PXPA_SALDC
ID PXPA_SALDC Reviewed; 244 AA.
AC B5FNE9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 25-MAY-2022, entry version 57.
DE RecName: Full=5-oxoprolinase subunit A {ECO:0000255|HAMAP-Rule:MF_00691};
DE Short=5-OPase subunit A {ECO:0000255|HAMAP-Rule:MF_00691};
DE EC=3.5.2.9 {ECO:0000255|HAMAP-Rule:MF_00691};
DE AltName: Full=5-oxoprolinase (ATP-hydrolyzing) subunit A {ECO:0000255|HAMAP-Rule:MF_00691};
GN Name=pxpA {ECO:0000255|HAMAP-Rule:MF_00691}; OrderedLocusNames=SeD_A0822;
OS Salmonella dublin (strain CT_02021853).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=439851;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT_02021853;
RX PubMed=21602358; DOI=10.1128/jb.00297-11;
RA Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA Leclerc J.E., Ravel J., Cebula T.A.;
RT "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT CRISPR-mediated adaptive sublineage evolution.";
RL J. Bacteriol. 193:3556-3568(2011).
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:0000255|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:0000255|HAMAP-Rule:MF_00691};
CC -!- SUBUNIT: Forms a complex composed of PxpA, PxpB and PxpC.
CC {ECO:0000255|HAMAP-Rule:MF_00691}.
CC -!- SIMILARITY: Belongs to the LamB/PxpA family. {ECO:0000255|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; CP001144; ACH75651.1; -; Genomic_DNA.
DR RefSeq; WP_001017925.1; NC_011205.1.
DR AlphaFoldDB; B5FNE9; -.
DR SMR; B5FNE9; -.
DR KEGG; sed:SeD_A0822; -.
DR HOGENOM; CLU_069535_0_0_6; -.
DR OMA; DRTYKQD; -.
DR Proteomes; UP000008322; 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 HAMAP; MF_00691; PxpA; 1.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR005501; LamB/YcsF/PxpA-like.
DR PANTHER; PTHR30292; PTHR30292; 1.
DR Pfam; PF03746; LamB_YcsF; 1.
DR SUPFAM; SSF88713; SSF88713; 1.
PE 3: Inferred from homology;
KW ATP-binding; Hydrolase; Nucleotide-binding.
FT CHAIN 1..244
FT /note="5-oxoprolinase subunit A"
FT /id="PRO_1000132069"
SQ SEQUENCE 244 AA; 26063 MW; 22D49961415858A0 CRC64;
MNIDLNADVG EGCASDSELL TLVSSANIAC GFHAGDAQTM LTSVREALKN GVAIGAHPSF
PDRDNFGRTA MALPPETVYA QTLYQIGALG AIVQAQGSVM RHVKPHGMLY NQAAKDPHLA
QAIAKAVHDY DPSLILVGLA GSELIRAGER HRLVTRQEVF ADRGYQADGS LVPRMQPGAL
IHDEEQALAQ TLDMVQAGRV KSVTGVWTTV TAQTVCIHGD GEYALAFARR LRAAFNARNI
HVIA