ID A0A270P9M2_9PSED Unreviewed; 250 AA.
AC A0A270P9M2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=5-oxoprolinase subunit A {ECO:0000256|HAMAP-Rule:MF_00691};
DE Short=5-OPase subunit A {ECO:0000256|HAMAP-Rule:MF_00691};
DE EC=3.5.2.9 {ECO:0000256|HAMAP-Rule:MF_00691};
DE AltName: Full=5-oxoprolinase (ATP-hydrolyzing) subunit A {ECO:0000256|HAMAP-Rule:MF_00691};
GN Name=pxpA {ECO:0000256|HAMAP-Rule:MF_00691};
GN ORFNames=CES87_27350 {ECO:0000313|EMBL:PAM81159.1};
OS Pseudomonas sp. ERMR1:02.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1805930 {ECO:0000313|EMBL:PAM81159.1, ECO:0000313|Proteomes:UP000215719};
RN [1] {ECO:0000313|EMBL:PAM81159.1, ECO:0000313|Proteomes:UP000215719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ERMR1:02 {ECO:0000313|EMBL:PAM81159.1,
RC ECO:0000313|Proteomes:UP000215719};
RA Kumar R., Acharya V., Singh D., Kumar S.;
RT "Pseudomonas sp. ERMR1:02, Genome sequencing and assembly.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-Rule:MF_00691};
CC -!- SUBUNIT: Forms a complex composed of PxpA, PxpB and PxpC.
CC {ECO:0000256|HAMAP-Rule:MF_00691}.
CC -!- SIMILARITY: Belongs to the LamB/PxpA family. {ECO:0000256|HAMAP-
CC Rule:MF_00691}.
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:PAM81159.1}.
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DR EMBL; NKJI01000023; PAM81159.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A270P9M2; -.
DR OrthoDB; 9773478at2; -.
DR Proteomes; UP000215719; Unassembled WGS sequence.
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 CDD; cd10787; LamB_YcsF_like; 1.
DR Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
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:SF0; 5-OXOPROLINASE SUBUNIT A; 1.
DR PANTHER; PTHR30292; UNCHARACTERIZED PROTEIN YBGL-RELATED; 1.
DR Pfam; PF03746; LamB_YcsF; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00691};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00691};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00691}.
SQ SEQUENCE 250 AA; 26990 MW; DC704291CA46660B CRC64;
MSRLLLNCDI GESFGNWTMG LDAEVMPFID CANIACGFHA GDPSIMRKTV SLALSHGVQI
GAHPAYQDLV GFGRRSMAYT SQELQDILHY QIGALDGICR AQGGRVSYVK PHGAMYNDMM
ANPAQLRAVL QAVAAYDRSL PLMLMATRDN SAAQQLGDEY GVTLWFEAFA DRAYDSAGML
VSRSLPGAVH HDPEKIIEQA LIIARDDHLT ASDGSALHLQ ANTLCVHGDN ASSVAAVQRI
RQALNEQSAS
//
