PXPA_MYCA1
ID PXPA_MYCA1 Reviewed; 252 AA.
AC A0QAC2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 66.
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=MAV_0580;
OS Mycobacterium avium (strain 104).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=243243;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=104;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) 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; CP000479; ABK67254.1; -; Genomic_DNA.
DR RefSeq; WP_011723652.1; NC_008595.1.
DR AlphaFoldDB; A0QAC2; -.
DR SMR; A0QAC2; -.
DR EnsemblBacteria; ABK67254; ABK67254; MAV_0580.
DR KEGG; mav:MAV_0580; -.
DR HOGENOM; CLU_069535_0_0_11; -.
DR OMA; DRTYKQD; -.
DR OrthoDB; 918580at2; -.
DR Proteomes; UP000001574; 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..252
FT /note="5-oxoprolinase subunit A"
FT /id="PRO_1000045209"
SQ SEQUENCE 252 AA; 26077 MW; BC4745517C8929FC CRC64;
MAGIDLNADL GEGFGVWRLG DDDAMLGIVS SANVACGFHA GDPAGLLRVC RSAAERGVRV
GAQVSYRDLA GFGRRFIDVA ADELLADVVY QIGALQAIAH AAGSSVCYVK PHGALYNTIV
THPAQAAAVA EAVRLVDPGL PVLGMAGSVF FDEAARRGLR VVAEAFADRA YRPDGRLVSR
REPGAVLADP AAIAERVLAM VETGAVTAVD GTRLALSVES VCVHGDSPGA VQIATAVRDR
LRAAGVEIRA FC