PXPA1_PSEAE
ID PXPA1_PSEAE Reviewed; 252 AA.
AC Q9I626;
DT 04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=5-oxoprolinase subunit A 1 {ECO:0000255|HAMAP-Rule:MF_00691};
DE Short=5-OPase subunit A 1 {ECO:0000255|HAMAP-Rule:MF_00691};
DE EC=3.5.2.9 {ECO:0000255|HAMAP-Rule:MF_00691};
DE AltName: Full=5-oxoprolinase (ATP-hydrolyzing) subunit A 1 {ECO:0000255|HAMAP-Rule:MF_00691};
GN Name=pxpA1 {ECO:0000255|HAMAP-Rule:MF_00691}; OrderedLocusNames=PA0492;
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 [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 cleavage of 5-oxoproline to form L-glutamate
CC coupled to the hydrolysis of ATP to ADP and inorganic phosphate.
CC {ECO:0000255|HAMAP-Rule:MF_00691}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-oxo-L-proline + ATP + 2 H2O = ADP + H(+) + L-glutamate +
CC phosphate; Xref=Rhea:RHEA:10348, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58402, ChEBI:CHEBI:456216; EC=3.5.2.9;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00691};
CC -!- SUBUNIT: Forms a complex composed of PxpA, PxpB and PxpC.
CC {ECO:0000255|HAMAP-Rule:MF_00691}.
CC -!- SIMILARITY: Belongs to the LamB/PxpA family. {ECO:0000255|HAMAP-
CC Rule:MF_00691}.
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DR EMBL; AE004091; AAG03881.1; -; Genomic_DNA.
DR PIR; G83584; G83584.
DR RefSeq; NP_249183.1; NC_002516.2.
DR RefSeq; WP_003103315.1; NZ_QZGE01000010.1.
DR AlphaFoldDB; Q9I626; -.
DR SMR; Q9I626; -.
DR STRING; 287.DR97_3460; -.
DR PaxDb; Q9I626; -.
DR PRIDE; Q9I626; -.
DR EnsemblBacteria; AAG03881; AAG03881; PA0492.
DR GeneID; 879645; -.
DR KEGG; pae:PA0492; -.
DR PATRIC; fig|208964.12.peg.519; -.
DR PseudoCAP; PA0492; -.
DR HOGENOM; CLU_069535_0_0_6; -.
DR InParanoid; Q9I626; -.
DR OMA; MPGSVIC; -.
DR PhylomeDB; Q9I626; -.
DR BioCyc; PAER208964:G1FZ6-497-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0017168; F:5-oxoprolinase (ATP-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
DR HAMAP; MF_00691; PxpA; 1.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR005501; LamB/YcsF/PxpA-like.
DR PANTHER; PTHR30292; PTHR30292; 1.
DR Pfam; PF03746; LamB_YcsF; 1.
DR SUPFAM; SSF88713; SSF88713; 1.
PE 3: Inferred from homology;
KW ATP-binding; Hydrolase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..252
FT /note="5-oxoprolinase subunit A 1"
FT /id="PRO_0000185025"
SQ SEQUENCE 252 AA; 27559 MW; 7DC557F4E0A0A956 CRC64;
MTEVDLNSDM GEGFGPWTIG DGVDAAIMPL ISSANIATGF HAGDPSSMRR TVEMAAEHGV
AIGAHPGFRD LVGFGRRHIA APAIELVNDM LYQLGALREF ARLQGLSLQH VKPHGALYMH
LARDEVAARL FVETLQRLEP ELLLYCMPGS ATWRIGRELG QPLVREFYAD RDYDRSGSIV
FTRRVAALDP QQVADKVLRA CREGKVRTVE GEDLDIAFDS VCIHSDTPGA LELVASTRAR
LEGAGIRIKA PR