PXPA3_PSESM
ID PXPA3_PSESM Reviewed; 256 AA.
AC Q87UC7;
DT 04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=5-oxoprolinase subunit A 3 {ECO:0000255|HAMAP-Rule:MF_00691};
DE Short=5-OPase subunit A 3 {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 3 {ECO:0000255|HAMAP-Rule:MF_00691};
GN Name=pxpA3 {ECO:0000255|HAMAP-Rule:MF_00691}; OrderedLocusNames=PSPTO_5378;
OS Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=223283;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-871 / DC3000;
RX PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA Collmer A.;
RT "The complete genome sequence of the Arabidopsis and tomato pathogen
RT Pseudomonas syringae pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
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; AE016853; AAO58800.1; -; Genomic_DNA.
DR RefSeq; NP_795105.1; NC_004578.1.
DR RefSeq; WP_011105454.1; NC_004578.1.
DR AlphaFoldDB; Q87UC7; -.
DR SMR; Q87UC7; -.
DR STRING; 223283.PSPTO_5378; -.
DR EnsemblBacteria; AAO58800; AAO58800; PSPTO_5378.
DR GeneID; 1187065; -.
DR KEGG; pst:PSPTO_5378; -.
DR PATRIC; fig|223283.9.peg.5504; -.
DR eggNOG; COG1540; Bacteria.
DR HOGENOM; CLU_069535_0_0_6; -.
DR OMA; DRTYKQD; -.
DR OrthoDB; 918580at2; -.
DR PhylomeDB; Q87UC7; -.
DR Proteomes; UP000002515; 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; Reference proteome.
FT CHAIN 1..256
FT /note="5-oxoprolinase subunit A 3"
FT /id="PRO_0000185033"
SQ SEQUENCE 256 AA; 27063 MW; 37A9E496119BC4D4 CRC64;
MRAIDLNSDL GESFGAWSMG DDAAMLDIVT SANVACGFHA GDPAGILRTL KAAAAKNVTI
GAHVSYPDKV GFGRRNMDVA SDELTADVIY QIGSLQGLAK AAGTSVRYVK PHGALYNTIA
HDRRQAMAVI EAIRAIDPAL VLVALAGSTL IELARSEGLQ CIAEAFADRA YTPQGTLVSR
REPGAVLHDP ELVAQRMLRL VQSGSIEAID GSLVRIEADS ICVHGDSPAA VEMARELRRV
LEQASTSLQP FAGKRS