PXPA1_BRADU
ID PXPA1_BRADU Reviewed; 255 AA.
AC Q89P49;
DT 04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=5-oxoprolinase subunit A 1 {ECO:0000255|HAMAP-Rule:MF_00691};
DE Short=5-OPase subunit A 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_00691};
GN Name=pxpA1 {ECO:0000255|HAMAP-Rule:MF_00691}; OrderedLocusNames=blr3634;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
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; BA000040; BAC48899.1; -; Genomic_DNA.
DR RefSeq; NP_770274.1; NC_004463.1.
DR RefSeq; WP_011086415.1; NZ_CP011360.1.
DR AlphaFoldDB; Q89P49; -.
DR SMR; Q89P49; -.
DR STRING; 224911.27351894; -.
DR EnsemblBacteria; BAC48899; BAC48899; BAC48899.
DR GeneID; 64023371; -.
DR KEGG; bja:blr3634; -.
DR PATRIC; fig|224911.44.peg.3296; -.
DR eggNOG; COG1540; Bacteria.
DR HOGENOM; CLU_069535_0_0_5; -.
DR InParanoid; Q89P49; -.
DR OMA; MPGSVIC; -.
DR PhylomeDB; Q89P49; -.
DR Proteomes; UP000002526; 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 GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
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..255
FT /note="5-oxoprolinase subunit A 1"
FT /id="PRO_0000184995"
SQ SEQUENCE 255 AA; 27341 MW; 5907C40FD72A69DD CRC64;
MKIGINSDMG EGFGNYRICD DEALMSIVSS ANVACGFHAG DPIIMDRMVR LAKQKGVEVG
AHPGLPDLLG FGRRVIQMDA AELEKHMVYQ IGALQAIAAN AGHRVTHVSF HAAMGNMVNA
DPDMADVVAR AIATINRDFI VFSQPDAEIV RAARKVGLRT LTLFLADRAY DENGHLVSRK
LPNSVVTSTE AVAERVKRFL DSGTVQTIEG KSIKVEARSI LIHSDTPGSV NLAGTVRRVI
EQGGGEVTPA TVLLN