PXPA2_BORBR
ID PXPA2_BORBR Reviewed; 250 AA.
AC Q7WEA9;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=BB4725;
OS Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)
OS (Alcaligenes bronchisepticus).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-588 / NCTC 13252 / RB50;
RX PubMed=12910271; DOI=10.1038/ng1227;
RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA Barrell B.G., Maskell D.J.;
RT "Comparative analysis of the genome sequences of Bordetella pertussis,
RT Bordetella parapertussis and Bordetella bronchiseptica.";
RL Nat. Genet. 35:32-40(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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX640451; CAE35088.1; -; Genomic_DNA.
DR RefSeq; WP_010927180.1; NC_002927.3.
DR AlphaFoldDB; Q7WEA9; -.
DR SMR; Q7WEA9; -.
DR STRING; 257310.BB4725; -.
DR EnsemblBacteria; CAE35088; CAE35088; BB4725.
DR KEGG; bbr:BB4725; -.
DR eggNOG; COG1540; Bacteria.
DR HOGENOM; CLU_069535_0_0_4; -.
DR OMA; PHGELYF; -.
DR OrthoDB; 918580at2; -.
DR Proteomes; UP000001027; 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..250
FT /note="5-oxoprolinase subunit A 2"
FT /id="PRO_0000184992"
SQ SEQUENCE 250 AA; 26569 MW; 422DB908B929A1DE CRC64;
MPSIDINCDM GESFGPWVMG QDTELMPHIT AANIACGFHA GDPDVMLATV RAAIAADVAI
GAHPGLPDLQ GFGRRVMAVT PDEVYALTVY QVGALQAIAR SQGGRLHHVK THGALYTLTA
RDPALADAVA RAVADVDPAL PIYVANAAIA QATRERGLRA VYEVYADRSY QDDGTLTPRS
QPHAMIEDVD QAIAQVKRMV KEGVVRALSG KDVPITADTL CIHGDQPGAA LFARRIRAAL
EAEGIEIRTV