ID   PURE_METSM              Reviewed;         339 AA.
AC   P22348;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Probable N5-carboxyaminoimidazole ribonucleotide mutase {ECO:0000305};
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};
OS   Methanobrevibacter smithii.
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX   NCBI_TaxID=2173;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2993814; DOI=10.1007/bf00383311;
RA   Hamilton P.T., Reeve J.N.;
RT   "Structure of genes and an insertion element in the methane producing
RT   archaebacterium Methanobrevibacter smithii.";
RL   Mol. Gen. Genet. 200:47-59(1985).
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; X02586; CAA26422.1; -; Genomic_DNA.
DR   PIR; S28656; S28656.
DR   AlphaFoldDB; P22348; -.
DR   SMR; P22348; -.
DR   UniPathway; UPA00074; UER00943.
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   Pfam; PF00731; AIRC; 2.
DR   SMART; SM01001; AIRC; 2.
DR   TIGRFAMs; TIGR01162; purE; 1.
PE   3: Inferred from homology;
KW   Isomerase; Purine biosynthesis.
FT   CHAIN           1..339
FT                   /note="Probable N5-carboxyaminoimidazole ribonucleotide
FT                   mutase"
FT                   /id="PRO_0000074991"
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   339 AA;  36694 MW;  EB94F7CF79EC9FD2 CRC64;
     MTPKVMIILG SGSDIAIAEK SMKILEKLEI PYSLKIASAH RTPDLVRELV VQGTNAGIKV
     FIGIAGLAAH LPGAIAAYTH KPVIGVPVDV KVSGLDALYS SVQMPYPSPV ATVGIDRGDN
     GAILAARILG LYDEEIRKKV LESKEGYRQK VIKNNEEIVQ KIDNPHITND FLRIKNLELN
     ETTEEFNGSY INKNAEVVII VGRHTDLITG KKVSVTLDRL KIPHDMQVIC PIRSGKKFRA
     YVNTMKNAKI FIGINSNSSQ VSGGLVGLTE KPVIGVPCEN ELGNNYLLST VNMPPGVPVA
     TVGVNNGRNA AVLSGEILSI NNPVLLELLE KLKNKKINI