PXPA_CUPTR
ID PXPA_CUPTR Reviewed; 246 AA.
AC B2AG42;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=5-oxoprolinase subunit A {ECO:0000255|HAMAP-Rule:MF_00691};
DE Short=5-OPase subunit A {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 {ECO:0000255|HAMAP-Rule:MF_00691};
GN Name=pxpA {ECO:0000255|HAMAP-Rule:MF_00691}; OrderedLocusNames=RALTA_A0068;
OS Cupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CCUG 44338 / CIP
OS 107171 / LMG 19424 / R1) (Ralstonia taiwanensis (strain LMG 19424)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=977880;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17343 / BCRC 17206 / CCUG 44338 / CIP 107171 / LMG 19424 / R1;
RX PubMed=18490699; DOI=10.1101/gr.076448.108;
RA Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D.,
RA Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V.,
RA Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C.,
RA Masson-Boivin C.;
RT "Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and
RT comparative genomics of rhizobia.";
RL Genome Res. 18:1472-1483(2008).
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; CU633749; CAP62741.1; -; Genomic_DNA.
DR RefSeq; WP_012351410.1; NC_010528.1.
DR AlphaFoldDB; B2AG42; -.
DR SMR; B2AG42; -.
DR STRING; 977880.RALTA_A0068; -.
DR EnsemblBacteria; CAP62741; CAP62741; RALTA_A0068.
DR GeneID; 29761463; -.
DR KEGG; cti:RALTA_A0068; -.
DR eggNOG; COG1540; Bacteria.
DR HOGENOM; CLU_069535_0_0_4; -.
DR OMA; DRTYKQD; -.
DR OrthoDB; 918580at2; -.
DR BioCyc; CTAI977880:RALTA_RS00340-MON; -.
DR Proteomes; UP000001692; Chromosome 1.
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 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.
FT CHAIN 1..246
FT /note="5-oxoprolinase subunit A"
FT /id="PRO_1000132048"
SQ SEQUENCE 246 AA; 26565 MW; 3C431AB1C9A932F5 CRC64;
MQIDLNADLG EGCGNDEALL ALISSANIAC GWHAGDAATM VQTVKWALAR GVAIGAHPSY
PDRENFGRTE MQRDPEHVYA DVLYQIGALD AIVRAQGGVL HHVKPHGALY NQAVRDPALA
RAIVRAVRDF DADLVFFGLA GSQMIDVAKE AGLRVKQEVF ADRGYNADGT LVRRGTPGAL
HEDEEVALDQ TLTMVREQRV RAIDGTWVPI RAETVCLHGD GAHALAFARR IRERLGAEGI
AIRAGD