ID   PURE_VIBVU              Reviewed;         161 AA.
AC   Q8DDD7;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 110.
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=VV1_1054;
OS   Vibrio vulnificus (strain CMCP6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=216895;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CMCP6;
RA   Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT   "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL   Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE016795; AAO09541.1; -; Genomic_DNA.
DR   RefSeq; WP_011079087.1; NC_004459.3.
DR   AlphaFoldDB; Q8DDD7; -.
DR   SMR; Q8DDD7; -.
DR   EnsemblBacteria; AAO09541; AAO09541; VV1_1054.
DR   KEGG; vvu:VV1_1054; -.
DR   HOGENOM; CLU_094982_2_2_6; -.
DR   OMA; SNSIDGW; -.
DR   UniPathway; UPA00074; UER00943.
DR   Proteomes; UP000002275; 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.
FT   CHAIN           1..161
FT                   /note="N5-carboxyaminoimidazole ribonucleotide mutase"
FT                   /id="PRO_0000074984"
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;  16696 MW;  17C09D4D44350A01 CRC64;
     MKVGIIMGSK SDWPTMKLAA EMLDRFGVEY ETKVVSAHRT PHLLAEYAST AKERGLKVII
     AGAGGAAHLP GMAAAFTSLP VLGVPVQSRA LSGLDSLYSI VQMPKGIAVG TLAIGEAGAA
     NAGLLAAQIL GTHDENIMAK VEAFRSEQTE SVLANPNPAE D