ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A939V213 | MERYVALYTKYRPQVFDDIVGQEAPIAALRQSVKTGKIGHAYLFCGQRGTGKTTIARVFARAVNCMHPVNGNPCNECASCKAILDGTGMDVIEIDGASNNGVDNIRKICDEVSFAPATSRYKVYIIDEVHMISTAGFNALLKTLEEPPAHAIFIFATTELHQVPNTIVSRCLRFSFKRILPDLIASRLKIICKGEGIKADDTALLKLAMLADGALRDAITMLDQVAVINDGRNKQITVKDVEDVVGVVDTDFLFKMSCALLDGNMRELLDLCSELHHSGRDLVHFTTDLANYMRDLLVIRVLPDPTKHLAYSPDVMQQMY... | 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: 706
Seq... |
A0A925DN11 | MSFFNILFVFLGGGGGSVLRFLISWVVKTQTAVTLPVATFLANAIAVVVYALVFLSLQQKENDTLKYLILVGFCGGLSTFSTFSYETFELFKRGENVWAIANIVLNNVFCITLFYFLVKKVAV | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 123
Sequence Mass (Da): 13655
Location Topology: Multi-pass membrane protein
|
Q5CW23 | MNNCSIQEVMDFVEIIPVVKKYEWGRKEKLALTKVFYRNIKQIKELENHHHKINSSFNIENGDTSNSIELISEDKIKVENKESYLLDDHNKKRLIENEQNKEKEEEDYDEKDPYAELWYGSHISSPSQISFNGKIIDKFTLDDVISCNFEKQALITPNISLNNKNQNNKIPFLLKILSISKPLSLQVHPDKILAKELHSTFPCIYSDDNHKPEIAIALSEFETFCGFRNTIEILSIIENFPETFDIFGISLEFIKKTINEYNQQDNKLKSDVINVNNNIHDQSQEDPFFTIKKDLFINMLNSKTETINDSLNKLVNRLKK... | Pathway: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 1/2.
EC: 5.3.1.8
Catalytic Activity: D-mannose 6-phosphate = D-fructose 6-phosphate
Sequence Length: 576
Sequence Mass (Da): 66077
|
A0A1G4MCL7 | MNRDNIEKVRDGLYHAGNTLIFLPPDPWPEEIRKALIIITFSILGTYTRLGLTDLTNYAGSYVQGPNVLWPNFTACFCMGLVQGLNKYKVIPSSLFGGLTTGYAGTASSFSSLMMELFNHSTAQNSANISMDIKFPNQAYGILEFLSVLTVELGVSICGLVLGYHVARELGKYMEEEKGMPSELSINLSSFLDGVEAAAIALALPFVIVQVVLAAVYSNFSRSWTLSAVFGIFGTLARYYISRWYNIIYPHFPLGTFIVNVGASMLLAVFELLIRGKLADGTMIIKSVNTSRVVGALGTGLCGAMSTISTFVNEGYQLPL... | Function: Fluoride channel required for the rapid expulsion of cytoplasmic fluoride.
Subcellular Location: Membrane
Sequence Length: 356
Sequence Mass (Da): 38943
Location Topology: Multi-pass membrane protein
|
A0A095VNY1 | MPSRKKADTDASPATLEATIAEIEGILGRMEGEEQPLEQSLKDFEAGITLTRRAQALLQEAEQQVQKLTENADGEPAATALDDDADA | 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... |
A0A9E1ASE5 | MIKISPSVLAADFADLGNEALKMEQAGADMLHIDVMDGHFVPNISLGVPVLASLNKRTDLFMDVHLMISDPYTYAEPFVKAGADMLTFHLEAADSPETVIEKIRSLGVKVGIAIKPATPADALFPYLNGIDMALVMTVEPGFGGQSFMSDMLPKIAALRQEANRLDKELDIQVDGGITDVTAPLCLNAGANVLVAGSYLFGAQHVCAAVNRLRLV | Cofactor: Binds 1 divalent metal cation per subunit.
Pathway: Carbohydrate degradation.
Function: Catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate.
EC: 5.1.3.1
Catalytic Activity: D-ribulose 5-phosphate = D-xylulose 5-phosphate
Sequence Length: 215
Sequence Mass (Da): 22954
|
A0A942EP86 | MSNVSSSLLALIGDNLVSLRFTPIDIVDILIIAFLIYVGLRLVIETNSVSMIIGLFLLFVLYGLALLFNLVLSRVILQSIVSILVIVIAIVYQNELRRILNFFTILGFARHRQSWSEKVVFALSEAAFSLAASRQGALLVLPGREPVDPYITSGEKLDGFVSQPVLMSIFDASSPGHDGAVIIERDRITSFGVHLPLAENMTTLTQYGTRHRAALGLSEKTDALTVVVSEEKGVVNIARQGKLQSIQSKEELIVELQRFYLDRFPRERTKSFFANFAKNTFIVGLTLVLAVGLWIVNARSSPPVQRQFTVNLEFQNVAPG... | Function: Catalyzes the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP), a second messenger used to regulate differing processes in different bacteria.
EC: 2.7.7.85
Catalytic Activity: 2 ATP = 3',3'-c-di-AMP + 2 diphosphate
Sequence Length: 407
Sequence Mass (Da): 45285
|
A0A9E2G5B1 | MSMTTQESTLPSTFEEVMAELSTILEQLETGDLSLEKSIQLYERGAELSRHGQTMLTEAQLKIDKLTRLGISGVESKPYTEGQ | 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... |
A0A8T3U7E7 | MKITIYQGAIKGERFEYFLEKVTELGVDKICVTPFKRNVVKFKENEKNKKIERFKKILESSSKQSRRIDIPKIEILDNMIDTVSKLEKEDAVFILYEKVIEDTINIKDMLANIVKNNYTNIALVIGAEGGIDETEIEKFRKLRNIRIVTLGERILRAETTGPSVLSILNYELGR | 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... |
A0A927P2D9 | MGQGPMALAGSRGSAPDRDPGAAPLVRCGAKPHIRGLGGEAPKIPLDHPLRLKYNRISKKAHKEGLPMSITSRPYGVTKAGHQVTEYTLTNKQGASIKAITYGAILTSIIVPDNKGNMADVALGFETLDRYEGDHACMGDTVGRFGNRIALGKFTLEGKEYQLATNNGRNHLHGGIVGFSAKMWEATPVEGREQDSLKFHLVSPDGDENYPGTLDVTVTYTWDDLCNLSIRYEATTDKTTHCNLTNHTYFNLAGHDHGTVRDHVIYIDSDCLTAVDAELIPTGYFAPVAGTPFDLREGRVIGEGLDLIGTSLTMQDAGGY... | Pathway: Carbohydrate metabolism; hexose metabolism.
EC: 5.1.3.3
Catalytic Activity: alpha-D-glucose = beta-D-glucose
Sequence Length: 420
Sequence Mass (Da): 45632
|
A0A9E0AJC3 | MSAHHLFMQRALELAQNGHGQVAPNPMVGCVVVHNNEIIGEGWHKVYGGAHAEVNAITSVTDKSLLAQSVLYVTLEPCNHFGKTPPCTSLILDLGIKQVVVASSDPNPLVSGRGIARLQGAGVNVETGILKSAADELNKRFFTFHQQQRPFVLLKYAQTADSYLGLDVQNSTQEEFVAHKQISGNAAQRLTHRWRSEEQAVLVGANTVINDNPQLNVRHWQGKNPVRVLIDAKGRVPLTAKLFDGLTRTIVFTLNAPYFKSVSAEVVKLTTQEPVIKQVLYYLYAQHFLSVLVEGGAATLSAFIDAGMWDEARIFTSPKH... | 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... |
A0A6A6NQN5 | MDLRSLMNPSADSNGLSQQRHPHPQPQPHPYHPHSASPSAVASPGGPPPISTPTSATAVLQTPLGNQQQHFFPPPNPSHPQLLHSPLQTQHSPPIPQLRRQRTSVSLSSSPLASRGSPEAVVHQHPGIGSERTGGVPGSHRSSIHSLTINNKEAPPPPGPQQGTTPVTPAAAAGGSPVLAGYQAQYQMLLQQQQQQQPGQQAFGLQAQQFQQQQQTQAPQSQFSSPRSSSHNSLPPQTPQQPPPSHYQQSQPQPPTPTQHPNQQHSQYYQQQPPTPHPPPSRSHSIATPSPVTAPNMPAAAATTTVTATASVAPPRSRTT... | Function: First step of mRNA capping. Converts the 5'-triphosphate end of a nascent mRNA chain into a diphosphate end.
Catalytic Activity: a 5'-end triphospho-ribonucleoside in mRNA + H2O = a 5'-end diphospho-ribonucleoside in mRNA + H(+) + phosphate
EC: 3.6.1.74
Subcellular Location: Nucleus
Sequence Length: 524
Seque... |
A0A7C6IXX5 | HNPQLYWKAIKIIENDEIVTEELSDKVKQSIGEIIREAEKYADGDIEAKIADLRYKFISKIVKESVKKYPNDSHVETRSDKLDKILTNRFLAIPIFTLVMYLMFAATFSENFLFIEGLPSPGVWLAGAAETLWGYVASVVDTLVSGASPWVYSLVMDGIIEGIGAIIGFIPLVLVLYILISFLEDCGYMARIAFVMDRIFRKFGLSGRSFIPLLMGFGCSVPAVMATRTLNSEKDRRITTVLTGFMPCGAKLPIFAMFVSLFFDNHNKTLVTYSLYMLSIIVAIVVSLIINKVVFKSAASNFVMELPRYRIPTLKSIGIH... | Function: Probable transporter of a GTP-driven Fe(2+) uptake system.
Subcellular Location: Cell membrane
Sequence Length: 542
Sequence Mass (Da): 60360
Location Topology: Multi-pass membrane protein
|
A0A7C6UE04 | MTYHQTYKLTKEDEDLYVRELLVRRFQFSSRLLRKLKVEGGIFLNGRPVRFRHKGRAGDVLQVRFPEESSYFEPEDIPLAVVYEDEDLLVVDKQPGLVIHPTKNYQSGTLANALAHRMRLDGANYKIRFVNRLDRDTSGLVMIAKNAHCQKHISDQMERNEVKKYYTAIVHGQPERDSGTIDLPVAKDPEHAARRKVMPEGLPSLTHYRVLERFCVQDGVLPGYALLELQLVTGRTHQIRVHLTHIGLPIVGDELYGPLYGYEAGEDRMNRQALHAGGLVLAQPTSGQAIRLCTGLPDDMNACLEALRNDCSQRP | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 315
Sequence Mass (Da): 35793
|
A0A1H0QSH0 | MVPFDQRTGHIWLDGGFVDWAEAKIHVLTHGLHYASSIFEGVRVYGGKPFLLREHVERLRVSAHILDFDLPHTDDELCAATVEVVAKAGFADGYIRMNAWRGSEVIQTAAPKTSVHLSVAAWEIPSGYYAAADALEKGISLQTGQYRRPSADSAPVKSKAAGNYMIGTVSKNLALRAGFDDAMLLDTDGMIAESTGAHIFFTKDGTLHTPTTKCTIEGITRATVLDLAARQGIECVEAELAPEFVAEADGAFICGTACEILPVSRIDDHTYDLAGNKVIATLITEYASLTRSAN | Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4.
Function: Acts on leucine, isoleucine and valine.
EC: 2.6.1.42
Catalytic Activity: 2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate
Sequence Length: 294
Sequence Mass (Da): 31715
|
A0A4Z0BLC2 | MKHAHAMRFGASLRRQGGVEFRLWAPAARRAELAVYPTLFGLSAKPSPSPSPAAQRPEYMLHAATRNAEGWWEAHVPDAAAGTLYHWRIDEELMVPDPASRHNPHGVHEPSAVVDPLAFEWDEDWRGRPWHEVVLYEMHVGAFTPEGTFAAAAKRLPELAHLGITAIEVMPLADFPGRFGWGYDGVLPFAPHSAYGTPNELKALIQAAHRLGLMVFLDVVYNHFGPEGNYLHRYAPGFFSTTRSSPWGAAINFDGPHCRPVREFFVENAVYWTTEYRFDGLRLDAVHAISDDSSPHILEEISQRVREATAGRHVHLVLEN... | Pathway: Glycan biosynthesis; trehalose biosynthesis.
Catalytic Activity: hydrolysis of (1->4)-alpha-D-glucosidic linkage in 4-alpha-D-[(1->4)-alpha-D-glucanosyl]n trehalose to yield trehalose and (1->4)-alpha-D-glucan.
EC: 3.2.1.141
Subcellular Location: Cytoplasm
Sequence Length: 634
Sequence Mass (Da): 70855
|
A0A4Z0CAY7 | MSTHVVVMGVAGCGKSAVGARLAQALGLPLVEGDSFHPAANIEKMSRGLPLDDSDRAGWLDTLGRELASRPHGAVLTCSALKRAYRERLRAAAPGLRFVHLALTPQQALERVASRKDHFYPPSLVDSQFAALQDPAGEPGVVVVDASLPLDEVVAAALRDLAA | Pathway: Carbohydrate acid metabolism.
EC: 2.7.1.12
Catalytic Activity: ATP + D-gluconate = 6-phospho-D-gluconate + ADP + H(+)
Sequence Length: 163
Sequence Mass (Da): 17153
|
A0A2M7H8P8 | MRCRVSEGVDKAKQIDGLDFEQALAMLNELVGKLEAGELPLEESVAAFEAGVKLSRRCEALLDAAEQRLQVLNDDQDA | 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... |
A0A292YHT3 | MRNILNEWLAAIEFLTRIPVPKYLRRPFDERTVVRSVRWYPYVGLLLGAILAGLSLFFFRWFPAGAAAVLLVVSGIALTGGLHLDGLMDTADGLLSGRDRERKLAIMKDSRVGSMGVIVFVSLFALKGSLLAALGSSHESLHFPILLLMPAIGRIAVVWAIAKYPPARAEGMGAMFAGRVDASQLVTAGLVIIFPIFFWLVKGLVILVITCGFFLWYCRRVNQSLGGLTGDVYGAVCELTEVVFLLVCTVVLV | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.
Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-riba... |
A0A356AW21 | MRILITGGGTAGHINPAIAIANLFKLKDNRHEILFVGTQKGLEKDLVPRAGYDIKFIHAKGFMRKLSLKNLSAVTQFFKGYREASKIIKEFKPDIAIGTGGYVAGAVLYSAHRHRVPVVIHESNAFAGVTNRFISRFAKLAYVNFENTINTFDKAGKVIVSGNPLKEGLLNANRDEARKELNLKPQEIYIVAMGGSRGSETMNQCIVDMLNSNPVKGKFKMIFATGEADYPKRSSLVNSNPDLSGVVSTVPYIYNVETHYAAADLVICRAGAMTCSEMCAMGKASIMIPSPYVTENHQEHNARAIEEHEACFVITEKQLT... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Catalytic Activity: di-t... |
A0A970ZBW1 | MNLEQQAAPLQLEGVVNKIIYRNEESAYLVMAVETAEGEEVVVGYSAGIAVGESIQAQGSYTTHASYGRQFAAASITSIPPSGEAAVRAYLAGGAVKGIGQVLADRIVERFGGEALEILAQQPARLAEVRGITPAKAAQLGRRFEQVSGMRRVLAELDGLALPPYVAVKLFKRYGTQAAEAVAANPYLLCADEYEMHFELVDAAALERFHIDPQSPHRVMAGILYILHHNLGNGHTFLPLEALVERACDFLEVGDDLVLHSVDRLQEAGEVVEWPVANLDGLFLARFHGAEATIADRLLSMATQRRAAQNVPALVEKIEQ... | Function: DNA-dependent ATPase and ATP-dependent 5'-3' DNA helicase. Has no activity on blunt DNA or DNA with 3'-overhangs, requires at least 10 bases of 5'-ssDNA for helicase activity.
EC: 3.6.4.12
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 745
Sequence Mass (Da): 81242
|
A0A127QKL2 | MILLATQPTPARLWSGLTIGFCFGLGWFACGLWWLYPGLHDFGATEAYFAALLVAGVIGYMSLFPALASGLIAHSGLLLRDAKASFMWRAIRLCAVAGIWAISEWLRGHLFIGLPWLETGYAHTTAPLAGYAPLIGVIGVGFMNSLIAILLAYGVLNYINKEFSVSGALQAVAAIAIVLAGGQLLRSIDWTEDTGRNVSVRLIQGNIAQEDKFSAEGLRQAANVYVEYSQTSSANLTIWPETIFSLEWHSLPDGIKQGLQSIANARASTILFGSPVVSKDPALEKTVSTNSALAISPGDEAGKYSYRYDKIHLLPLAEYV... | 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... |
A0A1G1RPC4 | MSAYIHGNLAVERKEIQRAPAREKMRMVVHRSSLTVKEKLFYLFIIVMCVAVSGTIIWRYSQIYQMNTNIQHIKRQIQTLETDNIDLKLQVSQLKDPKRMLAEAEKYGLVTNEGSKSQAATSAAANNSIALNKK | Function: Essential cell division protein.
Subcellular Location: Cell membrane
Sequence Length: 134
Sequence Mass (Da): 15268
Location Topology: Single-pass type II membrane protein
|
A0A149VR73 | MANSRKSAVNLIDQVGQFLQKYITDHNSHITVAVSGGLDSVVLLYLCSQLTDQLQFRLSAVHINHQLQSINDEMQQHVIKLCEKLSIPLTVVAVNVELDSGLGLEKSARQARYNVYKTLDTDFLLLAHHANDQAETFLIQLFRGSGLPGLAAMPESRLLKPTTIQLLRPLIHVKRSVLYDYALTRQLTWVEDPTNQDSYYARNYIRQVLAPLIGNKFSHWVDTLNRTSLHLAKSQQLLDTLALIDLQQCTLDNRLDGRKVVALGEERAANLVRYWLVKTNLPVLQEAQWQSWWQQVKTRKQDTHPRLDFAGVSLVSDNNY... | 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)... |
A0A356M2X7 | MDKIILHADLNSFYASVEMLSQPELRQVPMAVAGDVEQRRGIILAKNELAKACGIVTAETVWQARKKCPHLRLVPPDHRRYQHYSELAFGIFCRLSDRVESFGLDEAWMDVTGSTGLYGDGPAMADWLRRQMKEELGLTCSVGVSFTKVFAKLGSDMRKPDATTVITRENFQSLVWPLPVRELLFVGDATARRLNQVGIKTIGDLARCDKSLLQQWLGKSGPGLWLDANGLGDDTVAASDARHEIKSISNSTTTAQDLTGNDQVKAVIYQLADQVAVRLRAHGLRARTVQISIRDSQFRTIDRQAPLPCLTDLAADIAPL... | Cofactor: Binds 2 magnesium ions per subunit.
Function: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5'... |
A0A352BG90 | ASLLTKSGKIFCGANIENASYPAGICAERTAMSKAISEGEKEFVAICITCNHNTYPYPCGVCRQFMSEFAPNLVVIVAKSKTDYKTTTLAQLLPSNFSEDDLK | Function: This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
EC: 3.5.4.5
Catalytic Activity: 2'-deoxycytidine + H(+) + H2O = 2'-deoxyuridine + NH4(+)
Sequence Length: 103
Sequence Mass (Da): 11178
|
A0A3D5ZNV8 | MEKKTGKKNVEKVAQKQENSLKEQTVTATKTEKILAVKPAARAEEAKKDEKTVKTAAKKTVKKTGTKAATKPGQEVKSEALPVKEASGKTTEKATKTKKTTVKTGTKKETPSKAETKTETKVENTEKPVEKITVTKKRSVVFIGSEAAPFIATGGLADVLGSLPEAISENGNYDVSVILPMYSAINYEWRKNFEYVTNFSVNLSWRTQYCGVFRYVYRGVTFYFLDNEYYFKRDGKIYGHYDDAERFAFFSKAALDTIARLDIYPDVVHCNDWQTAPAIIYLKGMYYPDERFRRIKTVFTIHNIEYQGKYGMELYGDLFG... | Pathway: Glycan biosynthesis; glycogen biosynthesis.
Function: Synthesizes alpha-1,4-glucan chains using ADP-glucose.
EC: 2.4.1.21
Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + ADP-alpha-D-glucose = [(1->4)-alpha-D-glucosyl](n+1) + ADP + H(+)
Sequence Length: 607
Sequence Mass (Da): 68827
|
A0A923ZY98 | MRTFTTIASLKKYIAEQKQNGASIGFVPTMGALHAGHISLIARALQECSVVICSVFVNPTQFNNAADLQKYPRTLETDTALLAQNGCTAVFAPSADEMYPNDNTTILAFDLGTLDTVMEGESRPGHFAGVTTVVDKLFNAVQPNIAYFGQKDFQQLAVINAMTKVLHPTIKIVGCAIVREVDGLAMSSRNTRLNEHWRRESVQIFKILTHAKQLATKGIEPSVIIKIAIENFSHTQLQLDYFEIVNANTLLPATNYTQPCVLCVAAYAGDVRLIDNMRVE | Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-... |
A0A149VRE8 | MQIHLGLSQPLTKSCALTIGNFDGVHLGHQMMIKQVVTQARARHLNSVVMTFEPHPKDFFAPQFSQPRLTSLREKIELIEAANVDHVVILRFNHDLAKTTAEEFVNRILKQQLHTRYLLVGDDFRFGAKRQGDFAYLLSRATEAGFTCESMDSHRVGQERVSSSAIRETLQQGQLDMARQLLGRPFYISGRVAFGKQLGRTIGYPTANIPLGRRIPPLQGIFAVTVEGLHNEPIKGVASLGTRPSVESNHEPWLEVHLFDFNDNIYGRRIHVNFYHKIRDEAEFTTLDELIKQIDLDALEAKAYLTSLSL | Pathway: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1.
Function: Catalyzes the phosphorylation of riboflavin to FMN followed by the adenylation of FMN to FAD.
Catalytic Activity: ATP + FMN + H(+) = diphosphate + FAD
Sequence Length: 310
Sequence Mass (Da): 35099
|
A0A7W4HFB4 | MKYFLIAGEPSGDMHAARLIRALKDADAGAEFRYYGGDAMRAEATGMVAHYRELAIMGFFEVLVHLRTIARRFKETMLAIEAFAPDVLILVDFGGFNLRVAKLAKERGVRVFYYIVPKVWAWHEGRVKKLKRYVDALFVIFPFEVPYFLRHGLRVYYEGNPSVDTVAECGGMRDRSLMETVLRDGRRPVVALLPGSRRMEIRYNLPPMLRVVERFPQYRFVLCAADSIDDSTLDRYIPKGTPLTVVRGATLAALRLAEGAVVTSGTATLEAALLRTPEVVVYRGPWSSMLLMKLVIRVKWISLVNLILGYGCVKELKQHE... | 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... |
A0A947YX95 | MNSLKPFRIDNDFKFFLLDQRLLPYKEVWVLIDNYQEMAAAIKDMIVRGAPAIGIAAAFGYAMGFRDSENSPDGNIYMKDVKKTLAATRPTAVNLFWALERMSTLYSTGTDFKTLWNEAFSIALEDEVACKTMGKFGADHITGTKLRVLTHCNAGALATGGWGTALGVIRELHAQGRLDVVYSDETRPRQQGSRLTAWELKRDGINVEMTTDTMAGHMMKSGLIDCAITGADRIASNGDTANKIGTYQVAVCAHYNKIPFYIAAPVSTIDFSIPDGSFIKIEERDESEVTHINGEIQTAEGVKARNFGFDVTENNLISAI... | 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... |
A0A947YYN6 | MIVNPVKVGSVNLNIPVLLAPMAAITTPAVRILAEECGAEMTFTEMISAAALFRGVRAARNLIRRSSPGKVFAVQLFGSDPHEMGYSAWYLKNQGAQYIDINMGCPMKDIVSNGSGAALMKTPELASDIVKVVIDSVKDEVPVTVKIRAGWDFDSLNAVPFAQLMEKSGARAITVHGRTRNQLYTGKSNPQVIRDVKNSVSIPVFANGDIKTAADAMELIRFTKADGVMVARGSFGNPWIFRDIRKSFETGHCVETPVTSEEKLQMILRHLEMIEISQDADSLAQSRKQIAWYSKNLHDSSSFREMVFSTSDIQSLKKLA... | Function: Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines.
EC: 1.3.1.-
Catalytic Activity: a 5,6-dihydrouridine in tRNA + NAD(+) = a uridine in tRNA + H(+) + NADH
Sequence Length: 329
Sequence Mass (Da): ... |
A0A354MWI9 | MKRTRQNKILELIEKYEIDTQTTLQERLKEAGFDVTQTTVSRDIKEMKLVKGLTERGTYKYVLPNLRQEAPSPVLNSTLAAAITRLEVSDNIIVLRTLPGMANALASCVDGLSLPEILGSVAGDDTILFVVRAGEAEHVREKLLTVFNKK | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis [regulation].
Function: Regulates arginine biosynthesis genes.
Subcellular Location: Cytoplasm
Sequence Length: 150
Sequence Mass (Da): 16683
|
Q6VEH1 | MFSIALIIPTIVMFLPFILAQSRTDTELYSAFECGFDNLNHREFHSHPSFFYYQVIFLIFDMELVILIPLIWGSNTMSIITFSSFLLVVLLGWLYEWREGSLAWNKTC | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity of complex I.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NA... |
A0A7C6WWC1 | MVHLFVDATGGDHAPAAQVAGSIAALRADPDLKLTLGGDIRVLEGLAADAGDVAARLQLRDTPEVITNHDAPAIAIRQKKRSAIVEGMLSVRSGETDGFVSAGSTGGVLLGGMLRLGR | Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]
EC: 2.3.1.274
Subcellular Location: Cytoplasm
Sequence Length: 118
Sequence Mass (Da): 12038
|
A0A349HQW9 | MGHWGRSSASRQSDKKDRPQCHKNQLRSLINYDKIAHTIIHLNRSILMNIKNLLKEMDYLSYIGEDDIEIRGITNDSRKVNRNDIFVAIKGFTNDGHKFIENALENGASAVLCENIPENVKGKSNFIIVKSARASMAKAANIIYGRPSEKMKIAGVTGTNGKTSTTYLLNGIYDYLGVKSGIIGTMGVLIDGKKIKVDNTTPEAFDIQHYLAMMLEKDITHCCMEVSSHALELNRIDEVKIDVGIFTNVTRDHLDFHKTMENYYQAKKKLFYLTKVNNIINVDDPYGLRLYNELIKEGIKAISVGIENDADIKASNLKTT... | 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... |
A0A8J6I8H8 | MEGGTAVANWALSPLDISFLTVESAAIPMTIGAVAVLAAEPEGATDRWPLIELLRTRATEIPRLRRKLRSELFPPVSASWAEDRAFRADAHVRLHHTVGGGGSEELNSWIARIMSQRLDRSRPLWELHVLDGLADGRAAMLLKVHHAFLDGLGVGALAYALADGGSPDKVPAPAGTNGTANGSAGGNGHHGLPRFDPGKLLGPLAGLADPPALARTAARALSTATGVITHMSTAGPGFPFDTVVSPARGFATSSVALEDLRGLRTLCGGSVNDIGIGVLSGALRSWLELHHYRPDDTRLRALVPVGRARSGNDGSGNHFS... | Pathway: Glycerolipid metabolism; triacylglycerol biosynthesis.
EC: 2.3.1.20
Catalytic Activity: a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA
Sequence Length: 477
Sequence Mass (Da): 49501
|
A0A2V2DRJ5 | MRQRKASIWKKLSFFIVDAIILAIVAYTAVGIITQRSSYMRFGIDIKGGVSATFQSADENVVPTDAQLESAKAIIELRLDSNNILDRTVTIDRENHSVLVEFPWQASEENYDPVAAIAELGETAQLTFAVVKSADSAGENTYALTDENGKTIGYYTIEEQFMDGSKVSKANAGYLEGNYVVNLEFDSEGTTIFSEKTSSHVGDLIGILMDDHLISVAQVETAITEGSCYISGSFTASESKDLAAKINSGALPFAMESSNYSSVSATMGTHALNVMILAGLIALCIIVLFMCIYYRLPGFVASITLLLQAAGQLLIFHLMG... | 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: 446
Sequence Mass (Da): 47946
Location... |
A0A2V2G1L9 | MRTKGRFSMSEYIALYRKWRPSVFADVIGQEHITKVLRSEVEGHSVSHAYLFCGSRGTGKTTCAKILAKAVNCENPQGGDPCGKCPACLAFDDSYDIIEMDAASNNRVEDIRDLCEKVSFAPIEMKKRVYIIDEVHMLSTGAFNALLKTLEEPPAHVMFILATTELNKIPATILSRCKRFDFHRISPETMLPRLRMISDSENIGITDGALRLIAFLATGAMRDALSMLELFVGKKDIDRDTAAAALGVVGNAPILNLLRAVAEKDTAKALELLDSIYNASKDMSVLCSELAEMFRNLLIVKFAGNSVSRLLDADPDVISV... | 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: 603
Seq... |
A0A940A2Z5 | MADKSRENHIHLVVVTPDRTFFEGDVYSASVPATDGSMGVMADHEPQVVSITPGIVTVRDDQGIRHFFVAEGYCEISQNLLLVICNSAEWPEDINVTRIFQSYKTACDTIEEQNKDRSHKYPNDAYYMKQRAIARMLLIEKYGSDAKKKRLSELRGN | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 157
Sequence Mass (Da): 17844
Location Topology: Peripheral membrane protein
|
A0A970XJW0 | MREFTGSLTSPAVLAGLFREFGVVPLKKLGQNYLVDANVLSRIASAADLGEESFCLEIGPGAGALTAQLALRAARVVAVEVDRGLIPLLQFTLQAFDNVRIVHGDILRQDLHALADEHFGGAPFAVAANLPYNITTPAIMLLLESGLPVTHMVLLVQREAGERLNAKPGTKEYGALSVVAQWAYTAQTLFAVSPNCFMPKPGVESVVVRLQARERPVADVDDRRAFFGMVRALFAMRRKTVLNNLLAYRRDMGREAALFALETAGIRPGARTETLPIAALAELYAVVHGK | Function: Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
Catalytic Activity: adenosine(1518)/adenosine(1519) in 16S rRNA + 4 S-adenosyl-L-methionine = 4 H(+) +... |
A0A968VN40 | MANTFAQKIVDPYAEALLSIGQDLDLIDTFATDVRLVLGSLQSTPELGDFLSSPVVKAEAKKALLETTFGEQIHPILLTTLRVLGDRRRMMYVQDVGLRFLELQRKLQRIALAEVTSAVELSDQQKQAIADRVKQLGQADHVEVEARLDPDLIGGVVIKVGSQVIDLSIRGQLRKLALQLA | 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... |
A0A942JWG0 | MQIRRGIALEARRPVALFGAVAAAVLAIDQLTKYVIRAILDPAQSIPLIEGVFHLTYIRNTGAAFGLMPGQRSLFITTTVLVLAAIGVYCWRARPSGLVLVSSLALVTGGAIGNLIDRVVAGRVTDFFDFRNFPVFNIADTALVTGAAGLFVWALLAPIDEREDHAEGDQPQGSPDHPGDGLVEETGTSGEPDR | 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-, ... |
A0A970IIG9 | YIAIEDNKPEAISAMEKAVSNESNIQVVTLKTKYPQGSEKQLIQAITGRQVPSGGLPADVGVEVNNVATAAKIYEALETGMPLIERVVTVSGQGIREPKNLKVRIGTLFSDLIEQCGGFSCEPSKVIAGGPMTGIAQHSLEVPVIKGIAGILALSPEETKDEEVWPCIRCGKCIEVCPINLMPLSISAYSLKGDFDTCREYNALDCIECGCCSYICPSKRPLVQSIVVAKNEIIAKEKSNISNKDR | Cofactor: Binds 2 [4Fe-4S] clusters per subunit.
Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
EC: 7.-.-.-
Subcellular Location: Cell membrane
Sequence Length: 246
Sequence Mass (Da): 26472
Location Topology: Peripheral membrane protein
|
A0A9E0YUV7 | MKQILIFAGTTEGRQLIERLCQYHIQIHACVATEYGKEVLPHSKQITIHAQRMDSAQMEDFLSAHAFDCVVDATHPYAVEVTQNIQSACTNKSVPYLRLLRENSEYENCVFVSNTQECISYLNQTSGAVLLTTGSKELVAYTNVEHFKERLYARVLPMTSVVEQCIALGFQGKHLICMQGPFTVELNQALLKQINAKYMVTKDSGSNGGLDEKLEAAKKANAIPIVIGRPTQETGYSLEQLIQTLVQDFTLQKKEKDVIPYFPFFCNIKNKQILVVGGGVIAQRRIQTLLRFGCQITMITPECTDILRQHAEQKRITACF... | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
EC: 1.3.1.76
Catalytic Activity: NAD(+) + precorrin-2 = 2 H(+) + NADH + sirohydrochlorin
Sequence Length: 417
Sequence Mass (Da): 46750
|
A0A8D8BZU1 | FPPLPLARWNHIEDLDSFFTRVYCYHQKHGFYVMMLQKVFELFQFVFVVVLITYMFNCVNYSVLFNDNNPNHEKVTLPMAMLSPSECVAELGGLDWLVLFLAGVFWVFRLMR | Function: Phospholipid scramblase involved in autophagy. Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome. Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by di... |
A0A7C6TQI5 | MKRIWVMSNPSRDTGLKHANTVLNTLGAFDCQIRFVQKPADFPSAGEPADLLIVIGGDGTVMRAARRAAPLGIPILGINCGHLGYLAELEPDEIPLISRFFEGDYRIENRMMIRVRTDSGKSFLALNDAVISHGVISRMAELELLCDGDYVSKYYADGLIVATPTGSTAYSLSAGGPVVDPRLDCLVVTPICPHSFVARPILFSADAELCVVNPSLKNHSSVPPETGVLYLTVDGIDSLPLERSDKVTLIKSDITTSFIRMNRHNFYQVLSRKML | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
EC: 2.7.1.23
Subcellular Loc... |
A0A9E0YV57 | MVSKKLVKALNEHINLEMYSGYLYLAMSIKTHEENYKGYSSWLFKQYQEEFEHSHDFIHFMQQRDMSVELKPVQVEPIKETDPLKIAKLVLEHERNVTKSIYKLHDLAKQENDYATEIFMHKYINEQIQEEDTAQDIIDKFTFAGESTSAKYSIDKELGGRIN | Function: Iron-storage protein.
Catalytic Activity: 4 Fe(2+) + 6 H2O + O2 = 12 H(+) + 4 iron(III) oxide-hydroxide
EC: 1.16.3.2
Subcellular Location: Cytoplasm
Sequence Length: 163
Sequence Mass (Da): 19286
|
A0A927SQ52 | MLCEEIHSCVSGRFVNRPYEARVFYFRKTLFKVGESMAKKFNFEVVTPDRLFFSEEVESISFSTPEGEMGVLVDHAPMLIAVIPCILKIHKDNSEQFAAIGEGFVEITKEKVVAIVDSAEWPEEIDVNRATLAKNRAEEQLKSQKLDYEMEQLLKMSIERANNRIKTAKGL | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 171
Sequence Mass (Da): 19537
Location Topology: Peripheral membrane protein
|
A0A3D1WGY0 | MTKEDLKTKKVSAISLGCDKNRVDLEKMLFLLSNYGMQVIENVEDADIVIVNTCAFILPAKKESIANIIEMENLKKSGRIEKLIVTGCLPARHMREIKQEFTTADAIVPLSENKNIINIIENLYGVKPSKPKSSFDRVLTTSNGYAYLKIADGCNNVCSFCTIPRIRGKYKSEKMEDLVSEAKLLAKRGVKELILVAQDTTRYGTDLYGKPMLTELCTRLAKIKEIEWIRIHYAYPEMVDKQLLDLIENEPKMCKYIDIPLQHIDNEILKSMRRKHDEGFTRNLIADIHTNYPDIKIRSTFIVGYPGETGRAFKKLVKFL... | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein uS12.
EC: 2.8.4.4
Catalytic Activity: [sulfur carrier]-SH + AH2 + L-aspartate(89)-[ribosomal protein uS1... |
A0A969YH89 | MAVPVIPAATAEPVAAQPPAAVTDVDALAALAKALAAEGRPLAFCLGQTAAGIGAEDGRCWFVPYAVDLTSPGLYEEQILDALAAVFQAVPLTLHGAKALFHRLAGRGLPPPTVAFDTMLAAYLLEPTRKGFDLRETLAAGRKAQSEAEETMAEEEHPKGRKYAPPMAPPEQAGEDAAAMIPLARAQRNELEAKGMLALLTEMEMPLTRVLFAMEREGFSVDKAALADLGALFSAEIERCRGEVIAQTGGQEFNVNSPKQLGEVLFDRLGLTSPTRKSKAGAWSTSAEVLEALDHPAIEPLLRYRKLTKLMGTYIEGLSR... | Function: In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity.
EC: 2.7.7.7
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Length: 601
Sequence Mass (Da): 65166
|
A0A3N0ZC09 | MANKNLLIVESPAKAKTINKYLGKDFIVEASVGHIKDLNKHTLSVDISNNFQPIYQILKDKKKVIEKLRQTAKNCNEVLIATDPDREGEAIAWHIAEEIQQANPKIKRVLFNEITPKGIKEGLANPRDLDENLYYSQQARRVLDRLIGYKISPFVSNALVTKSANALSAGRVQSVALRLICEREEDIEIFEPFVYWNIIGQFLAGKEVIEAKLVEFDGKQIKNPEGSKKPHRNETQDDYHKRIKKFFFIETEQQAKELVERIKKVQEFVVSKVTKKRIKKAPKPPFITSTLQQEAARKLGFSNKLTMQLAQRLYEGVPLG... | Function: Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is ... |
A0A0T6A3L2 | MGVGGQGRTFAIASEGWPFILPLLGGALVLWTLGLQGAGLFLVLLAGAVCFFFRDPERLPPGETGAILAPADGRVVRIGPPVDGRRGTEISIFLSLFDVHINRAPCAGRIAEVVASRGRFKVAWKAEASQVNARTLIHLRGDIGDIFVRQVAGILARQIVTWVRPGQEVRAGERIGMIRFGSRVDLLLPEGVRPRVRIGEHVRGGESIIGVVA | 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... |
A0A969HRX6 | MTTWLSAARLRTLPLALSSIGMGSFLAACYQRFSWEIFGLCALTTLLLQILSNLANDYGDSQHGADNQDREGPLRAVQSGKISARAM | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis.
Subcellular Location: Membrane
Sequence Length: 87
Sequence Mass (Da): 9463
Location Topology: Multi-pass membrane protein
|
A0A927SRX3 | MKRIIAMLLCTLLLAGCAASAERYTASFLDVFDTASQLVIYSDDPAEANRIAQLVYDELVYYHRLFDQYNAASGVNGVYELNHHASERPIQVDAPLFQLLSLGKSMYYKTGGKVNIAMGSVLGLWHEAREYGVSNPSAAYLPDMAALTEAAQHTDPQSIVLDAEKQTVFFTDPLLKLDLGAVAKGYAVEKVADLLEEQGISGVLLSIGGNVRSVGNRPDGTAFPVGVQNPDLTAAKQHIAVLGLDNASLVTSGSYQRYYTVDGKQYHHIIDPDTLMPAEHVWAVSVVTEDSGLADALSTALFNMPVEEGKKLLESYPGTE... | 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... |
A0A149VPN8 | MTVNIPKTNAVQFKAPFEEVSGVLLLNKPFGLTSNTALQRARHLLRAKKAGHTGTLDPHATGLLPLCFGEATKFSQWILDAPKGYIATLKLGYVSDTLDGEGVISKYSDVNIDLSQVEGVLNAMIGVQHQTPPMHAAIKVQGKPLYSYARSGQTIERQPRVIDILRCRLISLDTDLLTIECLVSKGTYIRVMASDIGEKLGCGAYLTALQRVSTGPYQLHDAVELSDLMAMSETKRRECLLPSDSLLSGVSSLHLDSVHAEDMKCGRIITLSEYKPLGLYKVYDPLNCFLGLCELFTENKLRPIRLMATHTQK | 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: 313
Sequence Mass (Da): 34446
|
A0A149VQJ9 | MIIAEALNKSAPLSLERRRLVEYLTQQNYAYLLAHANDSLSEAQTSLFHQLLQRLHLGEPLAYVIGEQEFYGLSFKVNPAVLIPRADTELLIDTAVPLLNSLSHPRCLDLGTGSGAIAITLCALCPHIEMTAVDVSIDALAVAQDNASRLLKERVTQLSWLHSDWYNNVSGHYDIIVSNPPYIAEGDTHLTEDGLPFEPQLALTSPWRGTQALQHIITEAPRFLTRPGYLLVEHGYDQENPVHALMKEAGFNHIKTYQDLNRLPRLTSGILR | 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... |
A0A2N2IBZ4 | MPRKIWARSSASRGARPGPCAPSWARLQPKSGNVQSWKFWSNVSEEKLDPVKLVELGRVQKPHGLRGELCIEPYADSPFIFEGLTRVYLRLPGKKPKPCILEGWRAHQGRALITVDRSQGRDQAEAWRGADVLARERDLPPLDDDEFRPEDLIGLPVMHVNGSRIGLLEDIRDVAGQELWFIHDEDGNEIMLPAVDEFIRGIDLDAGVILVDPPDGLLELYQQS | 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 ... |
A0A356M7A5 | MASSSGNQYHETINPEPEYAVYLLSLGCAKNLVDAECMSRIITDGGYHIVNSPEMADILVINTCGFIEDAKKEAIEAILRLAELKQPQGQAQFLVVTGCLSQRYAREIRTELPEVDVVLGTAEYSRIASVIKDLRHIRPKPENDAGMPPPGSLEHLNVDRQPSTTGRYAYVKIAEGCSNCCTYCAIPGIRGPYRSRPMEDIINEARRLSAAGWDEIILIAQDSTRYGIDLYQKPMLAQLLPAICSLDPVRMVRILYVYADMLDDSLIQIMAKEPKIAHYLDLPIQHADDGMLRRMNRRDSQADLRRKIVCLRRAMPDLIL... | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein uS12.
EC: 2.8.4.4
Catalytic Activity: [sulfur carrier]-SH + AH2 + L-aspartate(89)-[ribosomal protein uS1... |
A0A316QCT8 | MCGIIGYTGRKNAVPVLISGLHSLEYRGYDSAGVAVIEDGNVVCVKSQGRISDMEALLEARCGGLCSHTGIGHTRWATHGAPSDKNAHPHGTELVHAVHNGIIENYAELRERLAALGYRFHSDTDTEAAVYLIDYHYRKTGDPMAAISAAVRELRGSWAFGILFADKDGELYATRHESPLIVASDDTGSYMASDVTALMDYTNQYIRLDEEEIAVLRADGIRVFRMDGTAVEKEVQAVTWNRDAARRGGFAHFMLKEIHEEPEAVRKTVGSVVHDKIPAFHAGGADIESIGRASHIEIVACGTAMHAGLIGKRWIERFSG... | Function: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
Catalytic Activity: D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate
EC: 2.6.1.16
Subcellular Location: Cytoplasm
Sequence Length: 610
Sequence Mass... |
A0A7S2UXA9 | MAKIHCFVLSLTILSLAAWNVGAFQLNIGSKLKNGNAKTQKSNLTFQPNWRNKMHNRVTSLHMVASYEDSETLGGNQQTHTQSQPDLSALVVKPGPLRIMFKGKAITFTGLCYLFWAFLWCGLSYPFLVPFWVWCLAFDRNCRCLVDEVVSIWARLSMLSMFYKPKVEGLENLPPKDETVVFMANHQSFLDIFTLSGFLPRRFKYISKVEILRIPLIGWAMNFAGHIAIQRASVASQIQVFRDAIKSLKDGNSVCIFPEGSRTRDGRMLPLKKGPFTIAKRAGVRIVPVSLGELFRYNPPSAWLPLGIPKDAVLKIHPPI... | EC: 2.3.1.51
Catalytic Activity: a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA
Sequence Length: 355
Domain: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Sequence Mass (Da):... |
A0A3N0ZEA2 | MLLFQISYSAVDNVLIIGAGKSGIASALLAKRQGFDRIFVTEKGSEENYLEAKRIFEANSIEFEFGKHSFNLLSDFELVVVSPGVPPDAEIIVEAERLNKRIVSEVEFAYSFCKNSIIGITGTNGKTTTTALVEFILNTAGKKAIAVGNIGAPFSDYVDKVEPETIFVLELSSYQLDRIEKFKPDVAIILNITPDHLKYHKTFSNYRNAKFRIFANQKENDLLILNFDDKETLIAKSQAGGKVAYFGLKPVEFGAYLNGDEICLRFPENSNEEVVMKAGDIKIPGVHNLYNSLASIVAVRSFEVQNEQIRYALMNFQGVE... | 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-... |
A0A970F1B8 | MTKSAKGINSFIAKLGLTLFIITAITALMLGGVFELTKNEIAGQQMKALNKALNSLVPDGKLLEDRTYTSESFNAYTLERSDGKLAYCLEVAPDGYGGPIKMIVGVEVADENGKFVKRVLGVAITRHTETPGLGSKATNENFLSQFKEIYHLAINENGTVNTEPSQIKINGSGENTIDAITGATVTSRAVAKGVMTALDSIKVSATGEVSFE | Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
EC: 7.-.-.-
Subcellular Location: Cell membrane
Sequence Length: 212
Sequence Mass (Da): 22538
Location Topology: Single-pass membrane protein
|
A0A948E2Y4 | MKILLTNDDGITSTHLQILSDTLVDNGFELTVVAPDSEMSAVSHSISLRNPVRMRKIDDQKYAVSGTPADCTYMGMFHIMEKKPDLVISGINNGYNLGLDVYYSGTVAGAMEGVLRGIPGISASIDRKVSELWIRNFSQKISDFAKELLKSNRKPILYNLNCPPVDKINGFMFTGIGYRHYKDEVLVKHDPKGVEYYWLGGPVSKGYDNLEDGERRALEDGYVSVTPMDPLIFSSRKDYMYTPLIDTQTISEVLISI | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
EC: 3.1.3.5
Catalytic Activity: a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate
Subcellular Location: Cytoplasm
Sequence Length: 257
Sequence Mass (Da): 28719
|
A0A971NJS9 | PISSGMDALAAALGKSGSGDAAQAIMTTDTRKKEAAIEFSLGGKPARIGAIAKGSGMIHPNMATMLVFVTTDAAISPEMLQKALGCSAEDTFNMISVDRDTSTNDTMLVMANGLAGNEEITGEGHDYEAFRAALFELSAHLCRLIARDGEGATKLLECCVSGAKDKASARAISKSVICSPLLKCAMFGSDANWGRVLCAIGYAGVETDLDKIGVTFKSRSGSVTVCRNGRGVSFSEDIAKRVLGEDEIIIDVALGDGEAAASAFGCDLSYEYVKINGDYRS | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic): step 1/1.
Function: Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and ace... |
A0A970K5C6 | MISLKIGIFGGTFNPPHNGHVRAARSAAERLQLDRLLVIPSAIPPHKALPEGSPTSRERLELTYLAFQEVPCAEVCPIEVEEGGVSYTADTLRTLRERYPGAQFFLIMGSDMFRTLDSWYSAETVLRLATPAVLSRGTKDDKDIAECAAKYKERFGADAVVIGNAITEVSSTELRQQLRERRGVEMFSDAVYSAIIARRYYGAKPSFDWLREKSYAMVLEKRIPHIKGCEREAVALAERWGGDVEAARESAILHDMTKYMPLREQLRVLDEYGIMADEMERADVKLLHAKTAAAIARARFGVPDDVYNAIFWHTTGRPGM... | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
EC: 2.7.7.18
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide... |
A0A9E2G3R1 | MEKNPKRRMTLVLSRLEELYPEVESALVTGNPYQKLVATILSAQCTDARVNLVTPALFVRYPDARALARAEVAELEGLIHSTGFYHAKARHLLGASLQLVERHDGEVPADLDALLALPGVARKTANCVLNDCFGVASGIVVDTHVARLALRLGFTVADKGRAEIIERDLMALVPREHWIVVSHRLIAHGRAVCTARKPACDRCPLSELCPSDGRV | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the ph... |
A0A7C6S5M9 | MNLPNRLSILRICLVPLIITLFLLDSVIPYSRLYATLVFILAAITDFFDGYIARKYNLITNLGKFLDSIADKILVSSSLILILLAAPTDYGFNIILAVAIIIILVRDLIVNNIRMLAASKNYIMAADIFGKAKTALQTIAIPMFMCARDLGGLFDFNYIYLYIGGFALFLISLVLTIFSGIHYFVKGRAVIRD | Pathway: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
Function: This protein catalyzes the committed step to the synthesis of the acidic phospholipids.
Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + sn-glycerol 3-phosphate = 1,2-diacyl-sn-glycer... |
A0A9E0HTC6 | MTWGLTGGIGAGKSEVAKILRQLGVPVLDADQISRMQMQSGHAVYDSVVATFGRQILNDDKTINRATLASLVFNNPALRAKLNQLTHGAVINEINGRIALLKQAKHPLIIVEAALIFEIGLTTILHEALAGVLVVIAPKELRVQRVLARDQADPSGIKARMNAQISDEERLAKATIVIENAGTLEELRNTTVGLLTTQLAQSTNK | 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... |
A0A0S8JRL1 | MLSKFRSFIQSNSLCQPSDRILLAISGGIDSMVLLHLFFAAGYKPGIAHCNFHLRGSESDGDEKFVKSAAENMGADFYRQDFDTEQSARESGISIQMAARNLRYRWFEEIRSRHGYDYIATAHNQDDVIETFFINLSRGTGIRGLTGIPVKSERIIRPLLFASRKSIEEYAIGHDISFREDSSNASDKYLRNRVRHHLIPMLEEENPSFRMALMETMLKLSETEKLYEQELVLLKNRLMRKEGDRIKIRIRDLSAHGARKSILFEILSEYNFSAQAMEDIIHSLGGPSGKQFLSATHRIVKDREDLIITPVDNKEERKYY... | 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)... |
A0A3D4YGG7 | MKQRIGVLGGSFDPIHYGHLILAEQIKIEAQLDRILFVPACVSPFKIWNKPADRTHRLRMLELAIGDHKDFEISTIELDRDEPSYTYETLCALRAQYGSDAELYFIIGTDAFMHIEEWNCSRELLSEFSFLIGLRKGYDEQKLESILYDLSTRYPLKAQYIPIPELEISASDLRDRMAAGKSVKFLLPDPVIDYIDRTGLYQNTARLLQAFVRIKVDQERYQHTEGVVAKAMELAHRYGADPEKAEIAAWFHDAYRETGNLEHGPIAARELQQQFGIDDEDIINAIQYHTTGRPGMSLLEKVIYLADSIEDGRRYPGIDE... | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
EC: 2.7.7.18
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide... |
A0A352BGS5 | MLGFVSGKLEDIDGNLITINCGGVGFEIMVSQTTLSKLGDVGQNVKVFTFLNVKEDEMSLYGFSTKEEKQMFLNLTMVSGVGPKTAISILSEMSLYDLASAIAGSDATAIARVKGIGKKTAERIVLELKERVQNFASLDKLQNSGSVENQEFEYAINVLLTLGLNRYEATKKIRELATPTDKAEDIIQKVLRSLS | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
A0A352BFM9 | METIVLASNNKNKIKEFKKILTNYNIIPMEDIGFDQDIVEDGKTFLDNSLIKTNTIAKYCKEKGLNYMVMADDSGLCVDALNGEPGVYSARYAGNHDHQANRKKLLENLKNVEDPNRTASFVCSITLKKPDRTTLVAEGKVDGKILKQETGTMGFAYDCLFFCNELNKCFGECSEEEKNSVSHRGRAIQNLLKQL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as ... |
A0A356AQG9 | MKNLTSFNMSDIANFFYLKSNNPLDYIINIIDIAIVAFLVYKLLVIIQDTRAWQLIKGMLIVLALAALSKAIGLTTISYIFDNVITVAAISLVVLFQPEIRRALEQLGKKNVFNNMFVDENNKRIKTTAVIEEVLKAVNRLSKSYTGALIVFERGIAIDDIAKSGVILDSQVSSELIENIFSPNTPLHDGAIIIRGDKIRAAAAFLPLTDNPDLGRNLGTRHRAAIGISEACDSIVVVVSEESGGISFVKNGSLIPNFEVDTLRKTLSNNLLKNTKDEEDYKRAIEKIKNKKFGIFNKEHPNQARWDVKAIWVIISDFLK... | Function: Catalyzes the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP), a second messenger used to regulate differing processes in different bacteria.
EC: 2.7.7.85
Catalytic Activity: 2 ATP = 3',3'-c-di-AMP + 2 diphosphate
Sequence Length: 381
Sequence Mass (Da): 42558
|
A0A3A5IJI6 | MLISRVPGFFKLSVEERLSLITNKWNFNEEEKKLLLGLTPFPIKIADSMIENTVGLMPIPLGIATNFKINGEDRFIPMATEEPSVVAAASNAAKMAYEKGGFFTSLSGSIMRGQIQVLDIADPYSAMARIYEKKAEILKRCNAKDPTLVSLGGGAIDIEVNVIKTSNQSMLILHLLVDTRDAMGANAVNTMAEAVAPFIETITSGRVALRIISNLADRRIARARAVFSAKQLGGIEVVKNIVNAFEFAEFDPYRAVTHNKGIMNGISAVVLATGNDTRAVEAGAHAYASISGQYRSLTKWEINEDGDLAGSIEIPMAVGI... | Pathway: Metabolic intermediate metabolism; (R)-mevalonate degradation; (S)-3-hydroxy-3-methylglutaryl-CoA from (R)-mevalonate: step 1/1.
EC: 1.1.1.88
Catalytic Activity: (R)-mevalonate + CoA + 2 NAD(+) = (3S)-hydroxy-3-methylglutaryl-CoA + 2 H(+) + 2 NADH
Sequence Length: 426
Sequence Mass (Da): 45909
|
A0A352WVV5 | MFENMQDVRVERDVSMASLTTFRAGGHAAYAVYPSTPEAWGAIIAAAKKENIPFAVLGNGSNVLATDEDFAGILIITTDMRDVRVEETCVYAQAGASLSAVAVTAMKAGLAGLEFSYGIPGTVGGAIFMNAGAYDGEMQFAVKQSRYLDEDGQVRVLEKEEHAFGYRDSYYQHHFGMIIDCILQLKPGNPEEIKAKMDDFMCRRKSKQPLMHPSAGSTFRRPYKGYASQMVDECALKGFRVGGAAVSEMHAGFIINDREGSVADIVAVIQSVQKKVFAEKGVMLEREVRMLHEIILNGIFNKNIP | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
EC: 1.3.1.98
Subcellular Location: Cytoplasm
Sequence Length: 305
Sequence Mass (Da): 33413
|
A0A8B6E3T9 | MLLELFLLLCLIGIFKFVISWLVSPQVLKLDGKHVLITGGSSGIGKAMAKEAIRRGAVVSIMARNITKLEAAKVDLEKVAGNNFKPVCIVSVDVAGDYEEVQKAVQKTEDKQGPVNMLINCAGIGVAKTFEDLKIDEFKKLMNLNYFGSVQTTKAVISKMKEQGGGRIVFISSQAGQLGLFGYTGYAASKFALRGLAESLQMEVRPYNIYVTVAHPPDTETPGFEEEERNKPEETKLISGTSGLFKPEAVAKQILQDSVNGRFCSYIGLDGWMLANITCGMSPVHSMCDAIQQVLTVSVFRLISFFYLCHFTRIVRKCKA... | Pathway: Lipid metabolism; sphingolipid metabolism.
EC: 1.1.1.102
Catalytic Activity: NADP(+) + sphinganine = 3-oxosphinganine + H(+) + NADPH
Sequence Length: 331
Sequence Mass (Da): 36539
|
A0A1I3HW34 | MKKTPVLASCLIFSCLIATSCSQKMETTSFTAMNTYMTVRSYGRSAKAANLQVQKEVERLEGILSTTIEGSDVYRINTSKAETDGFSKIPVMPETTYLIQKSLRFYEMTEGSFNPALYPIIREWGFTTGDYKVPSEEKILSLLKYTDFSKIEISEKLQSATPLDSILQADHDKADQSTASILTCPAGMQLDFGAIGKGYAGDCAIRLLKENGVKSALLDFGGNIQVFGSKPDGSDWTVGIKNPWGGDPVAAVKLRDACMITSGGYERFFTGEDGKKYIHIFDGTTGRPVENELESVTIICRQGIYGDALSTSLFVMGLDK... | 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... |
A0A7C6BQE7 | MIAKRYYLFANPHKQETITGAKVLAEQLVNHQTHVYMEEWLHHLLGIGQALPPHQIDNRFSCMISLGGDGTLLRVSSLAASFNVPVLGIHFGRLGFLLETKLTDPESLTFKLINEDFFLEDRILFQATIDDGTSYLVTNEIALMRGDSPSSIKVVVSVDGAKLYSLRGDGVLISTPTGSTGYSLSAGGPVIHPQLECISIVPVCSHAVNHRPVLLPPDKKVEIFMPFENKHASRVYVDGQISLAVARPVRITVTKSDKRVQFIRFKQSNFIKRYREKQLEWYDDEGES | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
EC: 2.7.1.23
Subcellular Loc... |
I0BK64 | MRNAIRFPKQLSVKAKFVITFLSSLTASMGFMGFILYDQASQAAIDQGKILMMQDVQQMKDSLSQKVTMVQSLSELIASGPSIQNFLGSPLLSQPYQSQEYRDNIAPIIGSMFLQNKYLHSIRIYVKNQSLPELYDGFYHLSRIEAEPSYAPFIQDMHRITRWRGLHNEHVLLPSPGSIRHTQVFSYDHKIFSSRYTDMAGILEIEVDRDDFFASLKASKDHYRGNVFVVDASGRVVSGSSGLTDLTDYGLQGLLGDVKIDQVMDVKGVRSIVISAPLDWLDLRIVGIYPVSPFIDGMKHSWSRMFFVLLAVLLALCLIV... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 590
Sequence Mass (Da): 66933
Location Topology: Multi-pass membrane protein
|
A0A6A6NUF2 | MRKNQIFPNAFLHSSANRVYFVFHACPSPATPSPPQRYPHPPYNIPIAPSNPPGQSLRSNCSNYYSNHLEGTVLSAALTHVPALGFSDAALRAGARDAGYTDATASSMFLPGEGAWELVRWHLVSSREGLGAAWRESWEALEEKEDMAEEQRHKVLKARARQLVVERLRMNTRAGLVARMSEALAIMAQPSHVPAALRELAWLADEFCFLAGDTAVDGSWYAKRGALATVYAAAEMFQMQDGSVEQLDTERFVGDRLDEVETLRKRVDGVGEWLGYTGWSVVNGLRSKGVRI | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: Lipid-binding protein involved in the biosynthesis of coenzyme Q, also named ubiquinone, an essential lipid-soluble electron transporter for aerobic cellular respiration.
Subcellular Location: Mitochondrion
Sequence Length: 292
Sequence Mass (Da): 32288... |
A0A9E2BJT1 | MTLFDLPLPKTVTEVARMLQETLLEEPPLQDLWVEGQLADLRVALSGHRYFTLRDEGAQLKAVLFAGEARRLARLLGSFPSLEDGLQVVVHGRLGFYEKGGQVQLYADVILPRGAGLLHAELEARKKRLEAEGLFRPERKRPLPPFPRRIGLITSPRGAAVRDMVQIIQRRWPGMEILIFPVRVQGEGAAEEMVAALELANDPSFGLDVLILGRGGGSFEDLSPFQDEGLVRAVAASRLPVVSAVGHETDVTLVDFAADVRAPTPSAAAELVTPLKSQVEAHVEGLKGRLARGLLQRVAREKRHLRLLALALHPRKLRAL... | 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... |
I0BSB7 | MGRNSLRFKLIVVLLIATIAPIVTSMIVTNAYTKQSVKEKAIQENTNLLGQSRINIVNYMNQLIDLSFSVYKNPSFIRLMDLGFRGYQSEAEIKNLIRTIAVNREVFQVYMNILERNPGEDRSFLLTNNTVIRPSPEVTMPLNPLIKPGSYEAVVETTHTSHDYGLSLLAYFTPREVLTIHRAIYRVPSMEHIGSLSVDFPLDTLSGLLHQLLNDQEEAYLLDSEGRLIYSSVPGVKFGWKLQDPWVEQMLQASDTHGTMEDKSSIHLYEKIETPYMNWYLVKKVPYEQLYRGARELTQIQFLILGILLFVVAGLTLWIS... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 604
Sequence Mass (Da): 68709
Location Topology: Multi-pass membrane protein
|
A0A917CYP3 | MRPLSYGTVKSADICRQQTQLYNKQFQDIYHHRSAIEESHYVFHQGNQLQQQWQAQSDQAVFVIAETGFGSGLNFLTTRQLWQNCSRKPRQLHYISTEQWLLTPAQLNAFYKPWPDLHADLEILNEVFAHNRAGFHNHRIDHDITLTLLLGDATACLKQLTAQIDAWFLDGFTPAKNPDMWSEALFSQVGRLSKPGSTFATFTAASQVRRNLQSVGFEVSKSPGFKGKRERLTGQFKAPLKTDQPQQSWAPTPAATPSPKKITIIGSGIAGLCLAHSAKQNGLHVTLIDRSDKPLAGASGNPYALFMPYLTAKSSPEALF... | 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... |
A0A970PQY0 | MSEYKNTANFEDKLEALEALVAQMEEGKLSLDELLATYEKGVKLADSLKLDLERAQAKLSELKQGSVKPVDEA | 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... |
A0A5P8NP96 | MSNIYNLIDNLHLEDLQNETHPSIFDENEGYDMLIVRLPVIYKELQVISTGFIITNENSYLYDRDNRVFKTLESRFEAPYKILDKMVDELLESFENYRDLIADMEESLYLNKTTTSFMNNWLKLKRNIVRVERTLFHASFTMNKAIQHYEKSDDFPINHYIDLHEHMERTLRSATLQLSKLDYLYSFYSARTNEKMNSLVYNLTMISAIFLPLNLVVGFFGMNTSGLPFTDTTDGTTNVMILILFLLAITAGAISFLKKKV | Catalytic Activity: Mg(2+)(in) = Mg(2+)(out)
Subcellular Location: Cell inner membrane
Sequence Length: 261
Sequence Mass (Da): 30529
Location Topology: Multi-pass membrane protein
|
A0A7C6TQZ7 | MLNEIRYLAAAKINLYLRVLRRLPNGYHEIDTVMQAVSLFDEVTLSPRERGIKLTCTDISLAREPIKNLAFRAAALFYQRCPNIRTGVNITLKKNIPIAAGLAGGSADAAAVLVGMNLLFGAGLSEADLCNLGVRIGMDVPFCIMGGIRRGQGMGERLSECSPMPDCRILIAIGAERINTAEAYKRLSLTGLKDAENMMLPALESGSLDNICRNLYNSFETVTESGNQIKQIMLRNGAAGALMSGSGPAVFGLFRDAESLERARAALAEKKYTTFACRAIN | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6.
Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
EC: 2.7.1.148
Catalytic Activity: 4-CDP-2-C... |
F8AAA6 | MICVSLVEKTRGEALQALARAESLADLIEIRLDALESPEIDLFLERANKSLLFTYRAREEGGLKESSLEERLNYLNQAAQKKAFAVDLELASGEQAISELKRACQKTKLLLSFHNFQGTPAQEELKEIARQMKEAGADLGKIVTYAREPEEALIPLSLISWARKELSFPLIAFAMGEAGCFSRVVCLLLGSPWTYAALPLGEKAAPGQLRADTLRSIFEKLKTT | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
Function: Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DH... |
F8ABC6 | MLDLSVKVAGVTFKNPVLLASGTWGFGEKLKSYLDLSTLGGLVSKGISLKPREGNPPPRLAETPCGLINAIGLENPGVEVFKKHILPQLLAFKTHLLVNIFGETIDEFLGVAEALKDEPITGLELNISCPNVAKGGLAFGHDPATVKTLVEEIGKIYSGFLVVKLPPVGPVLDVARVALESGADALTVANTYPALAVDLASRRLALGRGTGGLSGPAIKPLTLKLVYDLYRELKAPIFGCGGITSGKDVLEYILCGAAAVQVGTATLLDPQNPAKILTEIEEELKKLGETNLGNLLAALKY | 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: 301
Sequence Mass (Da): 31612
|
A0A8J9WKR5 | MGNHDHKRKREVTRLEKAPTTQAAAALKGYALEEAPDKASQRPAGSSLRKIESQQRENIHKSAAVHQSGQDEPPPKAQQEERPLSHELDAPAIRTMLENGEPQHVESSEEEDVLEALAGFQKRDAGLRAAEPGSGAAGGSPDEESDEERGFVSFIDERKAMRYPTKRRVKEEQDTKKKKVKHKGTKSNMKTGELVHAESAVPASQKLEVFGPVDSSSFRGLGLAEALSDHLEEINFVTPTRIQQSAIPVLLRGRDALVNAPTGSGKTLAYLAPIINDLQAQEPRVSRAEGTHALIIVPTRELCLQIADVLTLILRRYIWL... | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 768
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence Mass (Da): 84190
|
A0A8B6E9F5 | MQRFVDLYHIIPIPTIFQEDYIEQAANECFNIIDNAASKCLIFRKTKLKGVRKHKNRKWFDIDLVQKRKSLISKDFMACSVLGQVQFSRKQSVVTRLLQWIAVLKSEWTSTTDKYLENSQTMYHQGYNPQFEDQNYMYYVQQQFPAYMQNYNMNMPMQQNFRPRPRFQGRPPFQGGRRPDQRHWQQQDNYSSVRDNIRQDIINQLNIEVGDDELHNNPNYTAFNANNSNKKRKSDDDDSPSKSKRSKQDYILRIPPTPKSSSNSQITQAMIEYFVENHQTEEMYMKKVKLRDALYSILNGVLPHCGLYIVGSSMSGCGTM... | Catalytic Activity: RNA(n) + UTP = diphosphate + RNA(n)-3'-uridine ribonucleotide
EC: 2.7.7.52
Subcellular Location: Cytoplasm
Sequence Length: 587
Sequence Mass (Da): 69249
|
A0A971V9K9 | MKVKRFIGQNTQEAMQKISDEMGKDAVILNTRKIRQKGITGFFKKPLVEVVAAVDEHVPQNNQMLNTQIGRLYSQKQTFSVNENTPAVLKRLENQIELINKLVNRLTHGVSVVENTSRLPVKPAFLSYYEQLVKNEVHEDIAKVIIEKAISFYEEERTEFESCLNKVLLEYLGPSQPLQLPDGQRKIVMFIGPTGVGKTTSLAKMAAIFSIQQQKKVGLITADTYRIAAVDQLKIYAEILEIPLSILYSPKEVVDALHQHRDKDVILIDTAGKSIRDKAQEKEIMELINLSNADEIYLVLSCNTSYAGCKNIIDSY | Function: Necessary for flagellar biosynthesis. May be involved in translocation of the flagellum.
Subcellular Location: Cell membrane
Sequence Length: 316
Sequence Mass (Da): 35696
Location Topology: Peripheral membrane protein
|
A0A969ZN03 | MRLLAVKALKGKNIYADFPVIRADICIDKTIGEFISDIEDFNKRYLKLWSRLKGYKFNDHIYQGFSKKIKMDRYIIPIIESTILEIQKILGDDLTFIKTKYLENKDVYSIIYEYKDEVLGLQSAELAVDIISSILEKKNLNIIQRLEKIKKLVSINELGTSTAAIVNEARKRQIPVTRIGNNSLIQLGYGKYSRRIQGTITDNTRCIAVDTVCDKGLTNSILRIHGLPVPQGETVSTYDEVMKAVKKLGFPVVIKPYNGNQGRGVSLNLQSFHEVRNAYNIARQYSDKILVEEYISGKNYRITVINQKVIAVAERIAAHV... | Function: Catalyzes the ATP-dependent polymerization of arginine and aspartate to multi-L-arginyl-poly-L-aspartic acid (cyanophycin; a water-insoluble reserve polymer).
EC: 6.3.2.29
Catalytic Activity: [L-4-(L-arginin-2-N-yl)aspartate](n) + ATP + L-aspartate = [L-4-(L-arginin-2-N-yl)aspartate](n)-L-aspartate + ADP + H(... |
A0A943IYW0 | MKERIITGAVLTILFLPLAFPVVSGSPFMCILFAVFAAIGTLEILRCLQLLRFYAISVPLIVLCGLTPLFAYCLPISLFLRGALAAVLILYFYVMTITIWSKGKLRPLTAVSAVTLTAYIACGFCSVILLRGEAHGAFLIYLVFLGAWITDIFAYFTGMLFGKHKLIVDVSPKKTVEGAIGGVLFTALSYLLFGVILSHFKEVDVSLFSFFLIGICAAVVAQIGDLMFSLFKREYGIKDYGKIFPGHGGVLDRFDSFLAVAPFVYLLCGLFA | Pathway: Lipid metabolism.
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: 272
Sequence Mass (Da): 29741
Location Topology: Multi-pass membrane protein
|
A0A351J277 | MSGTWIGMQNPSDLEVNPVGKNKNGILKPTLALLILCLAVALLLSSVNMLTKDKIEHNKTLKTNDAIASLFQGTFDSFEELTEGFTYVGSADALYKVYDAGHILQGFVCRATPTGFGGDIGLLVAMDKNATVIGVKVLYSTETAGVGSKVTEDRYLEQYANKSGKLVLNEDIDAITGATISSKNVLTGVNDSMTTCRSLLGLEVAQ | Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
EC: 7.-.-.-
Subcellular Location: Cell membrane
Sequence Length: 206
Sequence Mass (Da): 21930
Location Topology: Single-pass membrane protein
|
A0A970YN08 | MKKEERQKLLQEKLLKMKQYENALYEKGIQYIAGVDEVGRGPLAGPVVSVAVVLPRDFSILGVDDSKKLSPKKREELYEQIKEEAVAYGVGCVDNETIDRINILEATKLAMKDALRELEGKLRDHLGEDWKKLTGDEDRQKPCCIQHVLIDALTLKDVP | 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... |
A0A7C6TQT1 | MPTNDINKSEKKVRAASLSRKTKETQISMALELDRKKGGFCGSTGIGFFDHMLNSFAVHGGFVINLDMEGDLEVDGHHSVEDVGIVLGKLFAEILGDRAGIARFGLSYVPMDEALARAVIDISGRPYLVFDAKFKTERIGEFDTCLAVEFFRALAFNMGATLHMKLEYSENDHHAVEALFKSAARAISAAAKETGVDAPLSAKGTL | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
Catalytic Activity: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
EC: 4.2.1.19
Subcellular Location: Cytoplasm
Sequence Length: 206
Sequence Ma... |
A0A357CV05 | MKKNIPNILSVIRLLLVPVFIYLFFNDFKITAAFVFAIASATDILDGYLARKYNWITAAGKILDPLADKLMQGAVICSLAIDNINNNKSMFFIGIAVLFLLKESAMIIGACIVIRKKHTIVVSNWYGKAATVAFFCITTILIFYSENMTLNIILGILLVAVLISALLLYYFKVFRGVYGIKFPSKKKK | Pathway: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
Function: This protein catalyzes the committed step to the synthesis of the acidic phospholipids.
Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + sn-glycerol 3-phosphate = 1,2-diacyl-sn-glycer... |
A0A0J1KBQ3 | MFRKATIALLILGLAGCAKPTERGQQYLDGEFNQILNRVETVESDKSRDYSQFQAQAEKVIERSPRMASKYQSLYHQIQLWVAQGGDPKELANYGIQIAQMGGGDSQGNVMFTGYFSPVIELRHTPDETYRYPVYAMPECPSRCPSRSEIYAGALAGQELELGYSASMLDVFMMEVQGSGFVHYEDNDELQYFAYSGKNGHRYVSIGRILIERGEVPKEKMSLKAIADWVSRQDEETARELLEQNPSYVFFKPKDNLDVIGSAGIPLLAHASVAADRDYLPMGSVLLAEVPQLDEEGNWNGKHVLKLLLALDTGGAVKKN... | Function: Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division.
EC: 4.2.2.n1
Catalytic Activity: Exolytic cleavage of the (1->4)-beta-glycosidic linkage between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) residues in peptidoglycan, from eit... |
I4YG31 | MAIKKKKTPITKSKKTASKSISSKKTKEIINNFHQLLKRRKTTTNEVEIKDIDRAIDELGGMEAYQHASTIGQSTPRGGDSSHYFVKWLAELGVKKSYVADKEKMSLLEIGALLPDNYHSERSWIETELIDLKSNHPSIKEQDFLQRPLPSKPDDEKDAISSSLVLNFVPTPQERGQFLYRLNSVLKMNGWLFMVLPAPCVVNSRYLTRNHFISILETLGFKLVKEKIGDLQKGSRIAYWLLQKTSKPNKPPIELTKKTVLVDGPKLNNFCILI | Function: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(1) position of an adenine present in helix 65 in 25S rRNA.
EC: 2.1.1.-
Subcellular Location: Nucleus
Sequence Length: 274
Sequence Mass (Da): 31179
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.