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Database: UniProt
Entry: A0A1I0NKC4_9GAMM
LinkDB: A0A1I0NKC4_9GAMM
Original site: A0A1I0NKC4_9GAMM 
ID   A0A1I0NKC4_9GAMM        Unreviewed;       171 AA.
AC   A0A1I0NKC4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
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=SAMN04515660_1778 {ECO:0000313|EMBL:SEW01318.1};
OS   Luteibacter sp. 329MFSha.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Luteibacter.
OX   NCBI_TaxID=1798239 {ECO:0000313|EMBL:SEW01318.1, ECO:0000313|Proteomes:UP000199162};
RN   [1] {ECO:0000313|EMBL:SEW01318.1, ECO:0000313|Proteomes:UP000199162}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=329MFSha {ECO:0000313|EMBL:SEW01318.1,
RC   ECO:0000313|Proteomes:UP000199162};
RA   de Groot N.N.;
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}.
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DR   EMBL; FOJE01000001; SEW01318.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I0NKC4; -.
DR   STRING; 1798239.SAMN04515660_1778; -.
DR   UniPathway; UPA00074; UER00943.
DR   Proteomes; UP000199162; 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; AIR 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          12..163
FT                   /note="PurE"
FT                   /evidence="ECO:0000259|SMART:SM01001"
FT   BINDING         20
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01929,
FT                   ECO:0000256|PIRSR:PIRSR001338-1"
FT   BINDING         23
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01929,
FT                   ECO:0000256|PIRSR:PIRSR001338-1"
FT   BINDING         50
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01929,
FT                   ECO:0000256|PIRSR:PIRSR001338-1"
SQ   SEQUENCE   171 AA;  17523 MW;  17692B74E08F7568 CRC64;
     MISNEGNEAG APRVGVVMGS RSDWETMEHA SSMLTRMGIV HEVRVVSAHR TPDLLFDYAN
     TARGRGIQVI VAGAGGAAHL PGMLAAKTPL PVFGVPVQSK ALNGMDSLLS IAQMPAGIPV
     GTLAIGRAGA TNAALLAAAV LALHDPAVAA ALDAFRAEQT QTVLDNPDPR S
//
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