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Database: UniProt
Entry: A0A0G3LMA5_XANCT
LinkDB: A0A0G3LMA5_XANCT
Original site: A0A0G3LMA5_XANCT 
ID   A0A0G3LMA5_XANCT        Unreviewed;       167 AA.
AC   A0A0G3LMA5;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 43.
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   ECO:0000313|EMBL:QEO26829.1};
GN   ORFNames=F0H32_12025 {ECO:0000313|EMBL:QEO26829.1}, FD63_11670
GN   {ECO:0000313|EMBL:AKK68086.1};
OS   Xanthomonas translucens pv. undulosa.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=487909 {ECO:0000313|EMBL:QEO26829.1, ECO:0000313|Proteomes:UP000324457};
RN   [1] {ECO:0000313|Proteomes:UP000035194}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Xtu4699 {ECO:0000313|Proteomes:UP000035194};
RA   Peng Z., Potnis N., Jones J., Liu Z., White F.F., Liu S.;
RT   "A complete genome of Xanthomonas translucens and the full TAL effector
RT   gene content using long read sequencing.";
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AKK68086.1, ECO:0000313|Proteomes:UP000035194}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Xtu 4699 {ECO:0000313|EMBL:AKK68086.1}, and Xtu4699
RC   {ECO:0000313|Proteomes:UP000035194};
RX   PubMed=26729225; DOI=10.1186/s12864-015-2348-9;
RA   Peng Z., Hu Y., Xie J., Potnis N., Akhunova A., Jones J., Liu Z.,
RA   White F.F., Liu S.;
RT   "Long read and single molecule DNA sequencing simplifies genome assembly
RT   and TAL effector gene analysis of Xanthomonas translucens.";
RL   BMC Genomics 17:21-21(2016).
RN   [3] {ECO:0000313|EMBL:QEO26829.1, ECO:0000313|Proteomes:UP000324457}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LW16 {ECO:0000313|EMBL:QEO26829.1,
RC   ECO:0000313|Proteomes:UP000324457};
RA   Peng Z., Huguet-Tapia J.C., White F.;
RT   "Xanthomonas translucens pv. undulosa LW16.";
RL   Submitted (AUG-2019) 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; CP008714; AKK68086.1; -; Genomic_DNA.
DR   EMBL; CP043540; QEO26829.1; -; Genomic_DNA.
DR   RefSeq; WP_003468225.1; NZ_MADU01000038.1.
DR   AlphaFoldDB; A0A0G3LMA5; -.
DR   STRING; 487909.FD63_11670; -.
DR   GeneID; 66890600; -.
DR   KEGG; xtn:FD63_11670; -.
DR   UniPathway; UPA00074; UER00943.
DR   Proteomes; UP000035194; Chromosome.
DR   Proteomes; UP000324457; Chromosome.
DR   GO; GO:0034023; F:5-(carboxyamino)imidazole ribonucleotide mutase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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   Lyase {ECO:0000313|EMBL:QEO26829.1};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW   Rule:MF_01929}.
FT   DOMAIN          8..159
FT                   /note="PurE"
FT                   /evidence="ECO:0000259|SMART:SM01001"
FT   BINDING         16
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01929,
FT                   ECO:0000256|PIRSR:PIRSR001338-1"
FT   BINDING         19
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01929,
FT                   ECO:0000256|PIRSR:PIRSR001338-1"
FT   BINDING         46
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01929,
FT                   ECO:0000256|PIRSR:PIRSR001338-1"
SQ   SEQUENCE   167 AA;  17180 MW;  CB930F0B0F98DB35 CRC64;
     MTSKQTTPLV GIVMGSRSDW ETMQHAAQKL DALGVPYEVK VVSAHRTPDV LFAYAEAAST
     RGLRAIVAGA GGAAHLPGML AAKTAVPVLG VPVQSKALNG LDSLLSIVQM PAGIPVATFA
     IGNAGAANAA LFAAAMLAAE HADIGTALHA FRQRQTDEVM AKDDPRQ
//
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