ID PURE_VIBPA Reviewed; 161 AA.
AC Q87KE1;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, 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=VP3036;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
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; BA000031; BAC61299.1; -; Genomic_DNA.
DR RefSeq; NP_799415.1; NC_004603.1.
DR RefSeq; WP_005394016.1; NC_004603.1.
DR AlphaFoldDB; Q87KE1; -.
DR SMR; Q87KE1; -.
DR GeneID; 70913849; -.
DR KEGG; vpa:VP3036; -.
DR PATRIC; fig|223926.6.peg.2920; -.
DR eggNOG; COG0041; Bacteria.
DR HOGENOM; CLU_094982_2_2_6; -.
DR UniPathway; UPA00074; UER00943.
DR Proteomes; UP000002493; 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 Gene3D; 3.40.50.1970; -; 1.
DR HAMAP; MF_01929; PurE_classI; 1.
DR InterPro; IPR033747; PurE_ClassI.
DR InterPro; IPR000031; PurE_dom.
DR InterPro; IPR024694; PurE_prokaryotes.
DR NCBIfam; TIGR01162; purE; 1.
DR PANTHER; PTHR23046:SF2; PHOSPHORIBOSYLAMINOIMIDAZOLE CARBOXYLASE; 1.
DR PANTHER; PTHR23046; PHOSPHORIBOSYLAMINOIMIDAZOLE CARBOXYLASE CATALYTIC SUBUNIT; 1.
DR Pfam; PF00731; AIRC; 1.
DR PIRSF; PIRSF001338; AIR_carboxylase; 1.
DR SMART; SM01001; AIRC; 1.
DR SUPFAM; SSF52255; N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase, 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_0000074983"
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; 16598 MW; 82A4BFA92B3450F2 CRC64;
MKVGIIMGSK SDWPTMKLAA DMLDQFGVSY ETKVVSAHRT PQLLADYASS AKERGIKVII
AGAGGAAHLP GMAAAFTSLP VLGVPVQSRA LKGMDSLLSI VQMPKGIAVG TLAIGEAGAA
NAGILAAQIL GTHDESIMAK VEAFRNEQTE TVLANPNPAE D
//
