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Database: UniProt
Entry: D7BRG6_STRBB
LinkDB: D7BRG6_STRBB
Original site: D7BRG6_STRBB 
ID   D7BRG6_STRBB            Unreviewed;       255 AA.
AC   D7BRG6;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 56.
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=SBI_02008 {ECO:0000313|EMBL:ADI05129.1};
OS   Streptomyces bingchenggensis (strain BCW-1).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=749414 {ECO:0000313|EMBL:ADI05129.1, ECO:0000313|Proteomes:UP000000377};
RN   [1] {ECO:0000313|EMBL:ADI05129.1, ECO:0000313|Proteomes:UP000000377}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCW-1 {ECO:0000313|EMBL:ADI05129.1,
RC   ECO:0000313|Proteomes:UP000000377};
RX   PubMed=20581206; DOI=10.1128/JB.00596-10;
RA   Wang X.J., Yan Y.J., Zhang B., An J., Wang J.J., Tian J., Jiang L.,
RA   Chen Y.H., Huang S.X., Yin M., Zhang J., Gao A.L., Liu C.X., Zhu Z.X.,
RA   Xiang W.S.;
RT   "Genome sequence of the milbemycin-producing bacterium Streptomyces
RT   bingchenggensis.";
RL   J. Bacteriol. 192:4526-4527(2010).
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; CP002047; ADI05129.1; -; Genomic_DNA.
DR   AlphaFoldDB; D7BRG6; -.
DR   STRING; 749414.SBI_02008; -.
DR   KEGG; sbh:SBI_02008; -.
DR   PATRIC; fig|749414.3.peg.2077; -.
DR   eggNOG; COG1540; Bacteria.
DR   HOGENOM; CLU_069535_0_0_11; -.
DR   Proteomes; UP000000377; 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; cd10787; LamB_YcsF_like; 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:UP000000377}.
SQ   SEQUENCE   255 AA;  26897 MW;  204B20EB1FF14C6C CRC64;
     MTDPTIDLNA DLGEGFGRWQ LTDDDALLSV VTSANVACGY HAGDPSTMRR VCELAAERGV
     RIGAQVSYRD LAGFGRRAMD VPPRELTDEI AYQIGALRVF ARSAGSDVVY VKPHGALYNR
     CVHDEAQAAA VVEGIRLAAD APLPVLGLPG SRLHEAAGAA GLPVVREGFA DRAYTAAGTL
     VPRSEPGAVV TDPGTIVKRS LAFARDKSVT SIDGRPVEVD IRSLCVHGDT PGAADIARRV
     RAELESAGVR VEPFV
//
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