PURE_PSEAE
ID PURE_PSEAE Reviewed; 163 AA.
AC P72157;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=N5-carboxyaminoimidazole ribonucleotide mutase {ECO:0000255|HAMAP-Rule:MF_01929};
DE Short=N5-CAIR mutase {ECO:0000255|HAMAP-Rule:MF_01929};
DE EC=5.4.99.18 {ECO:0000255|HAMAP-Rule:MF_01929};
DE AltName: Full=5-(carboxyamino)imidazole ribonucleotide mutase {ECO:0000255|HAMAP-Rule:MF_01929};
GN Name=purE {ECO:0000255|HAMAP-Rule:MF_01929}; OrderedLocusNames=PA5426;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PAK;
RX PubMed=8816818; DOI=10.1073/pnas.93.19.10434;
RA Wang J., Mushegian A., Lory S., Jin S.;
RT "Large-scale isolation of candidate virulence genes of Pseudomonas
RT aeruginosa by in vivo selection.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:10434-10439(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
CC -!- FUNCTION: Catalyzes the conversion of N5-carboxyaminoimidazole
CC ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide
CC (CAIR). {ECO:0000255|HAMAP-Rule:MF_01929}.
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:0000255|HAMAP-
CC Rule:MF_01929};
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:0000255|HAMAP-Rule:MF_01929}.
CC -!- SIMILARITY: Belongs to the AIR carboxylase family. Class I subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01929}.
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DR EMBL; U58364; AAB17257.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG08811.1; -; Genomic_DNA.
DR PIR; H82967; H82967.
DR RefSeq; NP_254113.1; NC_002516.2.
DR RefSeq; WP_003106314.1; NZ_QZGE01000012.1.
DR AlphaFoldDB; P72157; -.
DR SMR; P72157; -.
DR STRING; 287.DR97_2803; -.
DR PaxDb; P72157; -.
DR PRIDE; P72157; -.
DR DNASU; 877624; -.
DR EnsemblBacteria; AAG08811; AAG08811; PA5426.
DR GeneID; 877624; -.
DR KEGG; pae:PA5426; -.
DR PATRIC; fig|208964.12.peg.5686; -.
DR PseudoCAP; PA5426; -.
DR HOGENOM; CLU_094982_2_2_6; -.
DR InParanoid; P72157; -.
DR OMA; SNSIDGW; -.
DR PhylomeDB; P72157; -.
DR BioCyc; PAER208964:G1FZ6-5553-MON; -.
DR UniPathway; UPA00074; UER00943.
DR Proteomes; UP000002438; 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 HAMAP; MF_01929; PurE_classI; 1.
DR InterPro; IPR033747; PurE_ClassI.
DR InterPro; IPR000031; PurE_dom.
DR InterPro; IPR024694; PurE_prokaryotes.
DR Pfam; PF00731; AIRC; 1.
DR PIRSF; PIRSF001338; AIR_carboxylase; 1.
DR SMART; SM01001; AIRC; 1.
DR TIGRFAMs; TIGR01162; purE; 1.
PE 3: Inferred from homology;
KW Isomerase; Purine biosynthesis; Reference proteome.
FT CHAIN 1..163
FT /note="N5-carboxyaminoimidazole ribonucleotide mutase"
FT /id="PRO_0000074978"
FT BINDING 11
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01929"
FT BINDING 14
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01929"
FT BINDING 41
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01929"
FT CONFLICT 46
FT /note="L -> F (in Ref. 1; AAB17257)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="A -> E (in Ref. 1; AAB17257)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 163 AA; 16889 MW; 447CA86962BC31FF CRC64;
MSALVGVIMG SKSDWSTLSH TADMLDKLGI PYEVKVVSAH RTPDLLFQYA EEAEGRGLEV
IIAGAGGAAH LPGMCAAKTH LPVLGVPVQS SMLSGVDSLL SIVQMPAGVP VATLAIGKAG
AVNAALLSAS ILGAKHPQYH EALKQFRANQ TETVLDNPDP RDA
