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Database: UniProt
Entry: Q9KVT8
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ID   PURK_VIBCH              Reviewed;         377 AA.
AC   Q9KVT8;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   13-FEB-2019, entry version 94.
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=VC_0051;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A.,
RA   Gill S.R., Nelson K.E., Read T.D., Tettelin H., Richardson D.L.,
RA   Ermolaeva M.D., Vamathevan J.J., Bass S., Qin H., Dragoi I.,
RA   Sellers P., McDonald L.A., Utterback T.R., Fleischmann R.D.,
RA   Nierman W.C., White O., Salzberg S.L., Smith H.O., Colwell R.R.,
RA   Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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; AE003852; AAF93229.1; -; Genomic_DNA.
DR   PIR; B82370; B82370.
DR   RefSeq; NP_229710.1; NC_002505.1.
DR   RefSeq; WP_001265400.1; NC_002505.1.
DR   ProteinModelPortal; Q9KVT8; -.
DR   SMR; Q9KVT8; -.
DR   STRING; 243277.VC0051; -.
DR   DNASU; 2614419; -.
DR   EnsemblBacteria; AAF93229; AAF93229; VC_0051.
DR   GeneID; 2614419; -.
DR   KEGG; vch:VC0051; -.
DR   PATRIC; fig|243277.26.peg.50; -.
DR   eggNOG; ENOG4105CY8; Bacteria.
DR   eggNOG; COG0026; LUCA.
DR   KO; K01589; -.
DR   OMA; APRTHNS; -.
DR   BioCyc; VCHO:VC0051-MONOMER; -.
DR   UniPathway; UPA00074; UER00942.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0004638; F:phosphoribosylaminoimidazole carboxylase activity; ISS:TIGR.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009152; P:purine ribonucleotide biosynthetic process; ISS:TIGR.
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; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR005875; PurK.
DR   InterPro; IPR040686; PurK_C.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
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    377       N5-carboxyaminoimidazole ribonucleotide
FT                                synthase.
FT                                /FTId=PRO_0000075015.
FT   DOMAIN       97    287       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_01928}.
FT   NP_BIND     138    144       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT   NP_BIND     175    178       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT   NP_BIND     257    258       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT   BINDING      93     93       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT   BINDING     133    133       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT   BINDING     183    183       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
FT   BINDING     206    206       ATP. {ECO:0000255|HAMAP-Rule:MF_01928}.
SQ   SEQUENCE   377 AA;  41014 MW;  D5C1787315454BD3 CRC64;
     MRVLVLGAGQ LARMMSLAGA PLNIETIAFD VGSENIVHPL TQTVLGHGLE QAIEQVDVIT
     AEFEHIPHPI LDLCARSGKL YPSAEAIKAG GDRRLEKALL DRAQVANARY TMIRSRDDLT
     SAIAEIGLPM VLKSALGGYD GKGQWRLKEP TQIESVWQEL AQYLAANPEQ AIVAEEFVAF
     DREVSLVGAR NLVGDVVVYP LAENVHTQGV LSLSTAIDAP ALQTQAKAMF KAVAEQLNYV
     GVLALEFFEV QGQLLVNEIA PRVHNSGHWT QQGAETCQFE NHLRAVCGLP LGSTKLVRET
     AMINILGEDQ LPAEVLALEG CHVHWYGKAK RSGRKMGHIN VTADYSGELQ RKLCQLATVL
     DEKAFPAVHA VAKEIQP
//
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