PURE_AQUAE
ID PURE_AQUAE Reviewed; 167 AA.
AC O67239;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 122.
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=aq_1178;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
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; AE000657; AAC07201.1; -; Genomic_DNA.
DR PIR; D70401; D70401.
DR RefSeq; NP_213803.1; NC_000918.1.
DR RefSeq; WP_010880741.1; NC_000918.1.
DR AlphaFoldDB; O67239; -.
DR SMR; O67239; -.
DR STRING; 224324.aq_1178; -.
DR EnsemblBacteria; AAC07201; AAC07201; aq_1178.
DR KEGG; aae:aq_1178; -.
DR PATRIC; fig|224324.8.peg.916; -.
DR eggNOG; COG0041; Bacteria.
DR HOGENOM; CLU_094982_2_0_0; -.
DR InParanoid; O67239; -.
DR OMA; SNSIDGW; -.
DR OrthoDB; 1701464at2; -.
DR UniPathway; UPA00074; UER00943.
DR Proteomes; UP000000798; Chromosome.
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..167
FT /note="N5-carboxyaminoimidazole ribonucleotide mutase"
FT /id="PRO_0000074968"
FT BINDING 11
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01929"
FT BINDING 14
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01929"
FT BINDING 41
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01929"
SQ SEQUENCE 167 AA; 18037 MW; 99A62BE6000F50F4 CRC64;
MKPLVGVIMG SISDWEYMKK AVEVLKEFGV PHEVKVVSAH RTPELMYEYA KTARERGIEV
IIAGAGGSAH LPGMTASMTT LPVIGVPIPT KNLGGVDSLY SIVQMPAGIP VATVAIGNAT
NAGLLAVRIL SIKYPEYAKK LDEYTEKLKE KVAKMNEELQ KEVENGI
