLFATRKDCMAFGLPGNPRSVLMCYHVYVKAMLGQWTGQQEIS... | 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: 392
Sequence Mass (Da):... |
K2E1D5 | MISVRTVTFAPNHPILMADLALYRKYRPARFNHLMGQNHVQKTILNAIKSGHLSHAYLFCGPRGTGKTSTARLVAKAINCITPDPEGESCNQCDYCLMMNQGSLVDLIEIDAASNRGIDEIRDLREKIRFAPNQAPHKVYIIDEVHMLTTPAFNALLKTLEEPPPHAYFILATTEIHKVPDTIISRCQRFDFRRIDQETLVDRLRYISQQENVEAEEAALELISRSSQGGMRDAISLFEQTLREGKLHLSVVQEVLGLVGNEGAIHLFSALEQKETSLALSEIQKLHEEGHNLYQFNREFLEFLRARLLEDLEKPEKVAQ... | 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: 517
Seq... |
A0A9E7ECZ4 | MDFPSYSTSKEQARIYNEWFSFADSDGDGRITGNDAIKFFSMSNLSRPDLKQLVALAQAGNEITQDTLTNADLEKLNPPVMEGLDTLLSRNKASTKKIDPEIDVNSKPQSPPSTVQWFSSKSAKKIPLSQVTSIIDGLKRLYVEKLKPLEVTYRFNDFVSPLLTNSDFDAKPMVMLLGQYSTGKTTFIKHLLKTSYPGAHIGPEPTTDRFVVVMSGPDERTIPGNTIAVQADMAFSGLTMFGTAFLSKFECSQMPNPLLEHITFVDSPGVLSGEKQRTQRSYDFTGVTSWFAAKCDLILLLFDPHKLDISDEFKRVIGSL... | Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membra... |
A0A1J5E9U1 | MVTVSLGVLVSGRGSNLQAIIDAINGGKLNAAIRIVISNKKDAYALERAKKAGIKTIFIDPKDFLSWQDYEQQMVSQLKANGVELVILAGFMRILTPYFVNAYKDRILNIHPALLPSFPGLHAQQQALEYGVKVTGITVHVVDEGMDTGRIILQRVVDVLSNDTVKSLSERMLRIEHQVYPEAIALYCK | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (10-formyl THF route): step 1/1.
Function: Catalyzes the transfer of a formyl group from 10-formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), produc... |
A0A7J4V897 | MKVVTVDIGNSKIKTGEFYNSELIRTMVIDDPLEIKPLIYGSHIEVVVSSVVPKQTSLLESILRNQSNTDIFLLDHSLDFGFNVTYSPLNSLGLDRLCSVAGAKHLLEIDNALHDHDFVISIDFGTATTVNVLQVGKPSVFTGGMIAPGLRIMNSALNQFTAKLPLIESYQSGSFLGNSTENSIRSGILNSTVGLVERVFDHFTTISQDIKIFVTGGYAPQLMPHLQVPFQYEPFLNLIGIYSVYYRNKR | Cofactor: A monovalent cation. Ammonium or potassium.
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
EC: 2.7.1.33
Subcellular Location: Cytoplasm
Catalytic Activity: (R)-pant... |
A0A7J4VCQ7 | MQESNLQETLKKAFVSDDLLTQCMHCGMCLPTCPTYNITKLESSSPRGRIRLIKSVAEGKLEINDTFINEINYCLDCQACETACPAGVKYGAIVEAAREEVSRNDLEPFKNRFLRRFGLNFILANQSLLKIVARMIYFYQNTGLQGFLHRMGVFKILGTGLEKADQLSPAISKRFSSDVMDEVYSPAGPVRYRVLLPLGCLMDVAFADIHSDTLNVLLQHGCEVIIPRNQGCCGSLHAHNGEQKKGRELAQRTYDLFSRYEYDFIVSNSAGCGAYMKEYGHILSDPGVGGVSPLTTHHSPLIFSSKVKDLSEFLAETGFM... | Cofactor: Binds 2 [4Fe-4S] clusters.
Function: Component of a complex that catalyzes the oxidation of glycolate to glyoxylate.
EC: 1.1.99.14
Catalytic Activity: (R)-lactate + A = AH2 + pyruvate
Sequence Length: 443
Sequence Mass (Da): 49514
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A0A972R3H7 | MTSNETTQYDTIIIGGGVSGLVTAVRLKYAGQSVLVIEKKDQAGGAISTSHAEGFLFEGGPNSALDSNPLISELFQSLDIQGERCNAAPESSNRYILKHGELIPLPMSPPAFFATRLFPLRAKLRLFREPFIKPSPPDADETVADFVLRRLGRDFLDYAIDPFIAGIFAGKPDQLSVRAAFPKLFELEQKYGSLIKGQIKGKKERKKRLEKSKQTAGMFSFFNGMETLPRAMHRYLGNAVLLSTTVEAFSRSDGLFRVDLGERTVTAPRLVISAPADATAKFIKELAPDLGREFTAIPYPPVAIVGMGFKREDVKHPLDG... | Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis.
Function: Involved in coproporphyrin-dependent heme b biosynthesis. Catalyzes the oxidation of coproporphyrinogen III to coproporphyrin III.
Catalytic Activity: coproporphyrinogen III + 3 O2 = coproporphyrin III + 3 H2O2
EC: 1.3.3.15
Subcellular... |
A0A345UIG3 | MRSAMNLRITLLFFFLGMMVLSGCRSQRDTVRTGTVFERGEASWYGPGFHGQATANGERYDQEALTAAHRTLPFDTVVGVRNLHNGKKVVVRINDRGPYANNRIIDLSRAAAREIDMIQSGIAPVELTILRSPVPVQRAAIARELFTVQVASFNTRQEATAHARSIRGARVAEGRVQGQTVYRVYVGEFRNQRDAERQRRRLSRQGINGFVKQVQN | Function: Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides.
EC: 4.2.2.-
Subcellular Location: Cell membrane
Sequence Length: 216
Sequence Mass (Da): 24301
Location Topology: Lipid-anchor
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A0A151F9Z7 | MKNKFAQAMKEKESQLCVGLDPRPEQVQRDSIYEFCMNIVEQTSEHCFCYKPNTQYIMPLGFSEIKKLNEYIHEKGCLSISDHKLSDIGSTNKAALHWLSKMGFDAVTYSPFPGNIKETIDNAQNYDLGVITLTLMSNPEADFFMKSVIQGKLGYEFIAEQIAKYDGFGAVIGATCRVEDIKRIHSLLTDQLILSPGVGAQGGGLDIVRIFKERTMVNVSRDIITRDNPGERAQYYKELINNTLQE | Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC: 4.1.1.23
Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Length: 246
Sequence Mass (Da): 27780
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A0A1L5KQL0 | SRQHLAPVSLVESSIMDTITLTGVHANGTHGVLAFEHERPQTFVVDATLHLNLTRAGQSDDLNDTIDYGRVAKDIVAVIEGPHVGLIERLAQLIADRILADAPAVMQIDVTVHKPHAPIVVAFDDVSVSITRVRDGACGDAEQALSEQLHEPASSVVSPVIPSMHSAVVALGGNVSEVESTLRAAVREIDALPGTQVTGISPLYRTAAWGMADGTPDFLNAVVEL | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4.
Function: Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin.
Catalytic Activity: 7,8-dihydroneopterin = ... |
A0A971GPB9 | MKIKGLDNAVLLLDKPAGITSFDFISKIRRIARIKKIGHSGTLDKFASGLLVICTGQATKLTRYFLESNKRYTGKIRLGIVTDTCDITGEVVSRNDLQNINEFTIREAMARFIGDSVQVPPEYSSLKIRGERASDRVRRGETVTLEGRNITITRADIIAIDCDNGTVDFDIACSKGTYIRSIARDLGEVLGTGACLQELRRTESGKFLVENAASAEDVEAYAGCKIPAFFALDPAAALCSFGRIILDEAGAAKVLNGACFKRDEVVDHEIKALETYLVFDSHEELIAIADMDIDSWWINYHSVFNKMESY | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
EC: 5.4.99.25
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Length: 310
Sequence Mass (Da): 34266
|
A0A930X755 | MTLPEDSQQDPLELTIDALTVLPRTASLLERQNPEAVLSGASYQVLSKLGEGAMGMVHLVRDLHLEREVAFKQLIGASGSQSEAVRRFLGEVQITAQLSHPSIVPVYSLEQTDKGLGYTMKQVQGDTFKELIQAARAAVSAGTRRPPHLSRQTLIAHFLKVCDALAYAHYRGVIHRDLKPANLMLGAHQEVYVMDWGIARPFGAAAAAYPFEAEEAGKLIGTPRYASPEQARGLNAQLDPRSDIFALGLILHELLCLQPAYTGKGREAMLERVRQAQRDPCTALPGDEPLPPALIAIVDKATAWKRAHRYASVQELAADL... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.1
Subcellular Location: Membrane
Sequence Length: 697
Sequence Mass (Da): 77152
Location Topology: Multi-pass membrane protein
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A0A364K3N9 | MIILEGAGVMKHWRVIYSFILVIAWLGLGYFYFAYSLDPPKRDKDVVIDIPPNTSTDKVVQMLKEQKVVNQDWFLSFYIKYKNYEIKAGTYHVKPNEHVYYLLPRLAKGKEDRVHVTVVPGATIPEIANSLKAKGFDSEGFLKALKNRQPKYEFEKEIPDNPDAYHKLEGYLMPQTYLLTKGQNPEEIVDQMLGEFDKYHQKNKEKFRSIKLQNGKPLGVSGVVSIASMIQKEAFKQEEYPLIAGVIYNRLNNPSTYPYLNIDATSVFANKMEGNKYKTPYDAIQNIKQYNTYKSKGLPPGPIGNPGEATLNAALNPDKH... | 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: 365
Sequence Mass (Da): 41888
Location Topology: Single-pass membrane protein
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A0A7C2PQA2 | MMEEDSKRLLILAAGQSSRMGSLGQKQFLELQGLPIFLWSIKTALALSSNYSLTIVLVHSVGDREKYKDSLIKNLDSSSLPSISLVEGGASRSQSVYNGLQSISHDAEPNDSIIIHDSARPFLGVQDLLKVIDSLKHYSAVTLSYPVTNTIKLLKADTQEIQAHLKRDDLRAILTPQGFRFSVLWKAYREFIRSPYPVTDDTEIVAKMGHPIQCIDGKKSNIKITNPEDLLYAEFYCQKYNLKPSEKP | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6.
EC: 2.7.7.60
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate
Sequence Length: 248
Sequence Mas... |
K2C0B9 | MQMKNFPSLRLLLHDWVTLSKTQDITCEKITLDSRTVEPGSIFFAIPGLKEHGKIFMEEALSKGARAVVSDSLDENHVDILNYAEKKIPLIYIQNLKKYLGCIASRFYQHPQHTLDLIGITGTNGKTSCSHFIANALRDYGTPCGVIGTLGYGIGAHLHPLNNTTPDIFTLYHILRELHDQGARCVAMEVSSHALKQERIQGLKFKVGIFTNLTQDHLDYHGTMEDYAQCKKSLFHDYPVQSAILNIDDPHGLTWLDTIPEEIKKQAYSLHEKASSSYPLTHVQSFNSNKDGVFAAIKTPWGDGVFHSPLLGKFNLSNLL... | PTM: Carboxylation is probably crucial for Mg(2+) binding and, consequently, for the gamma-phosphate positioning of ATP.
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in... |
K2CMH0 | MVIVGLTGGIASGKTTVAHLFSQWGVDVIDADLVGREILEKNKIVSSEIKKKFGKEICKTSGKLDTKKLRKIIFENKNKKIWLEKLLHPIILEKIKKKIKKIKSSYGIVVIPLLLETGPFPFIDHVLLVDVSPATQIKRLRARDGLTVSEARAALANQLSRRARLLGAQDIILNEDSTSFSELAKQAKKLHKRILAADDIEKMKRYTPHAGKLHLFKE | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
EC: 2.7.1.24
Subcellular Location: Cytoplasm
Sequence Le... |
K1YK09 | MSTEIETIQKTAQAASEAVEATGGIGSLGINLKIFIAQAINFLIVVLVLWRWVYKPLVAILEKRQAHIEKSLKEAKEIEERLALVEKERSLVVAQARKQSADLLAKAEEQSKEQAQKMALSAKEEVQKILNNAKIALVAEKQAMIHDAKSELAKIAVLAAEKILSENIDKKKNELIAEKAIKDLV | 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: 185
Sequence Mass (Da): 20445
Location Topology: Single-pass membrane protein
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A0A5P9NN57 | MVFSRQHCRVHIVLLLILCACRVSAVSAGEWLSGGRAIMGTEVRVELWADDADVGRALQAQVFAEFERLDTMMSPWKPASEISRVNREAARSPQKVSAEMFNVVLRSLHYSQLSNGAFDISFAAAGQHYDYRSGKRPERETLKAAQAAIDFRSIVLDAQGQTIAFARPGMALDLGGIAKGYAVDRGISILVAAGITSAVVSAGGDSRILGDMGDRPRMIGVRHPREEGEYAAIIPLVDTAVSTSGDYERFFEEEGVRYHHILDPATGESADGLQSATVIAPLSLDCDALSTTVFVLGIERGLALVNSLEGVDAILIDADG... | Cofactor: Magnesium. Can also use manganese.
Function: Flavin transferase that catalyzes the transfer of the FMN moiety of FAD and its covalent binding to the hydroxyl group of a threonine residue in a target flavoprotein.
EC: 2.7.1.180
Catalytic Activity: FAD + L-threonyl-[protein] = AMP + FMN-L-threonyl-[protein] + H... |
A0A9E5XVS3 | MDIISVFIIAAGLSADSFAVSAADGLANPDIKLKNVLQIALIFAIFQALMSVTGFFAAYSFSDYLKVIDHWIAFILLSFIGTKMIYESLKKDNDDFLNLKLTPLTIAAQSFAASIDALIAGVSFAFIKINIGLTATIIGIVTFLFSLSGFYAGKKIGNRFSGKAEIFGGIVLILLGTKILIEHIRY | Function: Probably functions as a manganese efflux pump.
Subcellular Location: Cell membrane
Sequence Length: 186
Sequence Mass (Da): 20102
Location Topology: Multi-pass membrane protein
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A0A924E1R0 | MSLSEDAVSPRRSTLVFYLTALCWLALDQWSKSQVVQHIPLGSSMPVIAQYFALTHVTNTGGAWSLLAGKTIALGILSLAVCVGIMVYEQRLRQRVLVQTLGLAFLLGGAAGNMIDRLRLQHVVDMFDLQWHGHNIFPIFNVADIGIDVGVGLLLLVSFLERPQVQAQPAAPESAT | 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-, ... |
A0A345UH61 | MSSHYKALTRKYRPVRFSDIVSQEHVSSTLQNAIESGRISHAYLFCGPRGVGKTTMARVLARTLNDIGDDVDGEMLNQTLNIIEVDAASNNKVDDAHRIRESVRVPPQSGNYKIYIIDEVHMLSKQAFNALLKTLEEPPAYAIFIFATTEPHKVLPTILSRVQRFDFKPISVQQSVDRLRFICEREDITIDEDSLHMIAVKADGALRDALGILDQVIALCGTDIQYEALMKAFNAVGLERLFELTGYIDSGDSVAGIQLISDLLMEGHDISEFLGSLTGFMRNLLLARDPSNFYAIETSKDVKLRLNKAAQSFSDDDLMR... | 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: 679
Seq... |
A0A6P3DNL0 | MARILILFLINLMFPNLLLGDVISSQVDDLSYRLPIEIKPNFYELNLTVNLNSNLSETDFKFTGEVKIDIVAETQDVRSITLNMKNLTIKNISLYHSNKTAIKLDSTVYDDVHEFLIIMLDDKLKKGNNYLLTVSYSGVVNDQLRGFYRSRSADKNGNLIYVAATHFEPTGARLAFPCWDEPAFKARFNISITHSKSYHAISNMPVEELKVENDMKTTKFKTTPRMSTYLVAFIVSNYECNEDGMFRVCTKPQAVNQTHYALEKGKKLLDALNEYTAINFSHYLPKMDQVSLKDFSAGAMENWGLVTYRESALLYQDGVT... | Cofactor: Binds 1 zinc ion per subunit.
EC: 3.4.11.-
Subcellular Location: Cell membrane
Sequence Length: 923
Sequence Mass (Da): 107007
Location Topology: Lipid-anchor
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A0A920AB92 | MNLVAIFIGGGLGSLCRYGMGKFIMSYDSSVLAYATLFSNVLSTIVLALFVYFFQEKIDLNEVWKLLVVTGFCGGFSTFSTFSFETFEMLKNGQTALAFANLFLSVLLCLFVLYIIYKKSII | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 122
Sequence Mass (Da): 13617
Location Topology: Multi-pass membrane protein
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A0A1S8G2Z7 | MSKSTVKRIEQINHSVKQISKGNLEVHIPVLKSDEIGELATNINGMAESLKESIEKEKRSQEMKNEMIHNISHDLRTPVTSLIGYVDLVESKLHSNVEECNQYVAVLKRKSDELKNQIDDLLEYCHINYKEIQLHKEIIGVKALIEQIMIDFVPQLDEAKLHFEIECKQNLQIEADIHVIVRLIQNVISNSISYGKSGKKIIIQILQKKPNVEIKIKNYGQCISKEDLPYIFEKFYRGEKSRNAHTGGKGMGLAIAKSIAQLHEGDITVCSSNEETTFTILLPEYKEEL | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 289
Sequence Mass (Da): 32979
Location Topology: Multi-pass membrane protein
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A0A924E1A1 | MAAPRLFVDPAALHHGMAHLNKDERRYLITVLRLDIGAKVTILDGVGGLYQSTIAQVGKEAVVCELGPLETATGESEREVHLWMACIKSDRMEWLIQKATELGVAAIHLMDTARTVMHHPDGKMDRWRKIAREAAEQSERGRIPAILDSRPLAGRSLPLGAFYCAERRPDVPSIRTAAGKNAGEALHVLVGPEGGWTEAECAMFAEKGAGPVSLGTRILRAETAAIAALALLLLE | 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
S... |
A0A6S4QG54 | MIEIDFAGIPFKTPLVGVSGTAGYITDFKPFTDMNAFGGIAFKSITPLKRQGSPPPRVCECEAGFINSIGLQNDGIEAFLTCHYPRAQAIPVQKIVNLAAFSIADFTHLVRKVAELDDIALIELNVSCPNVDYNGRDFASDSGLLRELIVSCTPLKKDKPLMIKLSPHGAVISELALLCEKYGADALSLVNTFRGMKINIDTWQPFIKKIVGGYSGIGIKPISLAMVYEAAQTVSIPILGIGGVTSYEDVIEYMLAGASLVGIGTASLMNPRIPKRILKRFKAYLHNRGIVAADLIGAMKECP | Cofactor: Binds 1 FMN per subunit.
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway.
Function: Catalyzes the conversion of dihydroorotate to orotate.
EC: 1.3.-.-
Subcellular Location: Cytoplasm
Catalytic Activity: (S)-dihydroorotate + A = AH2 + orotate
Sequence Length: 303
Sequence Mass (Da): 32679
|
A0A933UYJ2 | MELTLPALLTAAILGLVQGLTEFLPVSSSTHLRFLHALFSFDAGASSVAFDVTLHAGTLCAVVIVLWRPQIIQKTPALRTVCMLAVSLASTVIVYIILKKAGITMKDSAVGADEHAVLIMFAAGLLVTGVLLIATRFIKNNTRDALSLGLVFAVVVGSAQGLALLPGISRSGITIISSLFLGAAPGFAGTYSFLLSIPAILGAAAMDIRHIAALDPLVLAVGFICAFISGFAALKLLITLIKKGRFYFFGFYCIAAGITALVVLLR | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
EC: 3.6.1.27
Subcellular Location: Cell membrane
Sequence Length: 266
Sequence... |
A0A931GH48 | MSIARTSQAASGEPRLYRRMLVLAAAILLIDQASKAWAISALSDGRNITLIPDLLGLRLLYNPGAAFSIGAESTWVFTLATAVTVAGVLFVGRRLRSAAWTAALGGLLGGAASHLLDRLSREPGFGRGHVVDFIDYGVFVGNIADIALTVTCAAIFLLNLRGVPLGDAADRPEPEPPAAEDGGAPPARTERA | 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-, ... |
A0A532V5V8 | MNNTGKLIVYEGIDGSGKTTQLQRSAEWLSSRKYLVRTYREPTSGPHGQKLRQSASTGRLSAEEEMNLFLRDREWNVTTRIRPALSERVTVLLDRYYYSSIAYQGARGLDTEMIRDKNRKIAQEPDLVLLFDLDPEMAIDRIRASRGDTPNLFEKIDYLKKVRAIFLSLTDPNMVRIDASEPIDTVWQQVEEALASLFPHP | 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: 201
Sequence Mass (Da): 23122
|
A0A9E7HK43 | MESCRGVQVPPVILMCSVRQQLESANLQRSYFDNKLKNATRDTNMKFRNPKFLSMLNQLRFCLLEMYLKLHKIPFFTALWKIDKDGKVKGAVDTCFRLLHSHARSSSWLTSIPIPMKNPLELACKGRRY | Pathway: Glycan metabolism; pectin biosynthesis.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 129
Sequence Mass (Da): 15051
Location Topology: Single-pass type II membrane protein
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A0A2H5YQA2 | MLRRRSASAVIIVLVAVVPALLGGWVFIALLIAVGLLGLWELARAFQHAGHTIDFRLSGVLFLIILLSITTGRSSAVLLLSTGTAVLVPLVWALRSTRHEEALAHAALTSLAVLYLALPLGAASMLRELDGTSLGGWLQSTAERLSSGDTALGLAWFLWGLSVTWLTDTAAYLFGTRFGHTKLVPHLSPGKTRAGAIAGLAAGAVTGLLGAALFGLPLPLWLAPLAGLVVSLTAQIGDLAESLIKRAACIKDMGNLIPGHGGVIDRIDALLFTLPLTLALATLVAEVHWP | 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: 290
Sequence Mass (... |
A0A924E3L0 | MVFPADSRATWIASWHDRRVVVLGGARSGIAAATVLQTLGARTVLSDRGQLGAPTMDQLTTVGITCEGGGHSATLLDDAVMVVPSPGIPLDAPILTEAVRRGIPLIGEIELAYRLCPSPMVAITGSNGKTTTTSLIDAILQAQGRNVGCGGNIGLPLVSIAQQAWEVLVAEISTFQLETVHELAPETAVLLNLYDNHLDRHGSRDVYFGLKAKLFARQTASDRAVYNADQPEIVRRLSGIASRHFPFSRLQTLPNGTGLADGWVVVWEDGQVTPVMPVSEIPLPGDHNVENVLAAVAAAWPYCNDVAALRETIRTFTGVH... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
Catalytic Activity: ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-... |
A0A6I8PCF8 | RFTVPAFRRLPILAPSPHREPPPPVLTPSPHPPVWILGIPTVPGTVTLRKDPQNLIGISIGGGAQYCPCLYIVQVFDNTPAALDGTVAAGDEITGVNGKSVKGKTKVEVAKMIQVVKGEVTIHYNKLQADPKQGKSLDIVLKKVKHRLVENMSSGTADALGLSRAILCNDGLVKRLEELERTAELYKGMTEHTKSLLRAFFELSQTHRAFGDVFSVIGVREPQPAASEAFVKFADAHRNIEKFGIRLLKTIKPMLTDLNTYLNKAIPDTRLTIKKYLDVKFEYLSYCLKVKEMDDEEYSCIALGEPLYRVSTGNYEYRLI... | Function: Probable adapter protein that bind to and organize the subcellular localization of a variety of membrane proteins containing some PDZ recognition sequence. Involved in the clustering of various receptors, possibly by acting at the receptor internalization level. Plays a role in synaptic plasticity by regulati... |
A0A4R1ETK5 | MGTLGDTLITKQLGLTDYESVWESMKNFTQSRDQDTPDEIWVVEHPPTFTLGRNGKEHHILQETSIPIVKVDRGGQVTYHGPGQIVIYLLLDLHRRGIGIRQLVTLIENCIVELLSAYEVTAYSDAKAPGVYVDKKKIAALGLRVSKGRTTHGLSLNVDMDLTPFGYINPCGYEGLEIIQCKDLGITDSMPVLSEKLTAIIHAEIMKAAETAKTTD | 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-A... |
A0A7C5W7R4 | MDKRTLLGLLLIAVLTTLWALYTSIYFAPRVPSADTTRPSPAAIAPQPSSSAVLETAPAAPEQWLEVETDLLRIRLSSWGGTLTRWELRRYKDWRGEPVQLVPPGEAELSISYYDAQGRRIELRRFPFVFSLPPNSQYRVAGSDSLVVRARYAIDSLRFVERWYVFYGNRYDIKLGVRLVNLEELVAQRRYELSWSGGLKYQEYNSVDESNSAAALISLAGDVEKLDATKFDEPAETHVTGRIDWAGLKTKYFAIAFVPSPRPAELTVFARGQRFHAPNSGIVERYDLTFRLPYRRGEEQQVFQLYGGPIQYDVLKSYGL... | Function: Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispa... |
A0A316ZD69 | MSTRSRARGHAPRQASEPCISTSALGEGETERTPLLAASTSASHPGLTASSSATSTAANSANDLEARWSRWKSKVARFAQGKRRAREDEEQLEPRLLVSVFDGAGADEAQQEEQGEDGISEKELWHQVSQVRAAIAQGLYPKMITTGSSGSYFARARIAVPRHGSSSKTDAVVTTLAVFKPKDEEPYGNLNPKRLFLRRYFSWAMGRPCLIPNFSAYSEVGASYLDARLALHLVPRTELVSLASPSFHYDYKDRMAHERQGKELPEKLGSWQTFLPGYTNASDFLRAHPWPSRPRALLERDLVAEARAHRKSRKKQGKRV... | Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ADP + H(+)
EC: 2.7.1.67
Subcellular Location: Cell membrane
Sequence Length: 813
Sequence Mass (Da): 88907
Location Topology: Peripheral membrane protein
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A0A933PXI8 | MSKNVKLVIVLLLFGITLWFLWPTLQWYSFTPKAEKEKTEYSIDTMISKGYTSEQVTQVLKLKRLRSQAVNLGLDLQGGMRVVLEADFDDYAKRLEKSVKEITPEEKSDGMARLLERLRGRIDKFGVSEVGIRRMDDARIIIELPGAKDPDRIMDVIKAKGKLDFMFVDEEATKAISTNDVWLGSFTNYAKVPAGCTNLYFYGKKDEFHRRVRGAPLILKTNIVLAGDMLKEARVGSGEFMEVTVDFELNAQGAEIFGEVTAANIGKQLAIVLDGNVMSAPNIRSEIPGGRGQISGGFDAQEAQDLATILREGALPLSIK... | 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: 503
Sequence Mass (Da): 55705
Location... |
A0A316ZD86 | MASAAPPPRRPSAAVLLLLSAVLLPLLSWLRPAAPGCVLRYGDFHLRFSLPLLALAAAAARPLLTPLDMARLVLLPAIAFVWTTPWDNEIVRQGAWSYPPPCVMARVGWVPVEEYAFFIIQSLLTTLQAVLLLRWLAPTPARAHRPLLFLLPLGVFFLGARFARPGEHSYYAGMIAWWAALPLALLWWGTQGAWMAMPRTHKAMWAAAWLAPSALLCALDRFAIHRGTWHITETTSFNIFPLPDLPIEEMCFFLVTNLILISASLAFDTCALQLRRTHASQTTPLSPSYMPLRASSLAALWTAFVAAPTGPSAADADAEV... | Pathway: Carotenoid biosynthesis; beta-carotene biosynthesis.
Catalytic Activity: 2 (2E,6E,10E)-geranylgeranyl diphosphate = 15-cis-phytoene + 2 diphosphate
EC: 2.5.1.32
Subcellular Location: Membrane
Sequence Length: 663
Sequence Mass (Da): 71697
Location Topology: Multi-pass membrane protein
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A0A269TII2 | MLFSYLKLKELAGLDNSVTIEDVSKAINSIGFEVESISSFQNVEGIKFGHVLKTYKNPEGDNLTVCEVQFNDQVRIIQTAAKNVVDGAYLMAFVPGSKLKGTTIEARKMKGIVSEGMMVSFAELIPNDTLAREEHKNGILLIDKIDLNLDPIKYYKLDDQIIDIKILTNRSDANSYLVMAQELRAYFQVNQKLENSSNKYELNKNLKVTKNEVENFVLLKTKDKFGITIEEQILLAKNNIKSINDVVDLTNLSLIMTGMPTHVYYEKDLQNVNISNSNDKVEILGNKEVKLDNTLVIKNNNDVISLAGVMGIEKFSVKES... | Catalytic Activity: ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) + L-phenylalanyl-tRNA(Phe)
EC: 6.1.1.20
Subcellular Location: Cytoplasm
Sequence Length: 717
Sequence Mass (Da): 82097
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A0A0E0B6B3 | MLAELAGSPGVDAVVFTVFTPSLMFASLAKTVTLSDVISWWFMPVNIGITFIVGGTLGWIAFCDEDGNPFGKDRSLCRSRGLSYSSLSMALGGLFIWTHTYSLMQKAGKMYHKMQFKSIQCPADSDEEHHPAQGHDQVKLDGETAYADEEAALLVSAKLAPEHNEENQMEAPLLTCEREIANKGGFWTNLKETVHQVVEELMAPPTVSAILGFVVGLVPWLKSLVIGNGAPLRVIQESLQLMGNGTIPCITLILGGNLTQGLRKSVLKRTVIITIVCIRYVIQPLIGMAVVHAAYGVGFLPHDPLYRYVLMMQFALPPAM... | Function: Involved in cellular auxin homeostasis by regulating auxin metabolism. Regulates intracellular auxin accumulation at the endoplasmic reticulum and thus auxin availability for nuclear auxin signaling.
Subcellular Location: Membrane
Sequence Length: 371
Sequence Mass (Da): 40670
Location Topology: Multi-pass me... |
A0A269TIL4 | MLITLEGLDGSGKTTIANSIFNELVGLGLEKNFIFTREPGGAGIIEAEKIREVILDSHSRLSNISEALLYSASRRIHIDRVIEPNYENKIIICDRYIDSFYAYQGYGRELGIKWTKDLTELVIGKYKPDLTIFIDITYEETRNRREKRETTDRLETQSQDFYKRTYEGYWKLINEDRERFLVIDGKLSVEEIVKIIMDKIKTLDKFKKMGK | 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): 24663
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A0A8U8BXK5 | MEQRRSVGQEKSGGKSVGQEGSVGGSMGQEGSEGGEGSPLQLQVEVMVREGRALAVLGWWELLRGLLVFALCSHPRLQQDPEAFLRASRRVLGARLWRALLSVSLWGQFAVGRSPAAVQELGQRLRARGLRPLLALPIEGEGPDGEG | 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: 147
Sequence Mass (Da): 15780
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A0A0Q5GAL6 | MPIQETLETSHTFLARLASEAAAFLPNLIAAILILAVGLFLAGRLANLVTRAFGVSTKVDQTVREPLVAIVRYVVVILTLIIALGQVGVQMTSLLAVLGAAGLAVGLALQGTLTNIAAGIMLLWLRPFRVGDYIETQTFAGRVHQIGLFVSHLETFDGLFVFAPNSTLWNVWMRNHSRAASRLLAWAVTVPRDMPFEAARQALIEAWQQESADGRLSEPVAFLDQLTVDAQILVLRGRVTEGETATAQRRIAEAIRTRFLQRFGEGQEPRAIQRIVPADNDPSRYLGQDEAPAANPTLVNDRPETPSQGVVTTARG | Function: Mechanosensitive channel that participates in the regulation of osmotic pressure changes within the cell, opening in response to stretch forces in the membrane lipid bilayer, without the need for other proteins. Contributes to normal resistance to hypoosmotic shock. Forms an ion channel of 1.0 nanosiemens con... |
A0A971GK46 | MPSAVAEVKKTILLVEDEFLIAMMESRDLEAGGYYVIHAADGPEAVAVIHEKGEAIDLVLMDIDLGPGMDGTDAARQILEIRDLPVIFLSSHTEMEIVRKTEEITSYGYVVKNSGVTVLLASIRMAFRLFEANRKIFLKNNEILRASSRLMELNEELLRSRNSIAESEERYKRIFESFIDIYYRVDASGIITEVSPSVEELSGWSMGEVIGRSVRDVYLEPADRELFLSAIAREGRINGYEVAFKRRDGQVIPISIHAKLIFDKNGAPAGIEGTLRDISGRKRTEDMFYRTFEKYRMLVDNSVDMIWTMDTSGIITYVSP... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cell inner membrane
Sequence Length: 943
Sequence Mass (Da): 103131
Location Topology: Multi-pass membrane protein
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A0A4R5TJH7 | MNRLFPRFAITCVVAMALSACATQPRRPAGPADEAAARMHDQQRAAITGWQLSGRLAVSSGSQGGSGRIEWSQDGDRYVISLSAPVTRQSWRLTGDPTGARLEGVEGGPLEGDDSERMLLAATGWRIPVRAMVAWVRGIAASEDMAAPARVVHGADNLPASLEQLGWRIDYRDWHPAATDRPALPRRMDVVDAARGDARVRLIVDQWQVTQAQAVQPGIGIEMLDAAGELAAALARLDLEDPAADLRRQVAGGDLRPLVVCGFACLAPGDPEGVLPEGEVRILDGSGDVVLGDRHLRLKHKAEAYARAYNQALVAWHTEA... | Function: Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein.
Subcellular Location: Cell outer membrane
Sequence Length: 332
Sequence Mass (Da): 35554
Location Topology: Lipid-anchor
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A0A4P5US73 | MFDIGGAEFLMIGLAILLLFGPKKIPEVMHSIGKGIRYFRKAQEDLKSQIRDISTEVEKQTNITNTVINESSSQIQIDTTIVESETQTISIRPAEGSLARNVHIDEIQEDSTHISDPNPQKTLEQGE | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
Subcellular Location: Cell membrane
Sequence Length: 127
Sequen... |
A0A9E7JYE9 | MITCWQLGLRNLPLQKTRRRLGGGDVPLLPVPSLWSHALLIVDYIHFQYNGWLRPRLSPLFRLSVLEEGKDVAGGLILPGPICFFHHFFVHLLRHHCRRGPWEASRRFPTMGTAMSTVSSRRSVHSCSMSRFVLIVQFVHTRMPMVAHDDQEMDKVHNRYKKTEKQVHSCLFPFGRGYACRQVSAFWVPCIVLDKALAFVLAKLELDVPAPKASSRRAGFSRYLKIQSAPQGNQTECFKCFRCKTRIYQTIWNALPSGIVGGVLRSATAPIYSMGSGS | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 278
Sequence Mass (Da): 31540
Location Topology: Multi-pass membrane protein
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A0A0B5I1P0 | MKELFDDYKDKLPTVVLEEIEALAESRNLNKTQVKKVIELAYEEYRNSMIEPGESVGLISAQSVGEPGTQMTLNTFHFAGVAEFNVTVGLPRIIEILDGRKNISTPMMEIYLVEPYSKGKDIKTIAESIKQTQFKDIVKEINLDITEATLEIKIDFEKMKRLGLNEAKLGKVLEKSLKGFTLKLKDDTLTLKSKGKQDNIAELYKLKEKIKSVYVSGIKGILQVLPVKREDEFVIVTAGSNLKDVMKLEYVDKTRTTTNDIFEIQALFGIEAARQAVINEVYNVIENQGLNVDIRHIMLIADVMSFSGKVRGITRYGVVS... | Function: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Forms part of the jaw domain.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
EC: 2.7.7.6
Subcellular Location: Cytoplasm
Sequence L... |
A0A0A8UQ96 | MAEIQIKVPDIGGSTDVDVIEVMVKPGDEISSNASLITLESDKASMEIPSPQAGKIKSLQVKVGDKVSEGDVILTLIVDEAESTKSAPESTEVTKQDESEKPKAQESKQTKATSASQRLEVRIPDIGGATDVDVIEIMVTVGQSIEKDQSLITLEGDKATMDIPSPAAGVVENVSVKVGDKVSQNSLVLILKTEQGDIAAEETPTAAEKIESDQEQPREKQASTEVVAVHTLPESTVGSNIPAGPAVRRMAREFGINLAEVKGSGRKARITKEDLQAYVKGRLSEKPATGGFALPTAPVIDFSKFGDIETKPLNKIKRLT... | Cofactor: Binds 2 lipoyl cofactors covalently.
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 (E... |
A0A1D8TF41 | MKKPFGLLMIITLFIGCSHYIPQSESLTTADDGNKDTFLDIAIKMGKEIGQDFQNVFRFGKNIIRNMLGEPTTIDSNDNRSKIKEHLSTMAKGLTNIKNELNNKASQEENTTKEANEVIDKIIAAINKIAEATDTNIGIGETKNDNKKKASIISNKQSVQSIINGIKEIVDIAKTSGVQIEKKDDDNTSISASSNTAATAALNGGGLYNAGAGQGSGAALAKVVSEADPWIMIDKIINASIASGSIHGNDNNNAGQLITGTTSEDKGAGSKSKADLAAAVALKAMSKGGQFAAYKTDNNNEEYVKKVKEAASEAVNKVLK... | Function: The Vlp and Vsp proteins are antigenically distinct proteins, only one vlp or vsp gene is transcriptionally active at any one time. Switching between these genes is a mechanism of host immune response evasion.
Subcellular Location: Cell outer membrane
Sequence Length: 341
Sequence Mass (Da): 36166
Location To... |
F6UT00 | MEMMAGRGEVDHPVNMLPVDGKGDESRPDAAPSLPVPECAICLQTCVHPVSLPCKHVFCYLCVKGASWLGKRCALCRQEIPEDFLDRPTLLSPEELKAAGRGNGEYAWYYEGRNGWWQYDERTSRELEDAFSRGKKSTEMLIAGFLYVADLENMMQYRRNEHGRRRKIKRDVVDIPKKGVAGLRLDCEPNGVSPARESSADGADGTSARGGAPPPPPAPSPAPSRPPTALDGPPPGPAAPSPAAGAGLEDSLAHLQLGGDGPGGRGPRGEGEEGREAPLPAGLPPPDAAARDGESDGDDGAAAPARRPSARRRLANPSGT... | PTM: Ubiquitinated; autoubiquitinated.
Pathway: Protein modification; protein ubiquitination.
Function: E3 ubiquitin-protein ligase that specifically binds poly-ADP-ribosylated proteins and mediates their ubiquitination and subsequent degradation.
EC: 2.3.2.27
Subcellular Location: Cytoplasm
Catalytic Activity: S-ubiqu... |
K8ZQJ0 | MESIPITYDYYAREEWANLNHQKMAIPLSEEELQILISTQDQLNLQDIQEIYLPLLHYLTLIYEEYRSLQQKRASFLQKRNTSIPFIIGIAGSVAVGKSTLARVLQVLLERIYGLSVSLVTTDGFLYSKSELEQKGLLDRKGFPESYDMPKLLHFLEELKVGKKEVHAPIYSHEKYDIIPDEVITICEPDIVIVEGINVLQNPWNERIYISDFFDFSIYLDAEIFRIQQWYCDRFLLLRGNEFATKEEAIRIATKVWKSINEKNLLEYILPTKYRADLILHKTKSHFMDYILLKK | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
EC: 2.7.1.33
Subcellular Location: Cytoplasm
Sequence Length: 295
Sequence Mass (Da): 34693
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A0A4R1ET05 | MKPRHKRLAFVLLALISVGAASALISKAMKGNLAYLHSPEEVLNGVVPTGQVFRLGGLVKEGSLERSDSKLEARFIVRDNRDHEITVVTNKILPDLFKEGKSQVSRGKMGEDGLFYADEVLAKHDSEYMPQELKDTLEKEHTVNASEGTK | Function: Heme chaperone required for the biogenesis of c-type cytochromes. Transiently binds heme delivered by CcmC and transfers the heme to apo-cytochromes in a process facilitated by CcmF and CcmH.
Subcellular Location: Cell membrane
Sequence Length: 150
Sequence Mass (Da): 16589
Location Topology: Single-pass type... |
A0A9E7EN21 | METPFASPKIRLASEFTAFIRLGFFFKISRANPRFFLTLAKLQDGEPTNLMIVDVGEEKQAKLAGSETLTRSSSSDRVNSPPPEHEEEEESQQTQPLRQQGLPPHKVARVSSDEVTMAAPSSLMLGLGLGLGRGPGAAKPVFTFMQLQELEHQALIYKYMAAGLPVPVHLVLPIWKSVAASSFGPYVYPSCSTPPS | Function: Transcription activator.
Subcellular Location: Nucleus
Sequence Length: 196
Domain: The QLQ domain and WRC domain may be involved in protein-protein interaction and DNA-binding, respectively.
Sequence Mass (Da): 21385
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A0A1L5KGR0 | MAVLQVLHIPDERLRKVAEPVKEVNAEIQRIVDDMFDTMYAEEGIGLAATQVDIHQRIIVIDVSENREERLVLINPELLEKDGETGIEEGCLSIPEQRALVPRAETVKIRALDREGKTFELESDGLVGYLYPA | Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
EC: 3.5.1.88
Catalytic Activity: H2O + N-terminal N-f... |
A0A660TTK8 | MKVAVFGASGYGGQILMRLLLDHPEVSKVLPVSSTSAGKPVDGRDSGLGPDLKGKLPEGRTFLSREEALEEKPDAVFSALPHGASAEFCEPFFGKSVVFDLSADFRLRDEKVHLQAYGAPAPYPELRSAAVYGLSEIYETQIRKSDLIAVPGCYPTCSMLPLIPLGREGLITSTITINSLSGISGAGRSAKEASLFVERSENSVAYNPGLKHRHLPEMIQEFNAAGGNSPIFFTPHLAPMRRGMLSTISTSVTGEPKAVFNKVEAALTAAYQGQPFINLTGNRIPSTRDVVGSNRCDIGWTVEGPINGSSMLYLFSTIDN... | 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 = ... |
A0A345UHS8 | MIPPGFENRLFTAAQSRDIDRRTIEELGIPGFTLMEVAAQRAADHIFEMQPGPVRVLSFCGKGNNAGDALAVSRLLLMKGFSVDVCLALGKTGMSADAAANLRILEKMLEADPELPLRFFEGVLPGRVYCTVIDGLFGTGLQRDVTGPLAEMIAEINRWQARVFAMDIPSGLHADSGAVMGTALQAHTTLMFGTAKAGCYLGRGAALSGKRVLCPLPFPAHLLREAEGAVLRSLSPGGKPQLENKLRKLREGREVRHKYQNGNVYVLGGSPGLTGAVILTAKAAWSTGCGSVQVFTTPEVSPAYDAHFVDITRKMIPGDG... | Cofactor: Binds 1 potassium ion per subunit.
Function: Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that... |
A0A159U821 | FIFGMWAGMMGLSMSLIIRLELGNPGSLIGNDQIYNSIVTTHAFTMIFFFVMPVMMGGFGNYLIPLILGAPDMAFPRMNNMSFWLLPPSLMLLILSMFVGSGTGTGWTVYPPLSSNLSHSSSSVDLSIFSLHIAGISSIMGSINFISTVFNMKIHKIENIPLLAWAMLLTAILLLLSLPVLAGAITML | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A660TDD6 | MNREAGKFFPVSDASVRAGGTFVSYKNSDPDIVSISIDSRTVSSGGLFIALNGEITDGHKYISSAFESGASAAMISSKYYAKHYNNVSFFNGCLIVVEDTLSGFHKLAASWVADFGKLTRVAVTGSNGKSTTKEMIGSILAEDGSTVINKGNLNSETGLPLSVMGIKKEHKYGVFEMGINHPGEMKALVSVFSPQFALVTNIGTAHIGPMGSQEAIAAEKSEIFSLFDKDNTGFIPDNDSWADYMETHCPGKTIRYGLNSTEGVEKAFNLGLKGWNIQYKNLEINLKLVGQHNLNNAIASISLSSALGIIPDKIKKGLEK... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein.
Catalytic Activity: ATP + D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-d... |
A0A9E7JKC3 | MVFDQMQRFVAPDVYSYTILIDALCKRRNVEEAMALFSDMERSGISASIVTYNALIDGLCKRNMLKEAFALKEKMVRISINPSIVTFGILINGLVKLDRFGDVELVLTEMEEIGIPPNVVIYNTLIYGHCKMGRPTEALKLRDKMVAKGIEPNCVTYNIIVQGLCDAGDMKQAEYILDEILSNGMEVNAGLFGSIIFWLVTKEQRLDCAVRLLGEMLLRNLRPNDSLLTTLIVELCRMEEAIGLLNQLKDEDLVPDLFTCSMIIDGYCKVKEIDKAKSFLKEMRTWGLEANVVVYNSLVSGFCKNGNITGASNLVDEMKS... | EC: 7.1.3.1
Subcellular Location: Membrane
Sequence Length: 1008
Sequence Mass (Da): 108160
Location Topology: Multi-pass membrane protein
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A0A923XTY8 | MNDEQKSGEYYSFKVDNSQELMRIDFYLLNKIRYATRNKIQKAAKENKVLVNNVPVKQSYRVKPNDNITILINEPKRNKEILPENILLNIIYEDDFLIVIDKPAGMVVHPAFNNYSGTLLNALEYHFNQTNNSKERLVKSGLVHRLDKNTSGLMIIAKEKETLDNLLKQFFYHSIERIYQTLVWGNINLKKGKIITNLEKDSKNKNIKVSITGKQAITNYLVLEDFYNSSLIECKLETGRTHQIRSHLAYIGHPIIFDDLYNNVENNQIFQKINLQVSNTLDRQALHSSSIKFIHPKLKKELFFQSPLPNDIKNTIEYLK... | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 326
Sequence Mass (Da): 37998
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A0A7V5SGP4 | MNIAVTYVSGAGNTFTLVREGRRRFPVEVWQRLAPQLCRWTDGLLVLRKADARGVVPVLFFNPDGSTGMLCGNGARCAASIAMGERHRELTLLFADMPISAVAVEGGIRLRLPPPRIFPQERQLRLPTGDLRLWFADVGAPHVVIPIHELSSTGIHSSLEQLPVEQLGRLLRFHPAFAPTGVNVSFYTIAEDGSIQVRTYERGVEQETQACGTAAMAVALTAWSAERLHPPITILPPSRSPLRVDWEGEAPEQLQALFLEGSVEVLGTDTVEVSLEEDE | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.
Function: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacte... |
A0A1F4CYV6 | MAEVRPVLAAASLARPKGERAAARREHWQKVAIAACEQCGRNRIPQVHALVPVEQYVLKENSSQKILLSPRAELRFSEACRTLGESLTLAAGPEAGFSAAEEAALLDCGFVPASLGPRVLRTETAALAALAALNALRGDF | 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
S... |
A0A7C5S5V5 | MPVVSPYGRDNAAVLFGLAAIAALVGGSLGGIASWIGGVVAGALVGLTLWFFRDPDRAIPAEAQRDGVVLSPADGRVVQIVRLQEPEFLGEEAVQVSIFLSPLDVHVNRVPVSGIVRFLRYVPGRFFAAYRPEASRQNEQTLIGVETPCGKVLFKQIAGVLARRIVCTLQEGQRVQAGERFGMMKFGSRMDVLLPALRAELCVREGMRVWAGQTILGYLIPESAGLSQRDT | PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme... |
A0A7H8PWW5 | MNNIDSNHYGDSFSSEEFVDLRKYFSILWSYKFPIVTVGLIAGILAAGFMWLQPKQYQATSTISFASGRANIVQIREIVETGNENRDYLQTQAEVIRSRQLASRVVERLQLTKASFDAPPNAITSLFELNGPTKPASELDSDAAMQQADQAAQESSETVPVSDARTSELTPEEVVSANSAPTSALLVNMLIKNLSVELVRGTQLITISVVTHSSELSAEIANTLAEEYLASQLEQKRDVASEATDWLGERLDVLRTNLEESEQTLLAFQRAENLVDVDGVRGLAAQELNEVTTQLLVAKRQLQQVSTSYQLVRRRGDDTE... | Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Subcellular Location: Cell inner membrane
Sequence Length: 782
Sequence Mass (Da): 86395
Location Topology: Multi-pass membrane protein
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A0A1I7YFW1 | MFILQTSIPQVSILQTSILCNVCSWQRPGALSLLRRQQIVNAFALELSEIRTSLQLISFLPFNGCFVFFLTAFCSHKYFSNFTLRQKRHSLSLSLKFAMIHFLHVSCLKRPFALRFLIGSVFSLRPPPSDMKRIKLTNRCVFVGIFLAVVSITIAILIFFSAPYRESSPDMEKTLYIMKTALNKANCLDHFWSRTGLXXXPLFSRTGPPLKCDEDVDLLVGVISLPSDFELRRTIRRTWADQSRYDTRRTRVLFFLGRQKNVSIEKEMDTYGDIIPITNDESYYNLTLKTYALLTYHQDYCGQAKCVLKVDTDVVANLAG... | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 485
Sequence Mass (Da): 55303
Location Topology: Single-pass type II membrane protein
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A0A1C9EYM1 | WSGMVGTSLSVIIRTELGHPGALIGNDQIYNVVVTAXAFIMIFFMVMPIMIGGFGNWLVPLMLGAXDMAFPRMNNMSFWLLPPXLTLLLSSSLVEAGAGTGWTVYPPLSSTIAHAGSSVDLAIFSLHLXGISSILGAINFITTIINMRAPGITFDRLPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNLNTSFFDP | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
K2A4M4 | MHLTGYKFENTFWRKGLSVAGADEVGRGSFAGPVVASAVAFAPHSCYRASLLKQKIRIDDSKKLSVGQRECADSWIKASCIGYGIGVGSVGLINRAGIVKATNFAFRSAIKKFTISCMLSIDYLLIDGFYVPNVANIRKSKQIPIIRGDAKSMTIAAASIIAKVYRDSLMVALNEEHPEYFWYHNKGYGTVDHIKSLERFGPTKHHRKLFIRNYI | 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.
Seque... |
A0A496QR17 | MGTNMINDYFDHVSGNDELNRNFVRPFSGGSRMIQLGLLTPPEALTASLVCFFLGSLVGIYLVWTRGPLILILGIVGVISGFFYSAPPFKFANRGIGELIIGLNFGLLMAVGSYYVQVQSFDAELVFVALPVMFLITAVVYINEFPDYEADRAVSETTMVVLLGRRRAVTGYVVIMTLAYLSIILSVTGGMISPHALLGLISLPLAVKAVDYLRHYYEKPFDLVPANVSTIMAHLITGTLLISAYIIERLGLKAVVALLPLAIVTVMVIVWLHRHIENQRRTFEGIRKAT | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis.
Subcellular Location: Membrane
Sequence Length: 290
Sequence Mass (Da): 31930
Location Topology: Multi-pass membrane protein
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A0A1L5KXW7 | MNLFQAIVLGIVQALTEYLPVSSSAHIRIVGDLMLGSDPGAAFTAIIQIGTELAVILYFRHDIANILTHWFACLFGKNGKDWKARMGRGDNYATLGWNIIVGSIPIVILGFTLQNVIETTLRNLWITATVLLLFGILLWVVDARAKQTKTMDDMTYRDAFLFGLGQSMALIPGVSRSGGTITVGRALGYGP | Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
EC: 3.6.1.27
Subcellular Location: Membrane
Sequence Length: 191
Sequence Mass (Da): 20801
Location Topology: Multi-pass membrane protein
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A0A2N9MNS5 | MRRRVAVKLVKAGMNTREVIARFESERQALALMEHPAIARVFDAGATPEGAPYFVMEYVAGVPITTYCDSHRLSTRERLELFMQVCQGVQHAHQKAIIHRDLKPSNVLVMEVDGKPAPKIIDFGVAKALTQKLTADTMFTRLGALIGTPEYMSPEQARSSGEDIDTRTDVYSLGIILYELLAGVPPLDLRKIAFEEFLRRLREEEPPKPSTKIRTQDEATSTEVAHKRQTEPLALAKQIRGDLDSIALKALEKDRSRRYGSPSDFAADIARYLNNEPVTAVSPSFGYRAGKFVRRYRVALATICAFVLVLVAAAAISIRQ... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.1
Subcellular Location: Cytoplasm
Sequence Length: 886
Sequence Mass (Da): 99373
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