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Database: UniProt
Entry: A0A246G3L6_9PSED
LinkDB: A0A246G3L6_9PSED
Original site: A0A246G3L6_9PSED 
ID   A0A246G3L6_9PSED        Unreviewed;       247 AA.
AC   A0A246G3L6;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
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=CEC48_05435 {ECO:0000313|EMBL:OWP72818.1};
OS   Pseudomonas sp. K2I15.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=2013577 {ECO:0000313|EMBL:OWP72818.1, ECO:0000313|Proteomes:UP000197956};
RN   [1] {ECO:0000313|EMBL:OWP72818.1, ECO:0000313|Proteomes:UP000197956}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K2I15 {ECO:0000313|EMBL:OWP72818.1,
RC   ECO:0000313|Proteomes:UP000197956};
RA   Orellana P., Castillo D., Corsini G.;
RT   "Draft genome sequence of the Chilean Antartic Pseudomonas sp. strain
RT   K2I15.";
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:OWP72818.1}.
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DR   EMBL; NIXO01000005; OWP72818.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A246G3L6; -.
DR   OrthoDB; 9773478at2; -.
DR   Proteomes; UP000197956; 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   247 AA;  26584 MW;  5EC0CFDF5E575F9B CRC64;
     MSRLLLNCDI GESFGNWTLG LDAEVMPFID CANVACGFHA GDPSIMRKTV SLAFEHGVQV
     GAHPAYQDLQ GFGRRSMAYT PQEIQDLLHY QVGALDGICR AQGGRVSYVK PHGAMYNDMM
     AKPAQLRAVI QAVAAYDASL PLMLMATRDN SAAQALGDEY GVTLWFEAFA DRAYDSAGHL
     VSRQLPGAVH HDPEKIIQQA LTIARGEHLV ASDGSPLHLQ ANTLCVHGDN ASSVAAVQRI
     REALTPA
//
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