ID A0A177PA09_9GAMM Unreviewed; 165 AA.
AC A0A177PA09;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=N5-carboxyaminoimidazole ribonucleotide mutase {ECO:0000256|HAMAP-Rule:MF_01929, ECO:0000256|PIRNR:PIRNR001338};
DE Short=N5-CAIR mutase {ECO:0000256|HAMAP-Rule:MF_01929, ECO:0000256|PIRNR:PIRNR001338};
DE EC=5.4.99.18 {ECO:0000256|HAMAP-Rule:MF_01929, ECO:0000256|PIRNR:PIRNR001338};
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=A1356_00685 {ECO:0000313|EMBL:OAI26684.1}, A1507_17105
GN {ECO:0000313|EMBL:OAI13296.1}, MKLM6_2143
GN {ECO:0000313|EMBL:ATG90370.1};
OS Methylomonas koyamae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylomonas.
OX NCBI_TaxID=702114 {ECO:0000313|EMBL:OAI13296.1, ECO:0000313|Proteomes:UP000077857};
RN [1] {ECO:0000313|EMBL:OAI26684.1, ECO:0000313|Proteomes:UP000077734}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R-49807 {ECO:0000313|EMBL:OAI26684.1,
RC ECO:0000313|Proteomes:UP000077734};
RA Heylen K., De Vos P., Vekeman B.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OAI13296.1, ECO:0000313|Proteomes:UP000077857}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R-45378 {ECO:0000313|EMBL:OAI13296.1,
RC ECO:0000313|Proteomes:UP000077857};
RA Ploux O.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ATG90370.1, ECO:0000313|Proteomes:UP000242123}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LM6 {ECO:0000313|EMBL:ATG90370.1,
RC ECO:0000313|Proteomes:UP000242123};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-2017) 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 ECO:0000256|PIRNR:PIRNR001338}.
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, ECO:0000256|PIRNR:PIRNR001338};
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, ECO:0000256|PIRNR:PIRNR001338}.
CC -!- SIMILARITY: Belongs to the AIR carboxylase family. Class I subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01929}.
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DR EMBL; CP023669; ATG90370.1; -; Genomic_DNA.
DR EMBL; LUUJ01000101; OAI13296.1; -; Genomic_DNA.
DR EMBL; LUUL01000069; OAI26684.1; -; Genomic_DNA.
DR RefSeq; WP_054759649.1; NZ_LUUL01000069.1.
DR KEGG; mko:MKLM6_2143; -.
DR OrthoDB; 9791908at2; -.
DR UniPathway; UPA00074; UER00943.
DR Proteomes; UP000077734; Unassembled WGS sequence.
DR Proteomes; UP000077857; Unassembled WGS sequence.
DR Proteomes; UP000242123; 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 PIRSF; PIRSF001338; AIR_carboxylase; 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 3..154
FT /note="PurE"
FT /evidence="ECO:0000259|SMART:SM01001"
FT BINDING 11
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01929,
FT ECO:0000256|PIRSR:PIRSR001338-1"
FT BINDING 14
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01929,
FT ECO:0000256|PIRSR:PIRSR001338-1"
FT BINDING 41
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01929,
FT ECO:0000256|PIRSR:PIRSR001338-1"
SQ SEQUENCE 165 AA; 17123 MW; B63F317D3B130195 CRC64;
MTALIGIIMG STSDWETMQH AAQTLEHLDI PHEVEVVSAH RTPDKLFRYA ETAESKGLEV
IIAGAGGAAH LPGMTAAKTA LPVLGVPVQS KALNGMDSLL SIVQMPAGIP VGTLAIGKAG
AINAALLAAA IVSNKHPQYR SALDAYRQQQ TDSVIATPDP RQVAG
//
