ID   PXPA_THET2              Reviewed;         250 AA.
AC   Q746B8;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 85.
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=TT_P0137;
OS   Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OG   Plasmid pTT27.
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=262724;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX   PubMed=15064768; DOI=10.1038/nbt956;
RA   Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA   Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA   Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA   Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT   "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL   Nat. Biotechnol. 22:547-553(2004).
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; AE017222; AAS82467.1; -; Genomic_DNA.
DR   RefSeq; WP_011174427.1; NC_005838.1.
DR   AlphaFoldDB; Q746B8; -.
DR   SMR; Q746B8; -.
DR   STRING; 262724.TT_P0137; -.
DR   EnsemblBacteria; AAS82467; AAS82467; TT_P0137.
DR   KEGG; tth:TT_P0137; -.
DR   eggNOG; COG1540; Bacteria.
DR   HOGENOM; CLU_069535_0_0_0; -.
DR   OMA; DRTYKQD; -.
DR   OrthoDB; 918580at2; -.
DR   Proteomes; UP000000592; Plasmid pTT27.
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; Plasmid.
FT   CHAIN           1..250
FT                   /note="5-oxoprolinase subunit A"
FT                   /id="PRO_0000185055"
SQ   SEQUENCE   250 AA;  26780 MW;  918934DBFE9D85EF CRC64;
     MKVDLNADAG ESYGAFAYGH DREIFPLVTS ANLACGFHGG SPGRILEAVR LAKAHGVAVG
     AHPGFPDLVG FGRREMALSP EEVYADVLYQ IGALSAFLKA EGLPLHHVKP HGALYLKACR
     DRETARAIAL AVKAFDPGLP LVVLPGTVYE EEARKAGLRV VLEAFPERAY LRNGQLAPRS
     MPGSWITDPE EAARRALRMV LEGKVEALDG GEVAVRAETL CIHGDNPNAP EVARAVREAL
     EQAGVEVRAF