ID Q2KTU9_BORA1 Unreviewed; 258 AA.
AC Q2KTU9;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=5-oxoprolinase subunit A {ECO:0000256|HAMAP-Rule:MF_00691};
DE Short=5-OPase subunit A {ECO:0000256|HAMAP-Rule:MF_00691};
DE EC=3.5.2.9 {ECO:0000256|HAMAP-Rule:MF_00691};
DE AltName: Full=5-oxoprolinase (ATP-hydrolyzing) subunit A {ECO:0000256|HAMAP-Rule:MF_00691};
GN Name=pxpA {ECO:0000256|HAMAP-Rule:MF_00691};
GN OrderedLocusNames=BAV3301 {ECO:0000313|EMBL:CAJ50911.1};
OS Bordetella avium (strain 197N).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=360910 {ECO:0000313|EMBL:CAJ50911.1, ECO:0000313|Proteomes:UP000001977};
RN [1] {ECO:0000313|EMBL:CAJ50911.1, ECO:0000313|Proteomes:UP000001977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=197N {ECO:0000313|EMBL:CAJ50911.1,
RC ECO:0000313|Proteomes:UP000001977};
RX PubMed=16885469; DOI=10.1128/JB.01927-05;
RA Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA Parkhill J., Temple L.M.;
RT "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT extensive diversity in surface structures associated with host
RT interaction.";
RL J. Bacteriol. 188:6002-6015(2006).
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:0000256|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:0000256|HAMAP-Rule:MF_00691};
CC -!- SUBUNIT: Forms a complex composed of PxpA, PxpB and PxpC.
CC {ECO:0000256|HAMAP-Rule:MF_00691}.
CC -!- SIMILARITY: Belongs to the LamB/PxpA family. {ECO:0000256|HAMAP-
CC Rule:MF_00691}.
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DR EMBL; AM167904; CAJ50911.1; -; Genomic_DNA.
DR RefSeq; WP_012418938.1; NC_010645.1.
DR AlphaFoldDB; Q2KTU9; -.
DR STRING; 360910.BAV3301; -.
DR GeneID; 41395131; -.
DR KEGG; bav:BAV3301; -.
DR eggNOG; COG1540; Bacteria.
DR HOGENOM; CLU_069535_0_0_4; -.
DR OrthoDB; 9773478at2; -.
DR Proteomes; UP000001977; 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 CDD; cd11664; LamB_YcsF_like_2; 1.
DR Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
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:SF0; 5-OXOPROLINASE SUBUNIT A; 1.
DR PANTHER; PTHR30292; UNCHARACTERIZED PROTEIN YBGL-RELATED; 1.
DR Pfam; PF03746; LamB_YcsF; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00691};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00691};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00691};
KW Reference proteome {ECO:0000313|Proteomes:UP000001977}.
SQ SEQUENCE 258 AA; 28315 MW; 0DAA06C3F9232990 CRC64;
MTKASIDLNS DMGEGFGPWK IGDGVDEQIM PLISSANIAT GFHAGDPNIM SRTVLMAREH
GVGIGAHPGF RDLAGFGRRD LKESAEGLVN DIVYQLGALR EFARLHGVRL QHIKPHGALY
MLAARDETLS RRLVQTLREL EPTLYLYCME NSVTCKVARE LGQPVVREFY ADRDYDSSGS
IVFTRYTKAL DPAQVAAKVL RACTEGRVRT VEGQDIPIDF DSVCIHSDTP GALELVEATR
QHLQAAGIRI SPPPFPAL
//