ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A661EGJ5 | MSLIVVGLNHNSAPVNIREKINFSEAQLQRAYGELLKISQIKAVLIISTCNRTEIYANSNQDGIDIIIRKLYEFHNLSAHQIVPYLFSYQNNEAINHLFGVCCGLDSLILGEPQILGQVKAAFKTACQYDAINSYFYKLFECSFATAKLVRTKTAIGANPVSVAFAAVSLAKQIFGGLEQYTALMIGAGETVELAISHLKKNKIKNIIIANRTYEKAQKLAKTCDGQAIIIKNIPDYLLQADIIISSTASQLPLLGKGAVESALKARKHKPMFMVDIAVPRDIEEQVNELDDVFLYTVDDLQDIITENQKSRQTAAIEAQ... | 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... |
A0A6L7MV34 | MTNAPAYIGRFAPTPSGPLHFGSLVTALASWLDAHAAGGQWLLRIDDVDTPRVDPAAEEAIVRALDAHQLHWDGTIVRQSDHEERYRAALRRLQPLCFACRCSRRVLGGARIYPGTCRHLGLAKSATTSIRIRVDDGRIEFEDRVQGRHTQQLADESGDFVVWRRDDMAAYPLAVVVDDDAMGVTHVLRGADLLPNTPRQLYIADALETRRPSYAHLPVIVETGGIKLSKHTGATALDNRFARHNLTNALNLLGFEPPPGDIPELLAWAVANWNIRRVPAVDAFTGFIALSS | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2-cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC an... |
A0A920RJN5 | MIVGIYNGFFSPAEAAGMGVLATIVMMVGLGKFTWRKFFDAVSESVKLFTFMFVALMAAVMFASTIALSQLPQFIADWALAQVDSPLAILYMIIVIFIIAGFFLESFGMVMMLVPLFFPVMVQAGFDPVYFGVIIVMLMEVGLLTPPAAPNIYVTQYVGRGGRCDGSHQWHATLLRYRAGIDGAPGAFSDDCDVAAGDHVINTQPKEKN | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 209
Sequence Mass (Da): 22744
Location Topology: Multi-pass membrane protein
|
A0A967VX41 | AETEAARLSGRRSARVHLRPGAWLGADGAERTGPPPAPALAVAGVGRPADFFDQAAAAGARLAETLAFPDHHPYRAAEVAELLRLAAGGPLVTTAKDAVKLAPLAPDADLWVLDQQVVFESGEGGLLDAVDGVLP | Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 6/6.
Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form te... |
A0A2E2U0G2 | MCSESIDFLVPESESNGTYVDATFGRGGHARKLLSVLGPNGRVIAIDKDIEAVTEARRLGVEDHRLVACHGSFSDIHDHLKTVGAEHVDGILMDLGMSSPQIDDSDRGFSFSKDGPLDMRMDQTGSMTAADWLNDASVEDISEVINRYGEERYSKRIAHSIVNERPLRRTADLVAAVAKGQARSSRGKHDATRTFQAVRIKINNELVDLEKGLIDGFNALKISGRIVVIAFHSLEDRIVKRFFRTLTHKPAIPRRIPIRYEKSKISAGVVSKALRPTREECERNPRARSAVLRAVERLL | Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.199
Subcellular Location: Cytoplasm
Sequence Length: 299
Seque... |
A0A2E2ZE65 | MQFSKNWLKDFIDLDLSTEEICYQLTMAGIEVDNFENVKSAITGNDAIIKLDITPNRGDCFSILGVARELAILNNLKLKLPKIAKLKSTYQDTISVNACAEGPVYFGRTVKDFDMNAVTLPHIAERLTLSDQKLIDPVVDITNYIILELGQPLHAFDRDKLNGDISVRLAKKDESITLLDDQTLNLDASCLVISDEKEAVAFAGVMGGKDSSVTSSTSSIFLESAYFKPSVIRGKARKFGFQTEASLRFERGVDYTIQEFALNRATYLLNQTIGGEIGSVISDSLIKELPNHKKINIDIDRTNKILGTTISTNSAKNYFK... | Cofactor: Binds 2 magnesium ions per tetramer.
Catalytic Activity: ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) + L-phenylalanyl-tRNA(Phe)
EC: 6.1.1.20
Subcellular Location: Cytoplasm
Sequence Length: 677
Sequence Mass (Da): 75660
|
A0A2E2WSB8 | MKGFLITGTDTDVGKTWFMLRFGEFLIENKIEFHFLKPVESGCIEPNNKIIPKDATKFSILEKIPLNKICKYTFKAYASPPKAAEMENRSIELSDIVSFIKINKSKNANCINLVEGCGGLFSPIAKNKLTSDLAKELKLPIILVVKNTLGCINHTLLSIEAIRNLNLKIKFIILNDVTKETPLDNFDELSNFTDIPIFKLGYNGKIDSNLMEQLT | Pathway: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 1/2.
Function: Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.... |
A0A2D5I417 | MQDISPLLSKVNLNKKVFIAYSGGVDSTVLLHAFYELSKVNKINLEAIHVNHNLNTQSKLWEAHCKNFCNKRAIKLHTASVKITKKGSGMESAARNERYQIFQNIISNEGQVLTAHHQDDVAETILFRLFRGTGIDGIRGLQEKRKLGNGVLIRPLLSFNKKELEEYATLNKLECIEDLSNHTNEQDRNFIRNELLPIIDSRWKKVANRINTTASSIDTKLGIFNDLFYSTYGSLISDSIPIDGIRAVEREVAVEILRASIRKNDIAMPSKKVIEEILKTFLLSRPGPKSIVSWSRSDKDQPGGYITYKNKTIHIHKS | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
A0A661EG96 | MANLFIITAPSGVGKTSLIRELMQQDVLSINLAISHTTRPARDGERDGVEYYFIDELSFKKMINDNDFVEYAEVFNNFYGTSKQEIANKLSENQNIILEIDWQGAKIARKVFKDAISIFILPPSIGTIEKRLNIRATDNLDIIKNRLKQSKIELSHYDEADYLIINDDFQQAVQDLHNIIVASHNNIKTMQKQYSELIESLLK | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
EC: 2.7.4.8
Subcellular Location: Cytoplasm
Sequence Length: 203
Sequence Mass (Da): 23311
|
A0A2E3UVZ1 | MIEYFIKEFFLIEVKILKALKDNYVYLLHDPLSKQTAVIDPSDEKVVLKELKNLKRQLNYIFITHHHWDHIGGNLKLKEATGCQIIGAKKDKMKIPGIDQMLEEGDSFKFGDTRAEIIETPGHTKGSICWYFKDESILFTGDTLFSLGCGRLFEGTAKQMLESLQKIKNLPTETKIYCGHEYTLQNAYFALSLDQDDQNLKDKIKDLEKISKAQTPSIPSFLSEELLMNPFLKTDKPSLQKKISPENLEEWEYFSLLRKMKDNY | Cofactor: Binds 2 Zn(2+) ions per subunit.
Pathway: Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 2/2.
Function: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
EC: 3.1.2.6
Catalytic Activity: an S-(2-hydrox... |
A0A920LG46 | MSKPSLKIKTKSNFSDSIVEWYKVYGRHDLPWRNSVTPYKVWISEIMLQQTQVKTAIPYFKKFVRKYPTLRSLKNASEDEILSLWSGLGFYKRARNIFATKEIIFDQFNGEFPTTFEKIIKLPGIGRSTAGAILSIAFNNGTPILDGNVKRIIVRHFDLPEDTKDKELWNYSEIMLSDNDPFIYTQGIMDLGAMICRPIDVSCNDCPVSSTCLQAFKPKIKLRNNVKAVKPVIEMNLLLCRHDNELLLKKIDDQEIWRGPLDTS | Function: Adenine glycosylase active on G-A mispairs. MutY also corrects error-prone DNA synthesis past GO lesions which are due to the oxidatively damaged form of guanine: 7,8-dihydro-8-oxoguanine (8-oxo-dGTP).
EC: 3.2.2.31
Catalytic Activity: Hydrolyzes free adenine bases from 7,8-dihydro-8-oxoguanine:adenine mismatc... |
A0A2A5D0S1 | MKPAEFKQRVTKWFKLHGRKDLPWQQNPTPYRVWISEIMLQQTQVNTVIPYYLKFMEKFATLESLAKATDDEVMALWSGLGYYSRARNLHKTALLISNDLNSLPEDLDDLVALPGIGKSTAGAILALSMDKKAAILDGNVKRVLARYFQISGWPGEAGVLKKLWQLAEILTPDFSVKDHSVKNYTQAMMDLGATICTRSKPACTSCPLSQSCLANKDGDQLNYPGKKKKKILPIKQQNYYLITNDNSEILMEKRPNTGIWGGLWTPLSCAQDIHANGNKADGFLLEEFGIKISDPARLPEFRHTFSHFHLQITPIKAKLK... | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Adenine glycosylase active on G-A mispairs. MutY also corrects error-prone DNA synthesis past GO lesions which are due to the oxidatively damaged form of guanine: 7,8-dihydro-8-oxoguanine (8-oxo-dGTP).
EC: 3.2.2.31
Catalytic Activity: Hydrolyzes free adenine bases from 7,8-... |
A0A9D8P2B0 | MSGFVLINKPVGLSSHQVVARLRKFFNTRKVGHNGTLDPFASGLLILSVGEHTKYMPYLPQSPKHYIGTLKLGEHTETWDKDSPITKTMPIPSLHHDLIVEAFSDICTMTTQEIPAYSAKRHEGRRLYEYARNLEETPKLYKPIKIETLRLISFDNHQIQFAACVSSGTYIRTIGQDIAKYLGTCGHLTQLTRTAIGHVDLTHSQELDDDLKCNTIPLDHIPAHVFNQSDIQKLCQGQILPNRNIAPGLYQLLNSESQFQGLIEVNHHSILAKRMHNPQNNK | 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: 282
Sequence Mass (Da): 31878
|
A0A534CC19 | MRLLVLNAGSSSLKFDLMEVPVDGPARPLKAGAFVDTADGSGAFALQTAEPAPPRSAPIRTLAAAADFVLAWLSQESVHGRDLLSGLDATVHRIVHGGESFRATARLADPQLASLAELNVLAPLHNPPALAVIAAVRARLGTLPVVGVFDTAYYAELPEAARCYAVPKRWQEAFGVRRYGFHGTAHRYLCHAARARVPAGRASSRVISLQLGRGCSVTATLDERAVATSMGFTPLEGLVMGTRSGDVDPGALLYVMERGGLSAAQVSRELNYESGLLGLSGRSADMRELLALEQGGDAGARLAIEIFCRRARHYVAAYMS... | Cofactor: Mg(2+). Can also accept Mn(2+).
Pathway: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 1/2.
Function: Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction.
EC: 2.7.2.1
Subcellular Location: Cytoplasm
Catalytic Ac... |
A0A8T7A3L1 | MARRKNKGRVLNGLLLLDKPAGESSNRVLQKVKRIFNAAKAGHTGTLDPLATGLLVICFGRTTKISDYLLAADKKYRVVLKLGVTTDTADADGEILEQRDTSKITEDQILQQAASLTGGIKQIPPMYSALKHQGLRLYELARKGIEVERVPRKVEIYSFEIIEYQGDLVTMQVHCSKGTYIRTLVEDLGKLLSCGAHVVELRRTSLGPFTDPIMHSLEELDQLAEQGFSAVEQILLPTDHALQDWPAISIDENQMIDIRNGHAMCLPNLPAEGQVRIYDADQKFYGIGTMREDGRMAPKPLN | 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: 302
Sequence Mass (Da): 33566
|
A0A534AEJ2 | MHPRPASGDDETATETIAAVATAAGAGGIGIVRVSGPRSAAIAHALTRKRLTPRKVYFCTFFDEHEAAIDRGLALYFAAPRSYTGEDVLELHAHGSPVLLAVLLRRVITLGARHARPGEFSERAFLNGKLDLAQAEAVADLIASGSEGAARAAMRSLEGEFSARVHEVLAELVQLRVWLEAALDFPEEDFTEEEQDFLAAPQLLHGLHDVRHRIDTLLSAARRGVVLRDGLHVVIVGRPNVGKSSLLNALARSERAIVTPIAGTTRDLLREHVDLDGIGLTLVDTAGLRESADIVEVEGIRRARAELERADVAILVTDAE... | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
EC: 3.6.-.-
Subcellular Location: Cytoplasm
Sequence Length: 463
S... |
A0A8T7BA45 | MNRHPKLQQNNPSGPRPDQKPDAAVAKVRQVVVDADQAGQRLDNFCMAQFRQVPKSRIYRAIRKGEVRVNGKRKKAEYRLQADDKVRLPPIVHDAQKSIPASPSLIEQLEQQIIFENDQLLVLDKPSGVAVHGGSGVSHGVIEALREARKDQLHDVSKMELVHRLDRDTSGCLLIAKKRSWLRALHKQMRENQIEKRYLALVKGQWPHGRYVCDAPLAITLRGQGERYAYVSENSNEKGAKSARTEFWPQDFYQGATLMAAQLHTGRTHQIRAHAKHLGHPVAGDERYGDAGFNRQLKHFGLRRLFLHASFVAFTDPVTG... | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 344
Sequence Mass (Da): 38791
|
A0A967VPJ0 | NTVARAVESAAALDVDMLTLHASGGTAMMRAARDAVGLDGPKLVAVTLLTSFSGSDVEEVWGKELRSIRDDVARLAALAAEAGLDGVVSSALEVEAVKRRHGSAFLVVTPGIRPEGEEAGD | Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
Function: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).
EC: 4.1.1.23
Sequence Length: 121
Sequence Mass (Da): 12441
|
A0A6N9CQ46 | MEPRIALSRTAAWAGGLLGALVLAAAAAVWWIDRWWTAPLTLASPAVLVLESGDTAVDLAAKIEAAGWLEHPRLLPWIMRFRGDAARLQAGEYRVAAGETLDGLMARLLVGDVVVHSFRIVEGSRIADLLNTLGMDGRFTHTLGAARPETLLADLGSEMAPEFGAHGEGWFFPDTYSFTLGDEDRTLLLRAHAKMRMELEAAWAGRAPGLPYGNPYEALIAASLVEKETSRAEDRAHVSQVFAARLKRNMRLQADPTVIYGLGEKFDGNLTRAHLRQPTPYNTYVHKGLTPTPIALPGRAALAAVLHPSGAEYLYFVARG... | Function: Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation.
EC: 4.2.2.-
Subcellular Location: Cell inner membrane
Sequence Length: 353
Sequence Mass (Da): 38398
Location Topology: Single-pass membrane protein
|
A0A964PKB5 | MKITNANLEWRDDGMPYAIDYDDVYFSRDDAEGESRHVFLDANRLRSRWQSLLPGSRFTIGELGFGSGLNFMQTLRLWQELPTQDSRLHYIAFEQHPLTHADMLRLHRRWPDCAEISQRLLQQYPDHTAGCHRLQLAANVVLDLYYGDASAQLSATAAFAHCHIDCWYLDGFSPARNPQLWQPQLLARIAALSSHGTTLSSYSVAGAVRQKLAAAGFSVQKLPGFGRKREMLYATLTQLEDPAVKEASIKDFYADAPWLRLPAAVAPATQGYAIVIGAGLAGCSTARSLAARGWRVTVLERGPRAASGAAAIPQMALRCR... | Function: Catalyzes the last two steps in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to fo... |
A0A2D9XG00 | MANGRVDSRRQRINNVNSESEIHKRKNDHLALAGSPSCQMNSSNGLETVRFEPVALPELNFAEIDTRVQFVNKPLSFPFLISSMSGGVREADKMNTTLAEAAEACQVALGLGSMRIALEKKSARTSFKLRSIAPTIPILANIGGTQLIQRNGTSDALRCIELAEADGIYVHLNALQELLQPGGDTDWRGVSAAIKELVAESPVPVFVKEVGHGISASSAKILIDLGVSWIDVAGTGGTSWSQIEHTRSGVRGTSAFAEWGVKTREAIEAIRGNGNSCKLVGSGGLRNGLDVAKVIRIGADIGAAAQPFLEPARTXVDKTI... | Function: Involved in the biosynthesis of isoprenoids. Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP).
Catalytic Activity: isopentenyl diphosphate = dimethylallyl diphosphate
EC: 5.3.3.2
Subcellular Location: Cytoplasm
Sequ... |
A0A967VMY8 | MSTTTAPPTPPRDTDRPAGGAAGTRIRRLIRWLDDRLGFSALAPLAKKKQVPVHRHSFWYYLGGMALFLFLLQIATGILLLFYYRPSAEGAFESVQFLMAEVEFGWLIRSIHSWGANLMILTLFVHLFSTLLLKAYRKPREITWMSGVALFGLALGLGFTGYLLPWNELAFFATRVGTEIPAVIPLVGDFLKEVLRGGEDITGATLTRFYALHISVLPGLAIVIVGLHLLLVQKHGMSVPPGVEKAGGPRRTVPFFPNFLLRDLVGWLAALALLAAAAAFFPAHLGEKADPFAPAPAGIKPEWYFMFMFQTLKMLPGHIL... | Cofactor: Binds 2 heme groups non-covalently.
Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis.
Subcellular Location: Membrane
Sequence Length: 383
Sequence Mass... |
A0A6P2BLC4 | MSPRTMQLMVDEAQWIATDAEFAALCESARDADSVAIDTEFERTDTFYPKLALVQFCIGDRIALLDPLALADVTPLRALLEDPSTEKVLHSCSEDVEVLAAWCGARPQALFDTQIAAAFCGGRYGIGYRDLVVQEFGVELDKDATRSNWLHRPLSAVQIRYAALDVALLLPLKARQEEALSVEGRVHWLREECDRAVSDVLDRPGPETAWRNVKRAGTLGARGLAALQRLAAWRERRARELDRPKGWLLKDEQLILLAGRLPERIEDLAGEGLPAGAVRRFGSELQPLLDAARGLPESELPQALPPPMGRAENERMKAFR... | Function: Exonuclease involved in the 3' processing of various precursor tRNAs. Initiates hydrolysis at the 3'-terminus of an RNA molecule and releases 5'-mononucleotides.
Catalytic Activity: Exonucleolytic cleavage that removes extra residues from the 3'-terminus of tRNA to produce 5'-mononucleotides.
EC: 3.1.13.5
Sub... |
A0A7C7Y0X2 | MILELDAGNTRIKWRVLEADSTVASEQGYVGTEAELADLEFAAASLSAIRMSSVRSEEANQLVSKWAVRTFNLSLQLAKVSRSCAGVTNQYKDVSRLGIDRWLAMVAAHNRCGGPCVIVDSGTALTVDVVNSDGVHDGGYIIPGIELMARTLETNTSIKLDPNRASPIPELGHSTDAAVRGGSLASLLALIEKVVSTVIKESPKSKLYLSGGDAELIQQHIVNIDAEIVATLVLDGLAFACPAGVT | 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... |
A0A8T7JDW2 | MKKIISFTITVFALLSCSSSEEPIRLTGQTMGTTYSIVISDPADISATALQREVDQRLLEINESMSTWIEDSELSRFNQSTSTDWFEISKDFYDVLSLSLDISQQTDGNFDVTVGPLVNLWGFGPKSTSANRVPSEAEITQAKMHVGFKYLSLAQSPYRIKKDNPAVYVDLSAVAKGYGVDQIATLVESKGVDSYLIEIGGEMATRGQSPRGTPWRLGIERPDANLRAVIQQFEISEANMATSGDYRNYFEIDGKRFSHTLNISTGYPIDHRLASITVLADNTATADAYATAMMSMGETVGLEYAERAGISVLMIIRLDD... | 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... |
A0A353D5G0 | MFDIGFFEIIFIMVIALLVVGPERLPRIARTAGLWVGKMRGFVSSVKADIDQELAAEELKKVLAKQAAVPELEELIDEVTGNPLAATESKSSGSSEKMLPADQSDRPAETRVTDDTAK | 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... |
A0A9D1TNC3 | MLNIVLVNPEIPQNAGNILRTAIATEAVVHFIRPFSFSLDQAHLRRACLDYYPKRQVVIWESVEDFLKENGEKELFLFTKKAKKIYTDTDYRDKKEIFLVFGKESSGLDPSLLLKYPDRLLRIPTSSSVRSLNLSNAVAISVYEVLRQKGFDKEWL | Function: Could methylate the ribose at the nucleotide 34 wobble position in tRNA.
Catalytic Activity: 5-carboxymethylaminomethyluridine(34) in tRNA(Leu) + S-adenosyl-L-methionine = 5-carboxymethylaminomethyl-2'-O-methyluridine(34) in tRNA(Leu) + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.207
Subcellular Location: Cyto... |
A0A2E6YAU0 | MKIQIYAIASRSTDGFEENFSIYQKRLPAHINLKLTTIPLAYRNKNSPIEEAVEKESELLLKRINTKDTLIVMDENGKTLSTKDFSNWMDQWMLNSINPILAIGGPDGFSNAMHQRANNHLSLSKMTLPHALVPVILAEQIYRAWTILDGQPYHRS | Function: Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
Catalytic Activity: pseudouridine(1915) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(3)-methylpseudouridine(1915) in 23S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.177
Subcellular Location: Cytoplasm
Sequence Length: 156
S... |
A0A661CD54 | MVLRIGLTGGIGSGKTTACEIFTELGVPVIDADIIAHELVKPGMPALEEIIRIFGEEVISNDGTLDRKIIRDKVFANNLDRKKLENILHPVVYKEISAQVENINSRYCIISIPLLLETGASKTVDRILVIDVPREQQLERASNRDKTDKNDINAIIDSQISRKDRLSAADDIVDNNGDINDLRKKIYELHEFYSNI | 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... |
A0A2E5VAU6 | MTKNSDINYIKKSLELAKLGLFTSDPNPRVGSLVVKENKIIGEGYHKRSGSPHAEIMALEQAREGATGATLYVTLEPCCFKGKTNPCTKAIIQSGITKVVCSTEDPNPKVSGKGIKELRQAGIRVELGILANKSKELNNGFFKRMLSDMPFVRSKLAISLDGKTALNNGISQWISGNSSRLDVHRWRARSSAIMTGSSTIFADNPSLNARLEDSVEINQPIRVILDSEVSISDSAKCLSIPGDIIIFTNKKELKNISKKIRNRAQIEIVNGNHHCEINEVLNRLSELEVNEILVEAGSKLNGSLLELGLIDELIVYISPK... | Cofactor: Binds 1 zinc ion.
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 2/4.
Function: Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'-phosphate.
Catalytic Activity: 2,5-diamino... |
A0A661D851 | MTNSNTKSIKDSVHNKSVLNSPDIDFVQWFRNAAPYINAFRNQTFVIYFSGDVLADNEFPSLIHDITLLNSLGVKLVLVHGARSQIEKRLNESNIQSEFFQGLRITNNKIMQVIKEVSGSIRINIEALFSTSLKYTPMAGSHINIISGNYVTARPKGILNGVDYLHTGDIRKIDTSSIEHSLNAGDVILLSPVGYSPTGEIFNLNGEDVATLSSIDLNADKLIFIDDAQGIFDHNHQLLNEITTRELKTIISETDAEQSDIIRHYQRISHASEMGVERVHIIDRNIEGSLLLELFTQKGIGTLVSADHLEDIRSATIEDV... | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4.
Catalytic Activity: acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-glutamate
EC: 2.3.1.1
Subcellular Location: Cytoplasm
Sequence Length: 456
Sequence Mass (Da): 51328
|
A0A353Y0H2 | MLNLTKIDRYISSEILRIFAVILTILVLVLVGGTLVQMLRLAAGGSIPPESIITLAALETLRLSGRLIPAAFFFATVMALGRMYQDQEMTVLQTSGVGPLRIMRIVSVAALPMVLISAWLVLWLYPVAGRVSDELKMQHQDAVLLSAIGAGRFYEARGGELVFYAESVDAASSTLENIFIQIRLKDEVVLITSDKGRHFLNDATNRRQVVLVNGNEYVGFPGSETFSTMHFDEYAIEINAAPGGKARFDYSNVDTIELLTYHDIEARADFQSRLVFPISVMAFALLAIPLSRGSPRASPYTRIIFSVLTFLVFMVLTKSA... | 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: 367
Sequence Mass (Da): 40761
Location Topology: Multi-pass membrane protein
|
A0A534IMJ4 | MARITVEDCLNNVDNLFQLVLLAAQRARRLANGAEPTVPLENPPPTPTTSPPSALRSSASETDGQTSKMDYASSLLGLLPGGRRTPGLKELLSSVGAYLPSDQVARIREAAEFGTSAHHGQKRLSGEPFIAHPVATAAILADLRLDADTIVAAILHDVIEDTPTPKDQLATRFGAVVAELVDGVTKLDQIKFKSREEAQAESFRKMLLAMVRDLRVILVKLADRTHNMRTIEAMAPARRRAIARETLEIYAPIAERLGLYSIKLELEDLGFKALYPRRYQVLERTLRRARGNQKEFLKKIEQQLNAALAKSNIQAQVLAR... | Pathway: Purine metabolism; ppGpp biosynthesis; ppGpp from GDP: step 1/1.
Function: In eubacteria ppGpp (guanosine 3'-diphosphate 5'-diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance.
EC: 2.7.7.6
Catalytic Activity: a r... |
Q73JD6 | MGFKTLAYLSALLYSNDMKNSTTPKRSEIAKSDKWNIELLFKNEEEWEAALASIPEGGKEILKYKEAFSKPETIDAATLLACLKASTGVDRIAEKVGNYAFLQKSSNEGDPENIKRISKYMMTVTELSAATSWLMPAIMEIPEEKIRSWIDPSSPTGKDFADFKVSLEKTLYLKPHTLSDKEEKILSLLSEPHGTPSQAFSVLTNVDFDFGTITTKEGDIKLTQSSYSKFMQNPDRALREKAYKQLYGVYGAHKNTIASLYTGQVQQNVALAKIRGYASAREKSLYVDKVPTAVYDNLVDTIHKNLKPLHKFYSMLKKHL... | Cofactor: Binds 1 zinc ion.
Function: Has oligopeptidase activity and degrades a variety of small bioactive peptides.
EC: 3.4.24.-
Sequence Length: 629
Sequence Mass (Da): 71383
|
A0A938PY60 | MLKFKTRAGEFTVELYEKEAPESCANFLRYVDDGHFDGTLFHRVIPGFMIQGGGFAPGMEQKDTRPPIHNEATNGLENLRGTLAMARTSDVHSATSQFFINLVDNDFLNHQPGNYGYAVFGRVTAGMDVVDAIAQVPTTRRRGHGDVPVDDVVIDSVTRENAA | 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: 163
Sequence Mass (Da): 17946
|
A0A2E9FIH2 | MTDFEVMQRVFDLAIKGGHNVAPNPLVGCVITKNGKIIGEGWHKKYGGHHAEVNAIRDCQKKFGKSAAKKLLHKSTFFVNLEPCSIEKNTPPCTEKLIEFKAKKLVCSIKDPNPLINGRGIKKLKQAGIDVQLGLMKGEARRLNKIFIANHLYSRPFITIKVAQTLDTKIGLRGAGQVRITNNKSIKDVHKLRREHDSIMIGSGTLNEDNPMLSTRFSLSKKISQPIKVIIGNNVNVKSKMGLFKDFSKVIFASTKEIVIPKDLPKDVINFKNAKQNIFENLFSYLLDLNCRSILVEGGSKLFRSFLSKGYYDELIIYTA... | Cofactor: Binds 1 zinc ion.
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 2/4.
Function: Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'-phosphate.
Catalytic Activity: 2,5-diamino... |
A0A2D5PQ55 | MKKHRKKRLFGVLLIIGSSCLGIGLILYALNSNLDYFLTPSELKQNDENVVLSSNTRVKLGGMVKKDSFFINENKVNFEVTDFEDSIKVIYEGLLPDLFKEGKGIVVLGKYIDGIFYADEVFAKHDENYMPPNXELN | 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: 137
Sequence Mass (Da): 15552
Location Topology: Single-pass type... |
A0A349EH00 | MDFKTTDLCDEFSDRLQVAEPIFGDYGGEVIFSGLIVTLKVFEDNSLVRAVLEEPGDGRVLVVDGGGSMRCALVGDQLAELAEDNEWAGVIV | Function: Catalyzes the aldol cleavage of 4-hydroxy-4-methyl-2-oxoglutarate (HMG) into 2 molecules of pyruvate. Also contains a secondary oxaloacetate (OAA) decarboxylase activity due to the common pyruvate enolate transition state formed following C-C bond cleavage in the retro-aldol and decarboxylation reactions.
EC:... |
A0A368BUL7 | MTLVVKLPLVFFYSALLLLAACSKNPDLISLKGNAFGTFYDIKLVTNSVSVSKIKKTLNDSIGEMNKCCSTYDEESLVSHVRDNKSINLFDLRLITIFDEINKISKAVNVITQGFILFDSYDHFNAVAKGYAVDLISSEFKKLNIENFFINIGGEIKAQGNKNDMSWKIGIEYPDEEKQEIFKIINLNNLSVATSGNYKNPGHILGKNKNTVIHNILSISVLDKGSTAKADALATGLYALESLKEVKKIIERNDIPALVIFIDDEEIKSFQSKYWEELLEY | 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.
Catalytic Activity: FAD + L-threonyl-[protein] = AMP + FMN-L-threonyl-[protein] + H(+)
EC: 2.7.1.180
Subcellular Location: Cell inner membrane... |
A0A358Y283 | MKLTLTGRLSKLILSLTCLLTSTVSAQSESPAQKTAQAAIAIPDPYAAAIAKEILMQGGNAVDAAVATGFALAVTYIDAGNIGGGGFMLTHIEGESAFLDYRERAPFAAHRDMYLDEQREVIENATLIGGRATAVPGTVAGMWTAHQRYGSLLWRDLIQPAIKLARQGFLPAQILVDEIHANLDWFGDKTNFKEYFSQISADQLFKQPELAMTLERIADAGPADFYQGETARLIVKQMDKDHGLISMEDLESYEAVWRAPLEARWRNFKVLSAPPPSSGGFGVIQLLKMKDALTPYFEGVEHNSHQYVHLIAEMEKQVFA... | PTM: Cleaved by autocatalysis into a large and a small subunit.
Pathway: Sulfur metabolism; glutathione metabolism.
EC: 2.3.2.2
Catalytic Activity: an S-substituted glutathione + H2O = an S-substituted L-cysteinylglycine + L-glutamate
Sequence Length: 482
Sequence Mass (Da): 52537
|
A0A2D7G378 | MSKDFERSLPGGQSHGATNRLNRIHLDPTLLILVLALCSCGLVVMSSVSGADMTLFYDQVGRLTIGLGILLLAAQAPPSIYLRWAVGFYLLGIFLLVLVIFFGVKVKGSQRWLDFYGLFRFQPSELVKITVPMGLAWYLQNKQIPLRSKHVWISLILVILPVSLIYAQPDLGTSILVAGAGLSVLFLAGISWRWILSALAFVAITLPLFWAFAMTGNQKQRVVTLLSGPEADPLGTGWNIMQSTTAIGSGGLLGKGLGKGTQSHLDFLPEAQTDFIIAVIAEEFGLIGVSVLLALYIAVLARALYLAVTSESTFVRLFGG... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Peptidoglycan polymerase that is essential for cell wall elongation.
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-... |
A0A1G2PCX5 | MKKKIAKQLVKNVSELRRDPVSGDWVVIATGRAKRPNTFAQGHQHDPAYESKENCPFENPQVSGNDKPILVFDHKAREMGKLSQDWFVQVIPNRFPAFAGPSVKRYVKHVGPYTVLEGRGSHEVVIMREHTKNISSFSSLEARAVIYAYMARFNILSLRPNVRYVSIFHNFGKEAGASLYHPHSQIMAIPVVPPDVARSLAGSQRYFQEKSKCVHCEMIAWEKKDNQRIVFENEHFIAICPFVSRAAFEIRIFPKKHESSFKDMGDEEIGKCADALRITLGKLEKALANPDYNFFIHTSPINIESLESHFYPHYHWHIEI... | Pathway: Carbohydrate metabolism; galactose metabolism.
EC: 2.7.7.12
Catalytic Activity: alpha-D-galactose 1-phosphate + UDP-alpha-D-glucose = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
Sequence Length: 356
Sequence Mass (Da): 40649
|
A0A1G7P8L3 | MKRFPNKIKNFIDKHALLSENDRVIVALSGGADSVCLISILQRLGYECEAAHCNFHLRGNESMRDEEFVTTLCQRLGITLHKVDFSTAEYAEQHKQSIEMAARELRYDWFEKLRVQTNAKAIAVAHHMDDNAETFMLNLSRGTGIQGLKGMSPRNGFIVRPFLCVHRAEIIGFLQEIGQDFVTDSTNLEDIYHRNFIRLRLLPEMQTLNPSVMDAINTTSQHIAEAFSIYKEAIDNYRNRLCHATENGMSIDTEELLQTVSPRTILFECLKHTHINETQLDNILAAVKSSNCGRQIHTDTHRIMIERGCIEVILVKETTE... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
A0A520T230 | MKHLIANWKMNFINSDAWLKDFDLNNIPKEIQVVICPNYLDIEDFFEISSKTHEKIFIGAQNLSAEIQGAFTGQISGKMLKNIGASYSIVGHSESRLQGEDDETILRKVHTALECELIPILCIGENQEEYSKGRTENKIKHQLTENLFPLKNLSKSVLIAYEPIYAIGSGIAVKNEHLEEVSLLVNDLVRDNLGIDFTMIYGGSVTSESAKKLAKVNGIDGFLVGNASLDPKEFANIALSLE | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
EC: 5.3.1.1
Subcellular Location: Cytoplasm
Sequence Length: 242
Sequence Mass (Da): 26887
|
A0A9E1NW03 | MMTSVSRQTQISLNTLLQGYVDESNLINVEVTGLSSNSSKVKKGDLFVALAGLTRHAMDYVKEVIDAGAVAIIYDANDSYCLQRIPLLEKQYNVSFIPVENLQQNLGEIASRFYAYPSQQFTLIGITGTDGKTSVTHLLIQALNKLNKKAGSVGTLGYGLSNQLKVTSYTTPDAITLQSILFELSIGSSEYVVMEVSSHALEQFRVSGCQFDIAALTNLGSDHLDYHGDLEHYREAKSRLFSKQSLTGRVLNLDDDFGISLAQTYKGDNVINYSVDATSDVVADVKLLSSMMTDQGIKITVTTPAGLLTIQTGLIGAFNI... | 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... |
A0A8I5TVB5 | METLYRVPFLVLECPNLKLKKPPWLHMPSAMTVYALVVVSYFLITGALPSQGSKSNIFFKAKLLLFLLLAIRCLINVLGKSSLANSVSMLVV | Function: Specific component of the STT3A-containing form of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascen... |
A0A2E4GJM3 | MHKNIFNYPLSYASALEHAVNKFHKAGISNPVIDAKALLCGVSDFSNATLILRGNDIIPQIELEKFWKFVKRRLSGEPIAYILKRKEFWSLDFSVDNSTLIPRPDSEILVEAVIDFIREIDIEKPKILDLGTGSGCLLIAILSELPEAVGFGVDISKAASKVAKTNAKRHELDSRAFFFVGDWAEPINSYVDLIISNPPYIKNQDRKTLAKDIIEFEPNKALFAGKDGLDSYRAIASDIRRILHPGGRIFVEIGAGQSEEVKKIFYDKGFYLVGTWHDLAGIERCMGFATTKLKKN | 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... |
A0A3C1N5Q9 | MLVIFLVIRTLGFLRMAAEGVMPLGRIVSLLGLKVLSYLDVMLPLMLYVAILLVLGRWRKDNELIVLAASGLGLPAFLRPAVTLMLISVLLIGGFSFYLSPLSVQAGARVETELRNRSDLESVVPGLFIESASASAVYFVESRDADSKRLKNLFAYGSDLGNEVVIVAANGYQETRSGTDYLVMTEGVRYDGTPGSPTYRVTRFEKYGIRIQQQSSGPLQVPLRGWKTQRLMGNPRSVADAVAWLVGDPNPLLVSE | 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: Membrane
Sequence Length: 256
Sequence Mass (Da): 28027
Location Topology: Multi-pass membrane protein
|
A0A8T7B2P8 | MGRENNKGNKKSANFDRDSIRVQLEQSLDALPVPEHISVAALAAALTNYLAELHKWNHAYNLTAVRDPGEMVTRHIYDSLTAAPFVSRARVSGKHVADVGTGAGLPGIPLALCFPDTRFMLIDTNGKKTRFVQHVATHLQLNNVDVLQTRVEEFTPEQPFDVVFCRAFTSLAAFAAGCSQLVAPDGCLIAMKGKYPADEVAALAGSGWTVSQSSEVQVPGLEGERHILELRRV | Function: Specifically methylates the N7 position of guanine in position 527 of 16S rRNA.
Catalytic Activity: guanosine(527) in 16S rRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(527) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.170
Subcellular Location: Cytoplasm
Sequence Length: 233
Sequence Mass (Da): 25... |
A0A920MH26 | MAIKAICGLMIESNLVEGRQEIGDGKNLTYGQSITDACIGWNETEKLILETNNILEKK | 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.... |
A0A661FQ57 | MTEKKDNNKMQEALSLDNPAYYYNRELSLLEFNDRVLAQARDKNIPLLERLNYLCIACSNMDEFYEVRVASVIQMAEMDPHVTACDGLNAQEQLDVIGIKAHKLVSEQYRVLHELMIPELAEQDIRFIRRDDWTDQQKDWLKKFFHEELQPILTPVGLDSAHPFPRILNKSLNFIISLTGKDAFGRNSGRAILQAPRALPRIIPLPAEETGGGKYDFVFLSSIIHAFVEELFNGMTVKNCHQFRVTRNSDLYVDDDAIDDLLNAVEGELAMRNYGDEVRLEIDAKCAEETVSFLAARFGINDDQVFLVNGPVNLSRVQEI... | PTM: An intermediate of this reaction is the autophosphorylated ppk in which a phosphate is covalently linked to a histidine residue through a N-P bond.
Function: Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP).
EC: 2.7.4.1
Catalytic Activity: [phosphate](n)... |
A0A525BZW5 | MKIAIIGTGGIGGYFGAKIANAIKDSNDEIFFLARGEHLNKIQSSGLKLITDNNPEIISFPDIASDSLSDFPKIDLALLCTKSYDLDDTSRKLNSITDDHSIVMPLLNGVDIAERVENHLEKGIVLPSCTYISSHIAEPGIIRQIGNDGVVVTGCPTDQPDFDLSKITTLFDRCNIKYQIQNNPHLAIWKKYLFITAFGLVTAYSGKTMAEVVNEAETTILVTTIMNEIIMLALAKGVVFPKNIIGEHLQTAAKYDSKTSYQRDIEANRDSESDIFAATIIKMGEDLQIATPETKKLFKSIENKNS | 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: 306
Sequen... |
A0A525CTP3 | MEIKDNFKEKRLFSNRTIVAAIMVFLMLIILIAQMFNLQILQYEKYRTRSVNNRLKIEPQPPRRGLIYDRDGVILADNTPSFQLTLIPEEVKNINDTTLRLRNIIEISDEEMERFEKLMKNLWRNNLHRFDHIPIKFQLTDNEVARFAINRHLFPGVYVKAHIARRYPLKEVASHIIGYVGRINEIELKTLDYFDYAGSTHVGKTGIEKYYEDVLHGTVGEIKVEKNVSGRYIRTIEETPPKPGNDIYLTINSTLQMEVEKAFGKYSGAVVAIEPSSGEILAMVSQPGYDLNLFVNGISSEKYKELQQDKMQPLFNRLTR... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Catalyzes cross-linking of the peptidoglycan cell wall.
Catalytic Activity: Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.
EC: 3.4.16.4
Subcellular Locatio... |
A0A2A4MKH0 | MSKGFFITGTDTEIGKTTISLGLINVLQHAGHKVSAMKPVASGCVLQNGALRNDDALKLIAACNQELIYDQVNPYAFEPPIAPHIAAEQVGVIINISTICDLANTLQSESDYCIIEGAGGWLVPLNENNTIEDLAIALKLPVILVVGLRLGCINHATLTAKAIQNSGLVLAGWVANHCNKDIEQADKMIGSLKQRIDAPCIGVVDYLYKLDAEAVGSNMDISLLT | Pathway: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 1/2.
Function: Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.... |
A0A2G6EUM9 | MYRLYNQIKDYAWGSHSAMAALFGLPNPDNQPQAEMWLGAHPAGCSAIITDNGPVGLDDFIRTNPGNILGQKTAKHFQTLPFLLKILAAEMPLSIQVHPNKLSAERGFADENARRIPLDAPQRNYKDDNHKPELIYALTPFQALNGFRELAEMIDLFVQAEISSLQQPIAALQQQTDKQGLRRFFTTVMTLTTDIRQQAIKELLRHIGTKGDDIGAKTAFALIKQLSELYPDDVGLFAPLLLNIVTLKPREAMFLYAETPHAYIHGTGIEIMANSDNVLRAGLTPKYIDVKELLEHIDYTPKSFSTLKLHPQTVDAGHKK... | Cofactor: Binds 1 zinc ion per subunit.
EC: 5.3.1.8
Catalytic Activity: D-mannose 6-phosphate = D-fructose 6-phosphate
Sequence Length: 399
Sequence Mass (Da): 43976
|
A0A525CN58 | MPWKQVTFNTPKQHVDPLEDHLLSMGALSVTLMDAEDHPILEPELNTTPIWDNNLVTALFENDTNIDAIAISIKATMSEDVTILKIETVDDQEWERAWMDNYHPMKFGDKLWIYPTNVDIPKTSDTIIRLDPGLAFGTGTHPTTALCLEWLDQADLKQKTVIDFGCGSGILAIAAALLGAKKSYGIDNDPQAIIASDSNAELNNLKETVSAHLPEDTPQIQADIVIANILSIPLISLVENISSLCKTGGELVMSGILEGQIDDVIESYSPYFADFTTSQKGDWFRISALRK | Function: Methylates ribosomal protein L11.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 291
Sequence Mass (Da): 32083
|
A0A9C9G7B3 | MEIDVKKAVKIIVAGLVAVSLSSCSWISDYFDSPDNTEPPAELVEFTPDVDIVERWYLDVDEGSKNLNLQVALSDTTAYVIDSKGLLSAIDPEKGNALWSRKTAVKVRSGPVYDAGVIYLGTRDAELVAVTADKVKDGNGVLWRTSLSSEVLALPTVTDDKVIVRMSDGRITAVSKVDGRHIWSFQRRQPLLTLRGVSRPLVNGNQVLVGLDDGHMVSLAEDTGQVIWDKAVAVPRGTTELQRIVDLDANPVIDQGSLFVASYSGKLAALSVDSGQPLWSRDLSIHSGIAISGSHVVVVDQNDAIWAIDRRTGASYWKQD... | Function: Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane.
Subcellular Location: Cell outer membrane
Sequence Length: 397
Sequence Mass (Da): 43296
Location Topology: Lipid-anchor
|
A0A2D8Y306 | MHKIVHEAKRQEAHPQLTRGQAPPASYYRDNCSEAFDFVFSQYKEMLPQHSLCQLNAYLGCSQDSQRLFARLLTRKGPLFRLDSLNYREVXNXGXAIEELINRRXINDQKVVPADRALGLLTKKELQXLWPHLDLSLRKTDLCLXLLSQHSXXQIVEXVQSXXPFIKLXXRESWSLFEFLYFGNEFQGWSEFVVRDLGIANFESPASTTRQFSSINEMTSHLDLLQCASYARRLDEFTELGGYLVERLKEPRTNLVSSRKRARILSRIAKWAEKNEHFKLACDAYRLIDQHPARERLVRINHKLGKIEERDELLSEIYGA... | Function: Nuclease required for the repair of DNA interstrand cross-links (ICL). Acts as a 5'-3' exonuclease that anchors at a cut end of DNA and cleaves DNA successively at every third nucleotide, allowing to excise an ICL from one strand through flanking incisions.
Catalytic Activity: Hydrolytically removes 5'-nucleo... |
A0A661CAL5 | MNDLRLILLGIGLSIIVLIYLWGTFKQKSEDRARTRKLTSFKRDPVKDAKLIPVFDEDEEASAEVLAEMDAFLNNPEPIDVNTSDFSLPTNNAKLDEGDFKLSKSVAEKPADQKKQSQDVAEDEARQQNSEHQIITFLIKAAPGKTFFGDNILGATDVVGMKFGDMNIFHHHGAEGMQSGQSIFSLASMYEPGYFDPDNMETYQTKGLTLFMQLPAPMDNIQAFDLLQETAMRLADLLQGEIWSTQHEPIDAKALQAMRDIVIEYS | Function: Essential cell division protein that stabilizes the FtsZ protofilaments by cross-linking them and that serves as a cytoplasmic membrane anchor for the Z ring. Also required for the recruitment to the septal ring of downstream cell division proteins.
Subcellular Location: Cell inner membrane
Sequence Length: 2... |
A0A359GUM5 | MAKIVVDGIEYEVNPDNNLLHECLSQGLDLPYFCWHPCMGSVGACRQCAVKQYRDADDEEGLLVMACMTPATDGTIISINNETAKSMRERVIESLMISHPHDCPVCEEGGECHLQDMTLMSGHNYRRYDKNKVTHRNQYLGPFINHEMNRCITCYRCVRFYDDYAGGSDLSAQASHHHTYFGRLVDGVLESEFSGNLVEVCPTGVFTDKPFSERYTRKWDLQTGPSVCTGCAVGCNTTPGERYGELRRIVNRYNSEVNGYFICDRGRFGFDYINSDSRFTVPIKHANGKSSSIDDLELQALLDEFKDGSYIGIGSPRASN... | Cofactor: Binds 1 [2Fe-2S] cluster per subunit.
Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic ... |
A0A368BXP4 | MSRLKFSHDSKVTLGKIVGHFGVRGWLKVFSYTKPREQITKYQEIKIDNDHLNSNFELEDWKIHGNQILLKIKKFDNRDDVEVFKNSLIIIDRKNLPDLTEGQYYWNDLEGMEVQGIDGKKIGKVSHMIETGSNDVMVMEDNKELIPFIFGQVVKRVDLEKNLIEVDWNWD | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but ... |
A0A368C0Y2 | MKETIKWINKSLNYKFNDEALLALALTHRSLSSKNNERLEFLGDAILSIIISDLIYREKSLLNEGDLTRLRAYLVKESTLCQIAKNINLSNHIHVGAGENKSGTRHRCSVLSDTLEALLGAIYLDSGFENTFSVIQELYKDVLSKLPSMDQLKDSKTRLQEIIQKESMNLPEYSIANITGQDHLQKFYVKCSVMDRNLITEGEGISIRKAEQHAAALMIEKYNDSELKK | Function: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the o... |
A0A8T6FL80 | MKVLVIGSGGREHALAWKVAESHAVEAVFVAPGNPGTAREEKVENLAIAEDDFEGLAGFVEREGVELTIVGPEAPLVAGIRDFFDARNLKCFGPSMAAARLEGSKAFTKAFMARHGIPTAAWAEFTDADEAERHIRAAAARQHNESTVPIVVKADGLAAGKGVVLAEDADTAVAAATDMLSGESFGDAGRRIVVEEFLRGEEASFICLCDGKTALPLASSQDHKARDDGDRGPNTGGMGAYSPAPVVTKAVHERIMAEVIRPTLAGMAAEGAPYQGFLYAGLMVLPDGGVRVVEFNCRMGDPEAEPLLMRLRSDLPQLCL... | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/2.
EC: 6.3.4.13
Catalytic Activity: 5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) + N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate
Sequence Len... |
A0A8T7J3L7 | MNDSAVLNQRLGVQFVQVEGDAAGQRIDNFLSSRLKGVPKSRIYKMIRSGEVRVNKGRVKPTDKLGFGDTVRIPPVILDNKPMTPPSWLLAQIEASILAETEHYYVINKPSGLAVHAGSGIEYGLIEGLCVLKDNPKLSLAHRIDRDTSGLVLVAKNRLSLNAAVEAFKRRQVTKRYQTLHSKALDRSHEVDLRLSRDHEEGGERLVKVDPEGQEALSIFTPLKTIDGFTRCAVDIHTGRTHQIRVHSLALSAPLVGDQKYGVKGVNADFKKRGFKHMFLHSSLLALNPEGFEPLNFKIDVPDNWGKYK | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 309
Sequence Mass (Da): 34416
|
A0A973DL41 | MAKGTKYTAKQADQTGFIHYSDEENKVWSELITRQMSWIDDTACVEFLDGLQRLNLPMDRVPQLEELNVVLRAATGWETAPVPALIGFEQFFNLLANKKFPVATFIRSREEIDYLQEPDIFHEIFGHCAMLTNPHFAAFTEHYGKLGLQATKQERVYLARLYWFTVEFGLVKSHDGLRIIGGGILSSPGETNYAYRKEAEITP | Pathway: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 1/6.
EC: 1.14.16.1
Catalytic Activity: (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + L-phenylalanine + O2 = (4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin + L-tyrosine
Sequence Length: 203
Sequen... |
A0A9D8J2W9 | MYPLLQFPDPLLNRPGKTVTVFDENLKEIVSNMFETHYAQENCAALAATQLGIEMKITVIDFSDMKNQPLCLINPEIIEKSGSHQEEEGCMSVSGVSAKITRASRIKIKYQDITGQEQQMSAEGFMAKCIQHEIDHLNGVLYLERLNHLKRKMLEMKILKLKIKKKS | Cofactor: Binds 1 Fe(2+) ion.
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 ... |
A0A937I661 | MKIYSVSEINTEARQVMLLAFEYPINVKGEISDYRQSRGHQYFKLRDVNGNYTVSCVMWKGSYGNINISQYLDMEVIVTAKVDFYAGFGQFQLNIIELSEFGDGFLKNEIEKIKKRLSDESVFSNKRNLPKFPKKIAVLTAKDSHALKDVCSKLNEKYCMAEILIYPSTVQGPQAPESLIKQLKKINQDSLADIILIVRGGGSLQDLMAFNNELLVREISQSIIPTITGIGHKPDITLADYASDSAQETPTAAAVHAVPDSQMLKQDIIHYENSITKLINNMILKTENKIKGNYLIIKMTNPFKTIESLSKDFIQRKKIF... | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.11.6
Subcellular... |
A0A1X6NSF9 | MAAAPAGSGLVRFLRSPTGPMTTHFWGPITNWGLSIAGFVDMYKPPDAVSERMTGALCVYSALFMRFAWRVQPRNLLLLSCHATNETVQLYQLQRCFGGVDFFYKPPPGRGGGDGTRVVRCTTADPLSIYPRCRRHSRTRARGARDCSSLIPLTSPPPRHDVGRRRTRPCVWGPLLLPPR | Function: Mediates the uptake of pyruvate into mitochondria.
Subcellular Location: Membrane
Sequence Length: 180
Sequence Mass (Da): 20025
Location Topology: Multi-pass membrane protein
|
A0A920J423 | MNHSVNKPDKIHFVGIGGSGMSGLAEVLINLGYSVSGSDLEESFITKRLASLGAKVYIGHKKSNVTDKDMVIISSAISKENEEILEANRNNLPILARAELLASLMNLKKGIAIAGTHGKTTTTSILASIMTDASLDPTFINGGIINSFATNAKLGSGDYLIAEADESDQSFLLLQPSLAVITNIEEDHLSNYENNFSLLKEVFVSFAKKIPFDGLIVACGDDLQVKELLPQFSRRVINYGFNEDNYYQIKNFSAKGLTSSFDLCEDGNKVLDVELNILGRHNALNAVAAIIVAIEEGVPLNTIQSSLKDFSGINRRMDIK... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Catalytic Activity: ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine
EC: 6.3.2.8
Subcellular Location: Cytoplasm
Sequence Length: 366
Sequence Mass (Da): 40015
|
A0A432ENX9 | MSHAKTDRRRLRGSRALKILDLYIAKSVLSYTVLVLAVLLGLLTFVAFIDEFDRIGSGSYNLWEASKYIFFTTPRRLYEIFPMTALIGTLLALSAMSADSELVVMRASGVSIAQIVLSVMKIGAVLAVFSFVIGEFVTPVSETKAQRDKALALQQNINQETTLGLWMRDKNIYVNVAEVLPDLTLLGIKIFEFDAGNRLKLNAIAHAQAGVYSPEEKKWELKNLRQTVFTDNSVKTDKAKDVYWKTVLSPEILNVFLIKPDQLSVWYLHRYIRHLRANSQNTNIYELAFWKKILGPFSTLVMVLLAVPFVFRQQLRAAGM... | 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: Membrane
Sequence Length: 375
Sequence Mass (Da): 42256
Location Topology: Multi-pass membrane protein
|
A0A9D0UNM3 | MKDWFLGLSPRERVMVAGGSALVLALMTYTLLWEPLVQDLARVEQALAEQRDLKVWMQGAAEEVRRLRGRGAGGQADTRSLLAVVDNTARQARLSGAVKRIQPDGQARVRVTLEQASFDDLIQWLGTLEARKGVHVAELTVDRREQAGQVNARVTLRRSGG | Function: Inner membrane component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm.
Subcellular Location: Cell inner membrane
Sequence Length: 161
Sequence Mass (Da): 17799
Location Topology: Single-pass membrane protei... |
A0A969EFV0 | MKFRMHENSLFAILLRSRWWISYAIAAAIFMVTSLFLDPGFAAFAGLPFLVIGSIALWRQLRVPGPARIERTLKAVREMTWSEFSGALEDAFRREGYVVSKFNGAAADLVMTRSGRTSLVACKRWKAARTGVEPLREPRSGRGVSATCTSASMSRRASSPMARALSLPNEDSRPARRGARANAAARRARIGAAEVAMDNVKMWTAGVPVEPDAYEQIANLASLPILGGHVAIMPDVHIGKGATVGSVIPTRGAIIPSAVGVDIGCGMMAVRTTLTASDLPDSLKAIRAQIERDVPVGFNAHDDPVSVGGQGLSGVAIQRR... | Cofactor: Binds 2 manganese ions per subunit.
EC: 6.5.1.8
Catalytic Activity: a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA + GTP + H2O = a ribonucleotidyl-ribonucleotide-RNA + diphosphate + GMP + H(+)
Sequence Length: 593
Sequence Mass (Da): 64599
|
A0A2E3DC17 | MESDLRHWLLIIGPLIVFGVILHGYFRMRSGNEKIKMDLDKSFLNKEKLSEGERFDTEFPNGGARVVENINLGFDEQESEVSEFENHLKKTSNEEVIRDHNTDLENIIALNIFSDDRELEGQQLLETVVDNGMVFGDMEIFHKFDSQDKIIYSLASAVEPGTFNISQISEFSTPGITMFMRIDGISDSEKNFEDMLDLAERISSEFDAQIYDETRSVLTRQTVEHIRQKIRNIKFKEIV | Function: Essential cell division protein that stabilizes the FtsZ protofilaments by cross-linking them and that serves as a cytoplasmic membrane anchor for the Z ring. Also required for the recruitment to the septal ring of downstream cell division proteins.
Subcellular Location: Cell inner membrane
Sequence Length: 2... |
A0A2E3QJI3 | MAEAELVTVARPYARAIFSSALSADGKLDHWSEILSSLVAVSNHKSGRELLNSPGYTNQQKTEFFESVMTDSLDVEAKNLISLLAENNRMGLLASIAEIYERMKAHHQKTLEVEITSAYELSSDESEALKNALSAKLGRDIELDISVDEKLIGGVIIKAEDNVIDDSVKGRLEKFANNLN | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
A0A952NYM5 | MKTLRLLLALQLLFVSTKSFALPSAGKNLLISGPHPEAVEAGLIIADQGGNAVDVAVAVALALTVTGPNYASLGGGGFAVVRMGKETQVIDFRETAPKATNPKTYTEPGKSSIDGGLAVATPGIPAGLVALHEKYGKLAWKDLFGPALRLSREGFRVTRKWVDVVGNEKSRFNPKAKAVFLNKGQDFAPTEIQKQPDLLKALLLYRSQKAKGFYTGDVAKDIVETVRKNGGVMTMQDMADYKVRWLKPIETEFRGYKLYLMPPPSSSGVVLKTALALTEKLKPFEKPALGIEESHLLSEILNRSFRYRSVLGDPDFHANP... | PTM: Cleaved by autocatalysis into a large and a small subunit.
Pathway: Sulfur metabolism; glutathione metabolism.
EC: 2.3.2.2
Catalytic Activity: an S-substituted glutathione + H2O = an S-substituted L-cysteinylglycine + L-glutamate
Sequence Length: 550
Sequence Mass (Da): 59567
|
A0A6L7XRN2 | MQYPLIDPVLVQLGPFALRWYGLMYVLAFGVMYLLGRRRAGAGTGWSVQDVSDLVFYGVAGIVLGGRLGFVLFYGLDQFLRDPLWLLRIWEGGMSFHGGLLGALAAMAVFARRRVAQEGDGSQGTQTLPQRRSFLEVTDFVAPLVPLGIGLGRVGNFINAELPGRVTESALGVHFPCASVQGLSIACYGEFETATRHVSSLYQAAGEGLLLFAVVWWFSARARSLAASGARSWWVTPGRVSGCFLVASGIIRFATEFFREPDAGIGFIVADWLTMGQLLSLPTAALGALLLLWTVPAKAGK | Pathway: Protein modification; lipoprotein biosynthesis (diacylglyceryl transfer).
Function: Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Catalytic Activity: 1,... |
A0A946YSF2 | MPAEYVSNCNLQRMHTLQLKSRARLFASLDNVEALPSLIEHADSKGLAVVPIGQGSNIVPAREVDALVVGLALQGQRVLDDSDDFIRLQVQAGENWHALVERCVAEHWYGLENLALIPGLVGAAPIQNIGAYGVEVASCVESVQIAPLDRRAIAGLASARGWQCNAQGIYSLTKQQCEFAYRDSLFKGALKGLCIVVSLVLRLSKRYQPELAYPALANHLGIAGRSNAALPCARQVFDAVVAIRREKLPDPARVPNAGSFFHNPVVSAALANELQQRHPALPMYAVPGATDKRKLAAAWLIEYCGFKGREGAAVGMYAKQ... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
EC: 1.3.1.98
Subcellular Location: Cytoplasm
Sequence Length: 365
Sequence Mass (Da): 39248
|
A0A0D8J3R6 | MLISVIIIIALTGLDQLTKHLATVYLAPVGSMPFIPGVMELRYVLNDGAAFSMLADAEWGRVFLIVVTGLALAALAVYFFWKKPSSWLERWVFILIFSGGLGNLIDRVLNGYVVDFFATTFMNFAVFNVADCFVCVGAALFVIAVLRQELNAKKEQKAGTDENA | 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-, ... |
A0A947FU60 | GYFGAGMSWVYISIYYFGDTGLILSTLFTIALVSLLAIFPALALSCLNRLFKNYSSTAYWLAAWPLAWLGFEWLRSWIFTGLPWLNLGHTQIDGPLSAFYPVLGANLVSLLICWLVGIAILLLRRTSGVIVASGLAAIILIGTVILTDKTWVTPRGESLSVISIQPKVAQDKKWDPAYRIESMWYLLDNTQGLKEDLVIWPEAAIPALPHQVLDFLETVDALAVSQNQTVLTGIPLYEDDKFYNGIILLGNDQGEYRKRHLVPFGEYVPYEEQLRGLIAFFDMPMSSFSKGQFKQPQLKIAGHTVAMAICYEIIFQDLVE... | Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipopr... |
A0A2D6JIM8 | MKFTVISPFQEMFEGPSKLGLVGSGIQKGLIDLEFINPRKFTSDIHQSIDDRPYGGGDGMLMSPGPLGSAIEEFKSKNPKAKLIYLSPQGKVFNQQMAKEFYKDGNVGLLCGRYAGVDERLISSEVDLEVSMGDFILSGAEIASMAIIDAVSRLVPGVLGNSESPVKESFEEGLLEWPQFTRPRDYKGMTVPEVLLSGDHKKIDKWRKLLSILRTLDRRPELLNDSGVDAAEIQEARDLFQKMSTHEKQICGLSEGLE | Function: Specifically methylates guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.228
Subcellular Location: Cytoplasm
Sequence Length: 258
Sequence Mass (Da): 28558
|
A0A352KQS6 | MSSYAIGDLQGCYQEFKLLLERIKFNPDCDQLWLTGDLVNRGPNSLDVLRAIYALRDNVFTVLGNHDLHLLAVALGGAELKPKDTLQNILKCKEADCLLSWLMNQPLMHYDKTLNVAMVHAGVSPRWDLPLSLSSAREAEQQIRGRNNSDFFSQMYGNHPLDWHPDLKGMERIRYIVNCLTRIRYCTKQGELELTEKGAPGSQKRDLLPWFDVPTRPQLKCRLLFGHWSTLGFFKKDELVCLDSGCLWGGFLTALELKPDPNAYFQPAA | Function: Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP.
EC: 3.6.1.41
Catalytic Activity: H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = 2 ADP + 2 H(+)
Sequence Length: 269
Sequence Mass (Da): 30626
|
A0A2E8K5F7 | MSMAQKALIVADGKCPVDSIVAGVSLLLLLSGLIMVASASTEVSAKLYGSPFHLVTRHAAYIFISTATGAFVLLVPMNYWQKLGIPLLALSFLLLIAVLVPGIGKEVNGAARWISLGSFTLQGSEFVKLFVVLYLAGYLVRQKEEVQSSFAALLKPLAIVTPLVLLLLGQPDFGATVVIMSAFMGVIFLAGIPMRYLLPVVSVSAVAISFIAILQPYRLARLTVFTDPWEHQFGGGYQLTQALIAFGRGEWFGLGLGNSIQKLFFLPEAHTDFLFSIIAEELGVVGAATIIVLFACLIIRALWIGYRAQIQGEDFHALTA... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Peptidoglycan polymerase that is essential for cell division.
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D... |
A0A2E3SHF8 | MSSNNNKKSLNFESTLSEIEKIIESLEEGNLSLEDSIKAYEKGISLTKACQKMLADAELKIKKLSSKEGEEVSFEDLSND | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.11.6
Subcellular... |
A0A9E2RVE8 | MRHHKLAAGLLLLSVFMFGFGFAMVPLYNALCRLTGLNGCGVESVAAAYAGEVDYTRTVPVQFAATTGSRRPFEFRPEVGSLRVYPGELYAANYNAADRSSTRIRAQAVVSYAPASAAHCVHKTECFCFMQENFAPGEVRHLPVKFYLDPSLPRDVQVVTVAYTYYKVSGNGIPAERSD | Function: Exerts its effect at some terminal stage of cytochrome c oxidase synthesis, probably by being involved in the insertion of the copper B into subunit I.
Subcellular Location: Cell inner membrane
Sequence Length: 179
Sequence Mass (Da): 19642
Location Topology: Single-pass type II membrane protein
|
A0A9E5M2F6 | MEARAALRSHAAVAGRETRCAARVATGRTRADAERTAECARPDHRARPGARAARTSARPAEVSTVALPLAFARRHGVLVRKVASGAAEGVMRADTTAEALAEARRHLRVPLRLATVSAEQFDELLRTAYEEGSDARLAADDIDSETDLAGLAQDLPEQADLLDSEDDAPIIRLINALLTQAIRNNASDIHVEPFENRLVVRFRIDGVMQEVLQTRRAIAASMVSRIKVMSKLDIAEKRLPQDGRISLKVAGRAVDVRVSTIPSGHGERVVLRLLDKQAGRLDLGQLGMDDTTTALVDALIHKPNGILLVTGPTGSGKTTT... | Function: ATPase component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm. Acts as a molecular motor to provide the energy that is required for assembly of the pseudopilus and the extrusion of substrates generated in t... |
A0A2E8I360 | MTETRLDSWPMDGWELLSPLLTNDRREKIFNTAQERTEHVRLIIQDVHDPHNISACLRSAEAFGVLNVDVIDQKAKYKPSKAAKGSFHWLEVHHWNSIEKCAQNLKDKGYQIAAGFPPPEGRSLYDTPTEKPIALLFGNEHEGVSSEWLPWIDHKFTIPMVGMVESLNISVSAAISMAHMTRSSKLSNPDNYKLNPLTQKYLLSKWGCRHFRNPHKQIEVLRQRSSSHP | Function: Catalyzes the 2'-O methylation of guanosine at position 18 in tRNA.
EC: 2.1.1.34
Catalytic Activity: guanosine(18) in tRNA + S-adenosyl-L-methionine = 2'-O-methylguanosine(18) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Length: 229
Sequence Mass (Da): 26232
|
A0A937I6G6 | MTLNFATLLTLLRITFIPIIVFTYIYNDGKYRDVSAYIFLVALITDYFDGVIARKFNQVTTFGIFLDPIADKLLVVVTVILLSSSNDSILFLMSALIIVSREFLVIAIRQRLAEIKRSMSIKVNLLAKVKTGFQMISLFLLLHTNIFFDVLNLHTLGLLLLFIAAVLTVISFIYYVRNSWSDIIR | Pathway: Phospholipid metabolism.
Subcellular Location: Membrane
Sequence Length: 185
Sequence Mass (Da): 21124
Location Topology: Multi-pass membrane protein
|
A0A2D8FBS8 | MLNGDKIYVEDLRVKATIGIFDWEKKIKQDVSISYEIPHDNVKAAKADAIEATTDYKSITKGIISFVENNKFELVETFAEKIAELVIKDFNIDEIRLRVSKPGALRFSKDVGVIIERDKSSYE | 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.
EC: 4.1.2.25
Catalytic Activity: 7,8-dihydr... |
A0A9E2RWA9 | MNARWIPNAISVTRMLLVLPAAWSIVRRQDEAALTLIIIAGVSDALDGFLAKRFDWVTRAGAILDPLADKLFVAGSFLAATWTGLVPAWITVIVIARDVVIVAGAAVYHWQVGDFRPQPSVLSKVNTLLQLLLVLAAVIQHYLHIVPRGVLPALVVAVALSTLTSGVDYFFRWGWRLARASHRKAA | Pathway: Phospholipid metabolism.
Subcellular Location: Membrane
Sequence Length: 186
Sequence Mass (Da): 20311
Location Topology: Multi-pass membrane protein
|
A0A975BE56 | MPDLNQDVEPDIKPDTENQEIFLKGIGAAPGICIGLAYLVDKEGVNVVKKYYIGAENIDNEKKRFKAAVKKAKDELHKIIQETPDDFRQHASILETHVVLLKDKMLYGKTIETINHEKINAEWALKKVVSELKKMFQSMSDPYFRDRADDIVHVSDRIMRSLVGGEQVNIRDINKRVILVASDLSPAETSQIQLVRIKGFVTERGGISSHTGIIARTLEIPAVLGLHNAGSLIKNDDLIIVDGTTGIVVIRPSEDTIVEYEERSIRYEAYKAEISRGSQLPAQTLDGFSIQIMGNIELPEEVVSVRDYGGNGIGLYRTEF... | Function: General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfer... |
A0A920HL90 | MKILNDRSTVFRYLEIPLSDKDNKKISKIVIDSRNVKEDCLFFGLEGKNTNGSLFAEEALQNGASLVVSSNKSFAMDSPNHIFHESPIDAMGKIASGIINDFTGNIIGVTGSSGKTTVKNLIKHTLDDCFGTIGNYNNEIGLPFSVMNLSQNHKTAVFELAAGKPKDIDFLAKIVRPHFGIITSIGHAHLKQMKSIDGVLKTKSEIIPNIREGGFLLIPHIEYVDYWKSIRNDISVFTFGDHPDSDYRISMIEPNEKLINFSVYVKEYGQTFDFVTNLLGMHNIQNITAAFICSQLIDDDYLAFQKRLEAFKNNENRLSV... | 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... |
Q60BP5 | MSIPISPSSEAFLKHMNFQEFFHMGGYAVYVWTSYGLCFAVLVFNLITPLRRKNEMLKSLRRQLKQESRP | Function: Required for the export of heme to the periplasm for the biogenesis of c-type cytochromes.
Subcellular Location: Cell inner membrane
Sequence Length: 70
Sequence Mass (Da): 8242
Location Topology: Single-pass membrane protein
|
A0A354W398 | MIRRVLGLTLLLLGVLSLPIAWRLLDRPIATIVVTGEVTEAERNQIRDALGQTSLQGILSTNLTQLHERLQSMGWPRNVDLRRRWPNKIVVSVTKVRPVARWGEGAYLAADGSELALPDDYPNLPHLNSGISSPQQTMEVFRLLQQLAERQDLRIVYLAESARGEWRLQFASGMRLQLGAERITERMHRFLRSHQQTLGHRVAAIDYVDARYTSGIAVRFFTDQETSEPLAAPLNRLELAARLNPEQPNEPEI | 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: 253
Se... |
A0A9K3CQ04 | MFRAKVTMVYFAICVVVTLLPQVTKSVQVYDYYLSWARIRNNKEYYRILTTFTYMGSVSAMPLSVVFGVINNISFMAKLENERYSGHTSRFLFAFAWGMIGMLLYTLFRPAEFLRSYLSDYFLYLWSKTSTTRIRVLGVLVIQPGWVPVFIAAVTWYKGGDCRLLMVSFLLAHTLFFMESVLPRAGWQPLGYVYDLMDVIARPFLLFVGVNMTERDAQRQRERDADLQRQRDREREVVAALTLQAKLEGDLCKDVQSLQERVEVLQRRVHTGMAEMPQRVPDGLQELQRGVPVEAPEWPADTVAEEEPIADAAPIEDTTP... | Function: May be involved in the degradation of misfolded endoplasmic reticulum (ER) luminal proteins.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 449
Sequence Mass (Da): 52204
Location Topology: Multi-pass membrane protein
|
A0A9D8P2D9 | MNRCIVIGLEVHVQLSCNTKIFSGSSTNFGAAPNSQACEIDLGLPGTLPNINVEAMNKAIMFGFATKSKINERNVFARKNYFYPDLPKGYQITQHHAPILVGGEIEIGEGENKQIIRIHHSHLEEDAGKSLHGADGAGIDLNRAGQPLLEIVSMPDMFSVEDAISYLKKLHHLVTYLGICDGNMQEGSFRCDANISLRDNASAPFGTRVEIKNLNSFKFIEKALKFEIKRQNALLDKNEEIIQETRLYHEETEQTRSMRKKEDSHDYRYFPEPDLPTIMVNQEHIDEIKKRMPMLPAERIMKYCQQWGLSDYDANVLVSV... | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an ... |
A0A923WZ02 | QIKVAPRIGHADDVWKNKFGHADHRGGGRSSGRETLCRVIAGSFAQMIFQSLNLKTEVHAFAEQIGPHKLTEATVLPENIKLFLSEAKIQGESHGGIVRCRIQKAPQNLGQPIFHKLKSDLASAMMGLGAVEGFEFGAGFTAVNMKGSDFHSKADSENYGGILGGISTGEEIIFRIAFKPTSSITDVAKKGRHDPCIVPRALPVVEAMAWCVLADHLLWIRTDQ | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.
EC: 4.2.3.5
Catalytic Activity: 5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate
Sequence Length: 224
Sequence Mass (Da): 24326
|
A0A8T7IX22 | MTDHTITCQLLNRMIEPNIATENWPIIRPLIDLLHSMSLEGHTSLPLSAARQLLSESLTSQWQRALDEEVINSRAISSGQNPHCPIVFDNGYLYWQRYHHLEVTIAESLLSRVNPLEFEKSTDPVIDRLFNPNNAHERQIDAARIATSQQLSIIVGGPGTGKTTTVAKILASLVELYDRTSLDILMLAPTGKAAARLAESMRHQIDQLDVSNDVKAQIPTEAKTIHRAIGLGRHKARFHANNPLLTDIVVVDEASMIDAGLMLKLLKALPAKTQLIFLGDANQLASVEAGSVLADLCLASQSPNSRLFGCLAELTHSYRF... | Function: A helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly rapid and processive ATP-dependent bidirectional helicase activity. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator) sequence from the 3' direction. Cuts ssDNA ... |
A0A965WJI7 | MSILIRNTLSGAKEVFVPHEDGKVKIYVCGVTVYDDIHMGHARSMIVFDTIVRYLRHCGYDVTHVTNFTDVDDKIIRKAAEEGVGALELSARYIGHYFEDAAKLGIRKADIYPKASEEMDSIIEMVGEIIEKGFGYATDDGSVYFSVDKVKDYGRLTNQKIEDMESSGRVALDEQKRNPMDFAVWKAAKPGEVSWDSPWGKGRPGWHIECSAMIRKYLGDEIDIHGGGNDLIFPHHENEILQTEAVTGRPLSKYWMHNGMLQVQGEKMSKSLGNFFRVRDVSQKFDRYAIRFYFLNTHYMSPLLYSEEMLAEARTSLERL... | Cofactor: Binds 1 zinc ion per subunit.
Catalytic Activity: ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys)
EC: 6.1.1.16
Subcellular Location: Cytoplasm
Sequence Length: 467
Sequence Mass (Da): 52759
|
A0A3M1RYZ0 | MPNGPVPPCGRDDISGLVLAGGLGTRMQGRDKGLIELGGGTMIERVVARLRPQVGPLLISANRNLSRYRQLELPVLQDPAAVRHCGPLAGLLAGLTAATTPWLAVVPCDAPRLPADLVARLASALERGDLLALASDGAREQPLFCLLSRSLEPDLAAWLAAGQRSVTGYFARPPLRRRLRLVDFSDSAENFLNINRPEDRAGFSRSAELAPGTGESR | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
EC: 2.7.7.77
Subcellular Location: Cytopl... |
A0A2D7U971 | MTRQKTSQQLRVPSIGSKRIAKKFFFLILFLGLIFVSFKLQFTLLQKIPVQDANQTFIVKKGDSLYGILLDLEKKYNLSSTWWIKFKYIFKEDPVIKAGRYNIFPNTSISELIERFEEGDVQLFKLAIIEGTVAKNNLINLENFIKDQKLNFDVSNNIKDMFSEEALLMPDTYFFSDQQDLIKVLSNSKLYLDEYLNNTWSEKSKDNPLQTPYEALILASIIEREAVLPSEQEKIASVFLARLEINMRLQADPTSSYGFYGDYGKKIGRAVLDDKNPYNTYQNKGLPPGPICYPSKGAIEAAIKSSPGEFFYFVAKGDGS... | Function: Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation.
EC: 4.2.2.-
Subcellular Location: Cell inner membrane
Sequence Length: 341
Sequence Mass (Da): 39199
Location Topology: Single-pass membrane protein
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.