ID A0A1G7JDA8_9ACTN Unreviewed; 254 AA.
AC A0A1G7JDA8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=SAMN05660662_1444 {ECO:0000313|EMBL:SDF22911.1};
OS Blastococcus aurantiacus.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Blastococcus.
OX NCBI_TaxID=1550231 {ECO:0000313|EMBL:SDF22911.1, ECO:0000313|Proteomes:UP000199406};
RN [1] {ECO:0000313|EMBL:SDF22911.1, ECO:0000313|Proteomes:UP000199406}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44268 {ECO:0000313|EMBL:SDF22911.1,
RC ECO:0000313|Proteomes:UP000199406};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FNBT01000002; SDF22911.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7JDA8; -.
DR STRING; 1550231.SAMN05660662_1444; -.
DR OrthoDB; 9773478at2; -.
DR Proteomes; UP000199406; 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 254 AA; 25773 MW; 7202F1E331C90805 CRC64;
MSSTVDLNAD LGEGFGVWRL GDDEALLGVV TSANVACGFH AGDPTTMRRV CAGAAATGVA
VGAQVSYRDL AGFGRRFIDV EPAELADDVL YQLAALDGIA RAEGTRVRYV KPHGALYNAA
VGHEGQARAV VDAVVAHDPA LPVLGLPGSA LLRAAEAVGL RPFAEGFADR GYTADGGLVP
RREPGALVHD PAEVAARAVR MAVEGTVVAV DGSTVPAAVA SICVHGDTPG AVELARAVRT
ALEQAGVALT AFTG
//