ID   PXPA_STRCO              Reviewed;         250 AA.
AC   Q9RL45;
DT   04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 83.
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=SCO0441;
GN   ORFNames=SCF51A.19;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(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}.
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DR   EMBL; AL939105; CAB56671.1; -; Genomic_DNA.
DR   RefSeq; NP_624762.1; NC_003888.3.
DR   RefSeq; WP_011027118.1; NZ_VNID01000015.1.
DR   AlphaFoldDB; Q9RL45; -.
DR   SMR; Q9RL45; -.
DR   STRING; 100226.SCO0441; -.
DR   GeneID; 1095864; -.
DR   KEGG; sco:SCO0441; -.
DR   PATRIC; fig|100226.15.peg.418; -.
DR   eggNOG; COG1540; Bacteria.
DR   HOGENOM; CLU_069535_0_0_11; -.
DR   InParanoid; Q9RL45; -.
DR   OMA; DRTYKQD; -.
DR   PhylomeDB; Q9RL45; -.
DR   Proteomes; UP000001973; 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..250
FT                   /note="5-oxoprolinase subunit A"
FT                   /id="PRO_0000185053"
SQ   SEQUENCE   250 AA;  25511 MW;  6F115EB480AD1700 CRC64;
     MIDLNADLGE GFGRWTLTDD DALLSVVTSA NVACGFHAGD PSVMRRVCDL AAERGVRIGA
     QVSYRDLAGF GRRAMDVPSD ELAAEVAYQI GALRVFAEAA GAPVAYVKPH GALYNRTVHD
     EGQARAVVAG VRLAGGALPV LGLPGSRLLT AAAEAGLTGV PEAFADRAYT AEGSLVPRSE
     AGSVVTDEDA VVRRALAFAV EGSVEAVDGT AVAVAARSLC VHGDTPNAAR IAARVREALE
     TAGVGIGAFA