PXPA_PHOLL
ID PXPA_PHOLL Reviewed; 252 AA.
AC Q7MZI3;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 2.
DT 03-AUG-2022, entry version 85.
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=plu4304;
OS Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS TT01).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Photorhabdus.
OX NCBI_TaxID=243265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15139 / CIP 105565 / TT01;
RX PubMed=14528314; DOI=10.1038/nbt886;
RA Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA Glaser P., Boemare N., Danchin A., Kunst F.;
RT "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT luminescens.";
RL Nat. Biotechnol. 21:1307-1313(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAE16676.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BX571873; CAE16676.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041380395.1; NC_005126.1.
DR AlphaFoldDB; Q7MZI3; -.
DR SMR; Q7MZI3; -.
DR STRING; 243265.plu4304; -.
DR EnsemblBacteria; CAE16676; CAE16676; plu4304.
DR GeneID; 24169250; -.
DR KEGG; plu:plu4304; -.
DR eggNOG; COG1540; Bacteria.
DR HOGENOM; CLU_069535_0_0_6; -.
DR OrthoDB; 918580at2; -.
DR BioCyc; PLUM243265:PLU_RS21270-MON; -.
DR Proteomes; UP000002514; 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..252
FT /note="5-oxoprolinase subunit A"
FT /id="PRO_0000185023"
SQ SEQUENCE 252 AA; 26882 MW; 554BB34593087E3F CRC64;
MNMIDLNSDL GEGFGQWKMG DDNTMLSIVT SANVACGFHA GDPAGIFQTL KSAHKNQVVI
GAHVSYPDLV GFGRRNMDVS SNELIADVIY QIGALKGLAV AAGTTVSYVK PHGALYNTIA
HNEYQALAVI TAIREVDDNL VLVGLAGSKL LDLAQENGLR TVAEAFADRA YTPQGTLVSR
REKGSVLHDA NLVARRMLQL VTEGGVEAID GSFTRIQADS ICVHGDSPDA VEMARQVKLT
LQQAGITVRS FI