(data stored in SCRATCH zone)

SWISSPROT: C0ZPT0_RHOE4

ID   C0ZPT0_RHOE4            Unreviewed;       253 AA.
AC   C0ZPT0;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   08-MAY-2019, entry version 55.
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=RER_07000 {ECO:0000313|EMBL:BAH31408.1};
OS   Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=234621 {ECO:0000313|EMBL:BAH31408.1, ECO:0000313|Proteomes:UP000002204};
RN   [1] {ECO:0000313|Proteomes:UP000002204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BAH31408.1, ECO:0000313|Proteomes:UP000002204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RX   PubMed=16423019; DOI=10.1111/j.1462-2920.2005.00899.x;
RA   Sekine M., Tanikawa S., Omata S., Saito M., Fujisawa T., Tsukatani N.,
RA   Tajima T., Sekigawa T., Kosugi H., Matsuo Y., Nishiko R., Imamura K.,
RA   Ito M., Narita H., Tago S., Fujita N., Harayama S.;
RT   "Sequence analysis of three plasmids harboured in Rhodococcus
RT   erythropolis strain PR4.";
RL   Environ. Microbiol. 8:334-346(2006).
CC   -!- FUNCTION: Catalyzes the cleavage of 5-oxoproline to form L-
CC       glutamate coupled to the hydrolysis of ATP to ADP and inorganic
CC       phosphate. {ECO:0000256|HAMAP-Rule:MF_00691,
CC       ECO:0000256|SAAS:SAAS01054855}.
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;
CC         EC=3.5.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_00691,
CC         ECO:0000256|SAAS:SAAS01122520};
CC   -!- SUBUNIT: Forms a complex composed of PxpA, PxpB and PxpC.
CC       {ECO:0000256|HAMAP-Rule:MF_00691, ECO:0000256|SAAS:SAAS01054844}.
CC   -!- SIMILARITY: Belongs to the LamB/PxpA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00691, ECO:0000256|SAAS:SAAS01054853}.
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DR   EMBL; AP008957; BAH31408.1; -; Genomic_DNA.
DR   RefSeq; WP_020906114.1; NC_012490.1.
DR   STRING; 234621.RER_07000; -.
DR   EnsemblBacteria; BAH31408; BAH31408; RER_07000.
DR   KEGG; rer:RER_07000; -.
DR   PATRIC; fig|234621.6.peg.1148; -.
DR   eggNOG; ENOG4105E7W; Bacteria.
DR   eggNOG; COG1540; LUCA.
DR   HOGENOM; HOG000237330; -.
DR   KO; K07160; -.
DR   OMA; VNIACGF; -.
DR   BioCyc; RERY234621:GHDE-717-MONOMER; -.
DR   Proteomes; UP000002204; 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   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;
DR   PRODOM; C0ZPT0.
DR   SWISS-2DPAGE; C0ZPT0.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00691,
KW   ECO:0000256|SAAS:SAAS01054845};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002204};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00691,
KW   ECO:0000256|SAAS:SAAS01090513};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00691,
KW   ECO:0000256|SAAS:SAAS01054854}.
SQ   SEQUENCE   253 AA;  26525 MW;  4317457A1AA53CAB CRC64;
     MGYSVDLNSD LGEGFGAWTL GDDDAMLELV TSANIACGFH AGDPTTLLAT CESAATRGVR
     IGAQVGYRDL AGFGRRFIDM SPKDLTADVI YQIGALDGLA RVAGSRVTYV KPHGALYNAI
     VHHRRQARAV VAAVVAYDSS LPVLGLPGSV FLEEAREAGL DVVAEAFADR AYTAEGTLVP
     RTESGAVLND PALVAERVRR MVVDGELDAV DGSTLKITAE SVCVHGDSPA AVDMAAAIRD
     LLESSDVEIT PFT
//

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