PXPA2_BURPS
ID PXPA2_BURPS Reviewed; 266 AA.
AC Q63NV1;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=5-oxoprolinase subunit A 2 {ECO:0000255|HAMAP-Rule:MF_00691};
DE Short=5-OPase subunit A 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_00691};
GN Name=pxpA2 {ECO:0000255|HAMAP-Rule:MF_00691}; OrderedLocusNames=BPSS0198;
OS Burkholderia pseudomallei (strain K96243).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=272560;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K96243;
RX PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D.,
RA Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A.,
RA Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A.,
RA Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z.,
RA Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S.,
RA Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M.,
RA Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT pseudomallei.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
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; BX571966; CAH37643.1; -; Genomic_DNA.
DR RefSeq; WP_004529746.1; NZ_CP009537.1.
DR RefSeq; YP_110218.1; NC_006351.1.
DR AlphaFoldDB; Q63NV1; -.
DR SMR; Q63NV1; -.
DR STRING; 272560.BPSS0198; -.
DR EnsemblBacteria; CAH37643; CAH37643; BPSS0198.
DR GeneID; 56531349; -.
DR KEGG; bps:BPSS0198; -.
DR PATRIC; fig|272560.51.peg.6266; -.
DR eggNOG; COG1540; Bacteria.
DR OMA; PHGELYF; -.
DR Proteomes; UP000000605; Chromosome 2.
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; Reference proteome.
FT CHAIN 1..266
FT /note="5-oxoprolinase subunit A 2"
FT /id="PRO_0000184999"
SQ SEQUENCE 266 AA; 28868 MW; 51DDB4CFC5EC3709 CRC64;
MRKHSVDLNS DMGEGFGPWK IGDGVDEEIM PLISSANIAT GFHAGDPNII ARTVQLAKNA
GVGVGAHPGF RDLVGFGRRD IGETPQALVN DIVYQLGALR EFARFHGVSV QHVKPHGALY
MRAARDEALS RLLVETLQQL DPALRLYCME ASVTYRIARE LGQPVVREFY ADRDYGRNGS
IVFTRRAGRL DPRQVADKVL RACVDGRVAT VDGEDIDIDF DSICLHSDTP GALALARATR
DALTAHGIRI AAPATAEANG IRIDEA
