(data stored in ACNUC6288 zone)

SWISSPROT: Q6BMF2_DEBHA

ID   Q6BMF2_DEBHA            Unreviewed;       261 AA.
AC   Q6BMF2;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   08-MAY-2019, entry version 77.
DE   RecName: Full=Gamma-glutamylcyclotransferase {ECO:0000256|RuleBase:RU363081};
DE            EC=4.3.2.- {ECO:0000256|RuleBase:RU363081};
GN   OrderedLocusNames=DEHA2F05962g {ECO:0000313|EMBL:CAG88946.1};
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC
OS   0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG88946.1, ECO:0000313|Proteomes:UP000000599};
RN   [1] {ECO:0000313|EMBL:CAG88946.1, ECO:0000313|Proteomes:UP000000599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968
RC   {ECO:0000313|Proteomes:UP000000599};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.F., Straub M.L., Suleau A.,
RA   Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR382138; CAG88946.1; -; Genomic_DNA.
DR   RefSeq; XP_460619.1; XM_460619.1.
DR   STRING; 4959.XP_460619.1; -.
DR   EnsemblFungi; CAG88946; CAG88946; DEHA2F05962g.
DR   GeneID; 2903395; -.
DR   KEGG; dha:DEHA2F05962g; -.
DR   HOGENOM; HOG000264264; -.
DR   InParanoid; Q6BMF2; -.
DR   KO; K07232; -.
DR   OMA; HYAPFHP; -.
DR   OrthoDB; 1238273at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
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   PANTHER; PTHR12192; PTHR12192; 1.
DR   Pfam; PF04752; ChaC; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6BMF2.
DR   SWISS-2DPAGE; Q6BMF2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000599};
KW   Lyase {ECO:0000256|RuleBase:RU363081};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000599}.
SQ   SEQUENCE   261 AA;  29869 MW;  10FDF97C5E0415E4 CRC64;
     MTNNEIPKPS GEGMWVIGYG SLIFKPLPYY QFKVSGYLKG FIRRFWQSSS DHRGTPEAPG
     RVVTLVSLDD LKKNRKFHND IHMYEAGDKY QETDLLSRTN SSADLGKEDI HDITHNISKL
     EEDDLKVWGC AYYVGPDDVA KVKDYLDIRE KNGYTTHKVP FHVLNVCDDS ENAKEVMQNI
     PKNKNGDYII ESLIYIGTTD NVSFVGPEDI EKTGEKIRTS RGPSGENSEY LIELCKAVRH
     LDDEGRSRDY YLEDLVKFVE L
//

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