ID G0LGX8_HALWC Unreviewed; 218 AA.
AC G0LGX8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=N5-carboxyaminoimidazole ribonucleotide mutase {ECO:0000256|HAMAP-Rule:MF_01929};
DE Short=N5-CAIR mutase {ECO:0000256|HAMAP-Rule:MF_01929};
DE EC=5.4.99.18 {ECO:0000256|HAMAP-Rule:MF_01929};
DE AltName: Full=5-(carboxyamino)imidazole ribonucleotide mutase {ECO:0000256|HAMAP-Rule:MF_01929};
GN Name=purE1 {ECO:0000313|EMBL:CCC39680.1};
GN Synonyms=purE {ECO:0000256|HAMAP-Rule:MF_01929};
GN OrderedLocusNames=Hqrw_1750 {ECO:0000313|EMBL:CCC39680.1};
OS Haloquadratum walsbyi (strain DSM 16854 / JCM 12705 / C23).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloquadratum.
OX NCBI_TaxID=768065 {ECO:0000313|EMBL:CCC39680.1, ECO:0000313|Proteomes:UP000007954};
RN [1] {ECO:0000313|EMBL:CCC39680.1, ECO:0000313|Proteomes:UP000007954}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16854 / JCM 12705 / C23
RC {ECO:0000313|Proteomes:UP000007954};
RX PubMed=21701686; DOI=10.1371/journal.pone.0020968;
RA Dyall-Smith M., Pfeiffer F., Klee K., Palm P., Gross K., Schuster S.C.,
RA Rampp M., Oesterhelt D.;
RT "Haloquadratum walsbyi: limited diversity in a global pond.";
RL PLoS ONE 6:E20968-E20968(2011).
CC -!- FUNCTION: Catalyzes the conversion of N5-carboxyaminoimidazole
CC ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide
CC (CAIR). {ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01929}.
CC -!- SIMILARITY: Belongs to the AIR carboxylase family. Class I subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01929}.
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DR EMBL; FR746099; CCC39680.1; -; Genomic_DNA.
DR RefSeq; WP_014555489.1; NC_017459.1.
DR AlphaFoldDB; G0LGX8; -.
DR GeneID; 12446441; -.
DR KEGG; hwc:Hqrw_1750; -.
DR HOGENOM; CLU_094982_1_1_2; -.
DR OrthoDB; 9473at2157; -.
DR UniPathway; UPA00074; UER00943.
DR Proteomes; UP000007954; 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 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 SMART; SM01001; AIRC; 1.
DR SUPFAM; SSF52255; N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase, PurE); 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01929};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW Rule:MF_01929}.
FT DOMAIN 32..191
FT /note="PurE"
FT /evidence="ECO:0000259|SMART:SM01001"
FT BINDING 40
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01929"
FT BINDING 43
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01929"
FT BINDING 84
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01929"
SQ SEQUENCE 218 AA; 23084 MW; D54D1FB1C3A56D39 CRC64;
MPAHTPNEPT IQALLDRLHT QADTDLTTAE TPDVGIIMGS DSDLDTMVGA HEALDKLGFD
EQTEFMTSPD ARFTYETYVV SAHRTPQVLY AYGETAADRG IDVIIAGAGG KSADLPNMTA
SIAYPIPVIG VPVQEKSVDS VIGMPTGAPI VAVDAGKSHN AALSAAQILS REHDVLKTRL
EEYHTALITD VAADSFRMHD AGVNTFRASD GESGTSND
//
