ID   PURE_ALIF1              Reviewed;         161 AA.
AC   Q5E1R4;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=VF_2537;
OS   Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=312309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700601 / ES114;
RX   PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA   Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA   Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA   Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT   "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT   pathogenic congeners.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
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; CP000020; AAW87032.1; -; Genomic_DNA.
DR   RefSeq; WP_005421516.1; NC_006840.2.
DR   RefSeq; YP_205920.1; NC_006840.2.
DR   AlphaFoldDB; Q5E1R4; -.
DR   SMR; Q5E1R4; -.
DR   STRING; 312309.VF_2537; -.
DR   EnsemblBacteria; AAW87032; AAW87032; VF_2537.
DR   GeneID; 51060711; -.
DR   GeneID; 64241553; -.
DR   KEGG; vfi:VF_2537; -.
DR   PATRIC; fig|312309.11.peg.2563; -.
DR   eggNOG; COG0041; Bacteria.
DR   HOGENOM; CLU_094982_2_2_6; -.
DR   OMA; SNSIDGW; -.
DR   OrthoDB; 1701464at2; -.
DR   UniPathway; UPA00074; UER00943.
DR   Proteomes; UP000000537; Chromosome I.
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_0000074982"
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;  16773 MW;  8E4E4D33F56002CE CRC64;
     MKVGIIMGSK SDWPTMKLAA EMLDRFNVPY ETKVVSAHRT PQLLADYATQ AKDRGIKVII
     AGAGGAAHLP GMAAAFTSVP VLGVPVQSRA LKGMDSLLSI VQMPKGIAVG TLAIGEAGAA
     NAGILAAQII GTSNEEVMAA VEAFRKEQTE MVLENPDPSE D