ID A0A165JX09_9BURK Unreviewed; 164 AA.
AC A0A165JX09;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=A1D30_17235 {ECO:0000313|EMBL:KZT14781.1};
OS Acidovorax sp. GW101-3H11.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=1813946 {ECO:0000313|EMBL:KZT14781.1, ECO:0000313|Proteomes:UP000077219};
RN [1] {ECO:0000313|Proteomes:UP000077219}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GW101-3H11 {ECO:0000313|Proteomes:UP000077219};
RA Ray J., Price M., Deutschbauer A.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KZT14781.1, ECO:0000313|Proteomes:UP000077219}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GW101-3H11 {ECO:0000313|EMBL:KZT14781.1,
RC ECO:0000313|Proteomes:UP000077219};
RX PubMed=29769716; DOI=10.1038/s41586-018-0124-0;
RA Price M.N., Wetmore K.M., Waters R.J., Callaghan M., Ray J., Liu H.,
RA Kuehl J.V., Melnyk R.A., Lamson J.S., Suh Y., Carlson H.K., Esquivel Z.,
RA Sadeeshkumar H., Chakraborty R., Zane G.M., Rubin B.E., Wall J.D.,
RA Visel A., Bristow J., Blow M.J., Arkin A.P., Deutschbauer A.M.;
RT "Mutant phenotypes for thousands of bacterial genes of unknown function.";
RL Nature 557:503-509(2018).
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:KZT14781.1}.
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DR EMBL; LUKZ01000017; KZT14781.1; -; Genomic_DNA.
DR RefSeq; WP_063461753.1; NZ_LUKZ01000017.1.
DR AlphaFoldDB; A0A165JX09; -.
DR STRING; 1813946.A1D30_17235; -.
DR OrthoDB; 9791908at2; -.
DR UniPathway; UPA00074; UER00943.
DR Proteomes; UP000077219; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW Rule:MF_01929}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 112..134
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 4..155
FT /note="PurE"
FT /evidence="ECO:0000259|SMART:SM01001"
FT BINDING 12
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01929,
FT ECO:0000256|PIRSR:PIRSR001338-1"
FT BINDING 15
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01929,
FT ECO:0000256|PIRSR:PIRSR001338-1"
FT BINDING 42
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01929,
FT ECO:0000256|PIRSR:PIRSR001338-1"
SQ SEQUENCE 164 AA; 17082 MW; 6F3148C48DD99A57 CRC64;
MKPIQIGVVM GSSSDWDTMQ HAVQILEQFG IAHEARVVSA HRMPDDMFAY AESAASRGLK
AIIAGAGGAA HLPGMIAAKT PVPVLGVPVA SRHLQGVDSL HSIVQMPKGI PVATFAIGTA
GAANAALFAV ALLANESPEL RQRLEAFRAE QTEVARNMTL PPAA
//
