(data stored in SCRATCH zone)

SWISSPROT: A1AYP7_PARDP

ID   A1AYP7_PARDP            Unreviewed;       246 AA.
AC   A1AYP7;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   08-MAY-2019, entry version 69.
DE   RecName: Full=Gamma-glutamylcyclotransferase {ECO:0000256|RuleBase:RU363081};
DE            EC=4.3.2.- {ECO:0000256|RuleBase:RU363081};
GN   OrderedLocusNames=Pden_0277 {ECO:0000313|EMBL:ABL68391.1};
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL68391.1, ECO:0000313|Proteomes:UP000000361};
RN   [1] {ECO:0000313|Proteomes:UP000000361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222 {ECO:0000313|Proteomes:UP000000361};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J.,
RA   van Spanning R.J.M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans
RT   PD1222.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the cleavage of glutathione into 5-oxo-L-
CC       proline and a Cys-Gly dipeptide. Acts specifically on glutathione,
CC       but not on other gamma-glutamyl peptides.
CC       {ECO:0000256|RuleBase:RU363081}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glutathione = 5-oxo-L-proline + L-cysteinylglycine;
CC         Xref=Rhea:RHEA:47724, ChEBI:CHEBI:57925, ChEBI:CHEBI:58402,
CC         ChEBI:CHEBI:61694; EC=4.3.2.7;
CC         Evidence={ECO:0000256|RuleBase:RU363081};
CC   -!- SIMILARITY: Belongs to the gamma-glutamylcyclotransferase family.
CC       {ECO:0000256|RuleBase:RU363081}.
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DR   EMBL; CP000489; ABL68391.1; -; Genomic_DNA.
DR   PRIDE; A1AYP7; -.
DR   EnsemblBacteria; ABL68391; ABL68391; Pden_0277.
DR   KEGG; pde:Pden_0277; -.
DR   eggNOG; ENOG4108NH8; Bacteria.
DR   eggNOG; COG3703; LUCA.
DR   HOGENOM; HOG000264265; -.
DR   KO; K07232; -.
DR   OMA; PRYAGKL; -.
DR   Proteomes; UP000000361; Chromosome 1.
DR   GO; GO:0003839; F:gamma-glutamylcyclotransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0061928; F:glutathione specific gamma-glutamylcyclotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006751; P:glutathione catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd06661; GGCT_like; 1.
DR   InterPro; IPR006840; ChaC.
DR   InterPro; IPR013024; GGCT-like.
DR   InterPro; IPR036568; GGCT-like_sf.
DR   PANTHER; PTHR12192; PTHR12192; 1.
DR   Pfam; PF04752; ChaC; 1.
DR   SUPFAM; SSF110857; SSF110857; 1.
PE   3: Inferred from homology;
DR   PRODOM; A1AYP7.
DR   SWISS-2DPAGE; A1AYP7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000361};
KW   Lyase {ECO:0000256|RuleBase:RU363081};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000361}.
SQ   SEQUENCE   246 AA;  26899 MW;  5BCF92A3D81A52F7 CRC64;
     MELSPPAGNL MSNCRPIVLS DDHVARVASA EEGLLHDPRW RMLEDADLDL LADRLTRGRP
     RPIPVFAYGS LIWNPGFAVG GRRRATAIGW HRRFSISLDH FRGTPERPGL MLALASGGSC
     EGLVLDIAEG TEAQSLRAIL RRELVAHELS ANACWIEVET DRGREDALTF YADPVGTQLA
     ELTVQEQAQR LARAAGAAGS GAEYLLRTAR GLAEIGIHDD YIWTLQQLVA EEIDAGTAEP
     EERPSE
//

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