PXPA_PECCP
ID PXPA_PECCP Reviewed; 245 AA.
AC C6DCC6;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 25-MAY-2022, entry version 59.
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=PC1_1228;
OS Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=561230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC1;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Balakrishnan V., Glasner J., Perna N.T.;
RT "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL Submitted (JUL-2009) 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: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}.
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DR EMBL; CP001657; ACT12276.1; -; Genomic_DNA.
DR RefSeq; WP_015839508.1; NC_012917.1.
DR AlphaFoldDB; C6DCC6; -.
DR SMR; C6DCC6; -.
DR STRING; 561230.PC1_1228; -.
DR EnsemblBacteria; ACT12276; ACT12276; PC1_1228.
DR KEGG; pct:PC1_1228; -.
DR eggNOG; COG1540; Bacteria.
DR HOGENOM; CLU_069535_0_0_6; -.
DR OMA; DRTYKQD; -.
DR OrthoDB; 918580at2; -.
DR Proteomes; UP000002736; 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..245
FT /note="5-oxoprolinase subunit A"
FT /id="PRO_1000212584"
SQ SEQUENCE 245 AA; 26112 MW; 85994D10B60C3921 CRC64;
MIIDLNADLG EGGENDEALL KLVTSANIAC GFHAGDAQTM RQSVRWGIGY GVALGAHPSF
PDRENFGRKA MNVPAEIVFA QMVYQLGALS AIVAAEGGTL SHVKPHGMLY NQAACEPALA
DAIAKAVKVV NPALRLVGLA GSELIRAGQR LGLETRQEVF ADRCYLPDGT LVPRTQAGAL
INSDELALAQ TLEMIQRQRV RAIDGSWVTV QADTVCIHGD GQHALLFARK LRSCFSEHQI
TVAAA