ID A0A1B1Z8W9_9BACI Unreviewed; 255 AA.
AC A0A1B1Z8W9;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=ABE41_017895 {ECO:0000313|EMBL:ANX13888.1};
OS Fictibacillus arsenicus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Fictibacillus.
OX NCBI_TaxID=255247 {ECO:0000313|EMBL:ANX13888.1, ECO:0000313|Proteomes:UP000077412};
RN [1] {ECO:0000313|EMBL:ANX13888.1, ECO:0000313|Proteomes:UP000077412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G25-54 {ECO:0000313|EMBL:ANX13888.1,
RC ECO:0000313|Proteomes:UP000077412};
RA Zheng Z.;
RT "Complete genome sequence of Fictibacillus arsenicus G25-54, a strain with
RT toxicity to nematodes and a potential arsenic-resistance activity.";
RL Submitted (AUG-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; CP016761; ANX13888.1; -; Genomic_DNA.
DR RefSeq; WP_066293325.1; NZ_CP016761.1.
DR AlphaFoldDB; A0A1B1Z8W9; -.
DR STRING; 255247.ABE41_017895; -.
DR KEGG; far:ABE41_017895; -.
DR OrthoDB; 9773478at2; -.
DR Proteomes; UP000077412; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000077412}.
SQ SEQUENCE 255 AA; 27610 MW; 113D80C6AA279A1E CRC64;
MSVIDINCDM GESFGAYRLG TDEEILKYVT SANIACGFHA GDPATMRKTV KLALEHGVGI
GVHPGLPDLA GFGRRNIDIS PQEAYEMVVY QIGSLWAFVQ AEGGEIQHVK PHGALYNMAA
VNRELSEAIS EAVYKVNPEL ILFGLAGSEL VKAGEKVGLR TASEVFADRT YQQDCTLTSR
KLPNCMIEND DEAVAQVIRM VKEGKVLTQQ KVDADITADT VCIHGDGAHA LSFAKKIRQT
LEDSGITVRK IGESI
//