ID A0A1N7LSM1_9BACI Unreviewed; 251 AA. AC A0A1N7LSM1; DT 15-MAR-2017, integrated into UniProtKB/TrEMBL. DT 15-MAR-2017, sequence version 1. DT 08-NOV-2023, 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=SAMN05421758_105141 {ECO:0000313|EMBL:SIS76701.1}; OS Salimicrobium salexigens. OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Salimicrobium. OX NCBI_TaxID=908941 {ECO:0000313|EMBL:SIS76701.1, ECO:0000313|Proteomes:UP000199777}; RN [1] {ECO:0000313|EMBL:SIS76701.1, ECO:0000313|Proteomes:UP000199777} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 22782 {ECO:0000313|EMBL:SIS76701.1, RC ECO:0000313|Proteomes:UP000199777}; RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.; RL Submitted (JAN-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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; FTOK01000005; SIS76701.1; -; Genomic_DNA. DR RefSeq; WP_076571309.1; NZ_FTOK01000005.1. DR AlphaFoldDB; A0A1N7LSM1; -. DR EnsemblBacteria; SIS76701; SIS76701; SAMN05421758_105141. DR Proteomes; UP000199777; 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 251 AA; 27127 MW; CBE2D19BF2396568 CRC64; MAIDLNCDMG EGFGVYNKGR DREVLDHVTS ANIACGFHAG DSRLMKETVR MAAEKNVAVG AHPGLPDLAG FGRRKMDITP EDAYDFVLYQ TGALQAFAEA EGTRLQHVKP HGALYNTAAK DAELAQAIAE AVRDAGGMML YGLAGSELLK AGKNAGLTVV SEVFADRLYQ PDGTLTPRKE KGAVITDREQ ALEQVRDMVL HQRVKTGEGT TIDIQADSVC VHGDNSEAVD FTRSIRKFLE DNDISMKAPD V //