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Database: UniProt
Entry: Q5HQA5
LinkDB: Q5HQA5
Original site: Q5HQA5 
ID   PURK_STAEQ              Reviewed;         375 AA.
AC   Q5HQA5;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   13-FEB-2019, entry version 97.
DE   RecName: Full=N5-carboxyaminoimidazole ribonucleotide synthase {ECO:0000255|HAMAP-Rule:MF_01928};
DE            Short=N5-CAIR synthase {ECO:0000255|HAMAP-Rule:MF_01928};
DE            EC=6.3.4.18 {ECO:0000255|HAMAP-Rule:MF_01928};
DE   AltName: Full=5-(carboxyamino)imidazole ribonucleotide synthetase {ECO:0000255|HAMAP-Rule:MF_01928};
GN   Name=purK {ECO:0000255|HAMAP-Rule:MF_01928};
GN   OrderedLocusNames=SERP0650;
OS   Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35984 / RP62A;
RX   PubMed=15774886; DOI=10.1128/JB.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T.,
RA   Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J.,
RA   Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S.,
RA   Haft D.H., Vamathevan J.J., Khouri H., Utterback T.R., Lee C.,
RA   Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H.,
RA   Hance I.R., Nelson K.E., Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete
RT   genome analysis of an early methicillin-resistant Staphylococcus
RT   aureus strain and a biofilm-producing methicillin-resistant
RT   Staphylococcus epidermidis strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
CC   -!- FUNCTION: Catalyzes the ATP-dependent conversion of 5-
CC       aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5-
CC       carboxyaminoimidazole ribonucleotide (N5-CAIR).
CC       {ECO:0000255|HAMAP-Rule:MF_01928}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ATP +
CC         hydrogencarbonate = 5-carboxyamino-1-(5-phospho-D-
CC         ribosyl)imidazole + ADP + 2 H(+) + phosphate;
CC         Xref=Rhea:RHEA:19317, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58730,
CC         ChEBI:CHEBI:137981, ChEBI:CHEBI:456216; EC=6.3.4.18;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01928};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC       5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-
CC       amino-1-(5-phospho-D-ribosyl)imidazole (N5-CAIR route): step 1/2.
CC       {ECO:0000255|HAMAP-Rule:MF_01928}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01928}.
CC   -!- SIMILARITY: Belongs to the PurK/PurT family. {ECO:0000255|HAMAP-
CC       Rule:MF_01928}.
DR   EMBL; CP000029; AAW53996.1; -; Genomic_DNA.
DR   RefSeq; WP_002486052.1; NC_002976.3.
DR   ProteinModelPortal; Q5HQA5; -.
DR   SMR; Q5HQA5; -.
DR   STRING; 176279.SERP0650; -.
DR   EnsemblBacteria; AAW53996; AAW53996; SERP0650.
DR   KEGG; ser:SERP0650; -.
DR   eggNOG; ENOG4105CY8; Bacteria.
DR   eggNOG; COG0026; LUCA.
DR   HOGENOM; HOG000034029; -.
DR   KO; K01589; -.
DR   OMA; APRTHNS; -.
DR   OrthoDB; 1165275at2; -.
DR   BioCyc; SEPI176279:G1G46-675-MONOMER; -.
DR   UniPathway; UPA00074; UER00942.
DR   Proteomes; UP000000531; Chromosome.
DR   GO; GO:0034028; F:5-(carboxyamino)imidazole ribonucleotide synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0004638; F:phosphoribosylaminoimidazole carboxylase activity; IEA:InterPro.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:InterPro.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   HAMAP; MF_01928; PurK; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR003135; ATP-grasp_carboxylate-amine.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR005875; PurK.
DR   InterPro; IPR040686; PurK_C.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   Pfam; PF02222; ATP-grasp; 1.
DR   Pfam; PF17769; PurK_C; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   TIGRFAMs; TIGR01161; purK; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Ligase; Nucleotide-binding;
KW   Purine biosynthesis; Reference proteome.
FT   CHAIN         1    375       N5-carboxyaminoimidazole ribonucleotide
FT                                synthase.
FT                                /FTId=PRO_0000075009.
FT   DOMAIN      112    296       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_01928}.
FT   NP_BIND     153    159       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT   NP_BIND     183    186       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT   NP_BIND     266    267       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT   BINDING     108    108       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT   BINDING     148    148       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT   BINDING     191    191       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT   BINDING     214    214       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
SQ   SEQUENCE   375 AA;  43226 MW;  F17CF729A50414C4 CRC64;
     MNFSKLKFGA TIGIIGGGQL GKMMAQSAQK MGYKVIVLDP NEDCPCRYVA HQFIHANYDD
     EQALNQLGEN SDVVTYEFEN ISSEQLKKLT KLYHIPQGYQ AIELLQDRLT EKQTLLEANT
     QIVPFVQIQT NQDLLKAIEK LGFPFIVKTR FGGYDGKGQI LVRNDSELDE AYQLVEKQEC
     VAEQYLDIQK EVSLTVTIGN EQQTTYFPLQ ENEHQNQILF KTVVPARSDK ENEARKEVEK
     ITRAIHFVGT FTVEFFIDKE NNLYVNEIAP RPHNSGHYSI EACDYSQFDT HILAITGQKL
     PQAIELLKPT VMMNLLGRDL DLLENEFSRH PDWHIHIYGK KERKPDRKMG HMTLLTDDVN
     QTEQYMLMKF EGRDK
//
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