ID M0M2A3_9EURY Unreviewed; 212 AA.
AC M0M2A3;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
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=purE {ECO:0000256|HAMAP-Rule:MF_01929};
GN ORFNames=C446_07964 {ECO:0000313|EMBL:EMA39841.1};
OS Halobiforma nitratireducens JCM 10879.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Halobiforma.
OX NCBI_TaxID=1227454 {ECO:0000313|EMBL:EMA39841.1, ECO:0000313|Proteomes:UP000011607};
RN [1] {ECO:0000313|EMBL:EMA39841.1, ECO:0000313|Proteomes:UP000011607}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10879 {ECO:0000313|EMBL:EMA39841.1,
RC ECO:0000313|Proteomes:UP000011607};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EMA39841.1}.
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DR EMBL; AOMA01000078; EMA39841.1; -; Genomic_DNA.
DR RefSeq; WP_006672528.1; NZ_AOMA01000078.1.
DR AlphaFoldDB; M0M2A3; -.
DR STRING; 1227454.C446_07964; -.
DR PATRIC; fig|1227454.3.peg.1604; -.
DR eggNOG; arCOG02464; Archaea.
DR OrthoDB; 9473at2157; -.
DR UniPathway; UPA00074; UER00943.
DR Proteomes; UP000011607; Unassembled WGS sequence.
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 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}; Reference proteome {ECO:0000313|Proteomes:UP000011607}.
FT DOMAIN 26..192
FT /note="PurE"
FT /evidence="ECO:0000259|SMART:SM01001"
FT BINDING 34
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01929"
FT BINDING 37
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01929"
FT BINDING 85
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01929"
SQ SEQUENCE 212 AA; 22827 MW; 7CAAF3FD78038848 CRC64;
MTDSVTDLID RFQKQADQDR SAAATPDVGI VMGSDSDLET MMTGGRRRGA YDAFVDELGF
AEQTNYESPP DERFTFETYV TSAHRTPDLM MAYAETAEDR GLEVIIAGAG GKSADLPNMT
ASIAYPLPVI GVPVQEKSVD SVIGMPTGAP LVAVDAGKSF NAALSAAQIL AREHEELRER
LVAYHEDLRE GVGTVSRALH DDGTPAFRGR ED
//
