ID   PXPA_THET8              Reviewed;         250 AA.
AC   Q53WG6;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, 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=TTHB195;
OS   Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OG   Plasmid pTT27.
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=300852;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27634 / DSM 579 / HB8;
RA   Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA   Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT   "Complete genome sequence of Thermus thermophilus HB8.";
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RG   RIKEN structural genomics initiative (RSGI);
RT   "Crystal structure of lactam utilization protein from Thermus thermophilus
RT   HB8.";
RL   Submitted (AUG-2006) to the PDB data bank.
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; AP008227; BAD71991.1; -; Genomic_DNA.
DR   RefSeq; WP_011229109.1; NC_006462.1.
DR   RefSeq; YP_145434.1; NC_006462.1.
DR   PDB; 2DFA; X-ray; 1.90 A; A=1-250.
DR   PDBsum; 2DFA; -.
DR   AlphaFoldDB; Q53WG6; -.
DR   SMR; Q53WG6; -.
DR   EnsemblBacteria; BAD71991; BAD71991; BAD71991.
DR   GeneID; 3169274; -.
DR   KEGG; ttj:TTHB195; -.
DR   PATRIC; fig|300852.9.peg.2147; -.
DR   HOGENOM; CLU_069535_0_0_0; -.
DR   OMA; DRTYKQD; -.
DR   PhylomeDB; Q53WG6; -.
DR   EvolutionaryTrace; Q53WG6; -.
DR   Proteomes; UP000000532; 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   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Hydrolase; Nucleotide-binding; Plasmid;
KW   Reference proteome.
FT   CHAIN           1..250
FT                   /note="5-oxoprolinase subunit A"
FT                   /id="PRO_0000185056"
FT   STRAND          2..9
FT                   /evidence="ECO:0007829|PDB:2DFA"
FT   HELIX           21..24
FT                   /evidence="ECO:0007829|PDB:2DFA"
FT   TURN            25..27
FT                   /evidence="ECO:0007829|PDB:2DFA"
FT   STRAND          29..34
FT                   /evidence="ECO:0007829|PDB:2DFA"
FT   STRAND          36..39
FT                   /evidence="ECO:0007829|PDB:2DFA"
FT   HELIX           42..54
FT                   /evidence="ECO:0007829|PDB:2DFA"
FT   STRAND          58..62
FT                   /evidence="ECO:0007829|PDB:2DFA"
FT   TURN            68..72
FT                   /evidence="ECO:0007829|PDB:2DFA"
FT   HELIX           80..100
FT                   /evidence="ECO:0007829|PDB:2DFA"
FT   HELIX           112..120
FT                   /evidence="ECO:0007829|PDB:2DFA"
FT   HELIX           122..135
FT                   /evidence="ECO:0007829|PDB:2DFA"
FT   STRAND          141..143
FT                   /evidence="ECO:0007829|PDB:2DFA"
FT   HELIX           148..155
FT                   /evidence="ECO:0007829|PDB:2DFA"
FT   STRAND          160..164
FT                   /evidence="ECO:0007829|PDB:2DFA"
FT   STRAND          174..176
FT                   /evidence="ECO:0007829|PDB:2DFA"
FT   HELIX           189..201
FT                   /evidence="ECO:0007829|PDB:2DFA"
FT   STRAND          203..207
FT                   /evidence="ECO:0007829|PDB:2DFA"
FT   STRAND          210..214
FT                   /evidence="ECO:0007829|PDB:2DFA"
FT   STRAND          218..222
FT                   /evidence="ECO:0007829|PDB:2DFA"
FT   HELIX           229..241
FT                   /evidence="ECO:0007829|PDB:2DFA"
FT   TURN            242..244
FT                   /evidence="ECO:0007829|PDB:2DFA"
SQ   SEQUENCE   250 AA;  26725 MW;  EAD787FFC4C5D597 CRC64;
     MKVDLNADAG ESYGAFAYGH DREIFPLVSS ANLACGFHGG SPGRILEAVR LAKAHGVAVG
     AHPGFPDLVG FGRREMALSP EEVYADVLYQ IGALSAFLKA EGLPLHHVKP HGALYLKACR
     DRETARAIAL AVKAFDPGLP LVVLPGTVYE EEARKAGLRV VLEAFPERAY LRSGQLAPRS
     MPGSWITDPE EAARRALRMV LEGKVEALDG GEVAVRADTL CIHGDNPNAP EVARAVREAL
     EQAGVEVRAF