ID   PURE_VIBCH              Reviewed;         161 AA.
AC   Q9KVT7; Q7B8Z7;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=N5-carboxyaminoimidazole ribonucleotide mutase {ECO:0000255|HAMAP-Rule:MF_01929};
DE            Short=N5-CAIR mutase {ECO:0000255|HAMAP-Rule:MF_01929};
DE            EC=5.4.99.18 {ECO:0000255|HAMAP-Rule:MF_01929};
DE   AltName: Full=5-(carboxyamino)imidazole ribonucleotide mutase {ECO:0000255|HAMAP-Rule:MF_01929};
GN   Name=purE {ECO:0000255|HAMAP-Rule:MF_01929}; OrderedLocusNames=VC_0052;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=El Tor C3294;
RA   Soares C.A.G., DiRita V.J., Santos E.O., Coelho A.;
RT   "Identification of two Vibrio cholerae El Tor genes induced in the
RT   estuarine environment.";
RL   Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., 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 conversion of N5-carboxyaminoimidazole
CC       ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide
CC       (CAIR). {ECO:0000255|HAMAP-Rule:MF_01929}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole + H(+) = 5-
CC         amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate;
CC         Xref=Rhea:RHEA:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:58730,
CC         ChEBI:CHEBI:77657; EC=5.4.99.18; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01929};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC       amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-
CC       phospho-D-ribosyl)imidazole (N5-CAIR route): step 2/2.
CC       {ECO:0000255|HAMAP-Rule:MF_01929}.
CC   -!- SIMILARITY: Belongs to the AIR carboxylase family. Class I subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01929}.
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DR   EMBL; AF459402; AAL66729.1; -; Genomic_DNA.
DR   EMBL; AE003852; AAF93230.1; -; Genomic_DNA.
DR   PIR; C82370; C82370.
DR   RefSeq; NP_229711.1; NC_002505.1.
DR   RefSeq; WP_000215768.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9KVT7; -.
DR   SMR; Q9KVT7; -.
DR   STRING; 243277.VC_0052; -.
DR   DNASU; 2614427; -.
DR   EnsemblBacteria; AAF93230; AAF93230; VC_0052.
DR   GeneID; 57991242; -.
DR   KEGG; vch:VC_0052; -.
DR   PATRIC; fig|243277.26.peg.51; -.
DR   eggNOG; COG0041; Bacteria.
DR   HOGENOM; CLU_094982_2_2_6; -.
DR   OMA; SNSIDGW; -.
DR   BioCyc; VCHO:VC0052-MON; -.
DR   UniPathway; UPA00074; UER00943.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0034023; F:5-(carboxyamino)imidazole ribonucleotide mutase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01929; PurE_classI; 1.
DR   InterPro; IPR033747; PurE_ClassI.
DR   InterPro; IPR000031; PurE_dom.
DR   InterPro; IPR024694; PurE_prokaryotes.
DR   Pfam; PF00731; AIRC; 1.
DR   PIRSF; PIRSF001338; AIR_carboxylase; 1.
DR   SMART; SM01001; AIRC; 1.
DR   TIGRFAMs; TIGR01162; purE; 1.
PE   3: Inferred from homology;
KW   Isomerase; Purine biosynthesis; Reference proteome.
FT   CHAIN           1..161
FT                   /note="N5-carboxyaminoimidazole ribonucleotide mutase"
FT                   /id="PRO_0000074981"
FT   BINDING         9
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01929"
FT   BINDING         12
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01929"
FT   BINDING         39
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01929"
SQ   SEQUENCE   161 AA;  16645 MW;  5E843DF107809FCB CRC64;
     MTVGIIMGSK SDWPTMKHAA EMLDQFGVAY ETKVVSAHRT PHLLADYASS AKERGLQVII
     AGAGGAAHLP GMTAAFTSLP VLGVPVQSRA LSGLDSLYSI VQMPKGIAVG TLAIGEAGAA
     NAGLLAAQII GIHNPEVMSK VEAFRAKQTQ SVLDNPNPAE E