ID A0A162FI80_9EURY Unreviewed; 360 AA.
AC A0A162FI80;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
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_1 {ECO:0000313|EMBL:KZX13425.1};
GN Synonyms=purE {ECO:0000256|HAMAP-Rule:MF_01929};
GN ORFNames=MBCUR_06890 {ECO:0000313|EMBL:KZX13425.1};
OS Methanobrevibacter curvatus.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=49547 {ECO:0000313|EMBL:KZX13425.1, ECO:0000313|Proteomes:UP000077245};
RN [1] {ECO:0000313|EMBL:KZX13425.1, ECO:0000313|Proteomes:UP000077245}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11111 {ECO:0000313|EMBL:KZX13425.1,
RC ECO:0000313|Proteomes:UP000077245};
RA Poehlein A., Seedorf H., Daniel R.;
RT "Genome sequence of Methanobrevibacter curvatus DSM 11111.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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:KZX13425.1}.
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DR EMBL; LWMV01000146; KZX13425.1; -; Genomic_DNA.
DR RefSeq; WP_067090232.1; NZ_LWMV01000146.1.
DR AlphaFoldDB; A0A162FI80; -.
DR STRING; 49547.MBCUR_06890; -.
DR PATRIC; fig|49547.3.peg.741; -.
DR OrthoDB; 9473at2157; -.
DR UniPathway; UPA00074; UER00943.
DR Proteomes; UP000077245; 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; -; 2.
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; 2.
DR PANTHER; PTHR23046:SF2; PHOSPHORIBOSYLAMINOIMIDAZOLE CARBOXYLASE; 1.
DR PANTHER; PTHR23046; PHOSPHORIBOSYLAMINOIMIDAZOLE CARBOXYLASE CATALYTIC SUBUNIT; 1.
DR Pfam; PF00731; AIRC; 2.
DR SMART; SM01001; AIRC; 2.
DR SUPFAM; SSF52255; N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase, PurE); 2.
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:UP000077245}.
FT DOMAIN 3..151
FT /note="PurE"
FT /evidence="ECO:0000259|SMART:SM01001"
FT DOMAIN 214..360
FT /note="PurE"
FT /evidence="ECO:0000259|SMART:SM01001"
FT BINDING 11
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01929"
FT BINDING 14
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01929"
FT BINDING 41
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01929"
SQ SEQUENCE 360 AA; 38911 MW; 10251F8379CAC99C CRC64;
MNPKIMIILG SSSDIKIAEK AIDVLEKLQV PYSLHIASAH RTHEKVKNLV IQGTNEGIEV
FIAIAGLTAH LGGVIASYTH RPVVGVPVKA KLGGIDASFA TAQMPYPAPV ATVGIDRGDN
GAILAGQIIG INDYNVRKNI SNLRNSYVEK VDIDDKKIHS KLNGNYFNNT FLNDIINEKL
EDTDNLTDNL TDKYKINGDN DPNFNESKKD KDSPIVCVIP GSYSDMKVAK KVTNTLDRLR
INYDVNIISP VRNPVKFQKY IESQENVKVF IAVTGLSAHV SGSLVALSEK PVIGVPCAIE
LDGLDSLISM ISMPPGVPVG TVGISNGKNG AILAAEILAI ENKDIEANLK LLKYESNSIN
//
