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Database: UniProt
Entry: A0A1R1I2U2_9RHOO
LinkDB: A0A1R1I2U2_9RHOO
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ID   A0A1R1I2U2_9RHOO        Unreviewed;       165 AA.
AC   A0A1R1I2U2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
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=BJN45_11835 {ECO:0000313|EMBL:OMG52934.1};
OS   Azonexus hydrophilus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Azonexaceae;
OC   Azonexus.
OX   NCBI_TaxID=418702 {ECO:0000313|EMBL:OMG52934.1, ECO:0000313|Proteomes:UP000187526};
RN   [1] {ECO:0000313|EMBL:OMG52934.1, ECO:0000313|Proteomes:UP000187526}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZS02 {ECO:0000313|EMBL:OMG52934.1,
RC   ECO:0000313|Proteomes:UP000187526};
RA   Salah Z., Rout S.P., Humphreys P.N.;
RT   "Alkaliphiles isolated from bioreactors.";
RL   Submitted (OCT-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       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}.
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:OMG52934.1}.
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DR   EMBL; MTHD01000004; OMG52934.1; -; Genomic_DNA.
DR   RefSeq; WP_076095487.1; NZ_MTHD01000004.1.
DR   AlphaFoldDB; A0A1R1I2U2; -.
DR   STRING; 418702.BJN45_11835; -.
DR   OrthoDB; 9791908at2; -.
DR   UniPathway; UPA00074; UER00943.
DR   Proteomes; UP000187526; 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   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}; Reference proteome {ECO:0000313|Proteomes:UP000187526}.
FT   DOMAIN          6..157
FT                   /note="PurE"
FT                   /evidence="ECO:0000259|SMART:SM01001"
FT   BINDING         14
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01929,
FT                   ECO:0000256|PIRSR:PIRSR001338-1"
FT   BINDING         17
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01929,
FT                   ECO:0000256|PIRSR:PIRSR001338-1"
FT   BINDING         44
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01929,
FT                   ECO:0000256|PIRSR:PIRSR001338-1"
SQ   SEQUENCE   165 AA;  17019 MW;  F65B3B0428215E58 CRC64;
     MSEKKIAVGI VMGSDSDWPT MQAAAVMLKD FGVAFEARVV SAHRTPDLLF EYAETAGPRG
     LKAIIAGAGG AAHLPGMLAA KTIVPVLGVP VQSKALSGVD SLHSIVQMPK GIPVATFAIG
     EAGAANAALF AIAMLANEDP ALNEKLQAFR KAQTDKVLAM KLPEA
//
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