(data stored in SCRATCH zone)

SWISSPROT: B6HGE8_PENRW

ID   B6HGE8_PENRW            Unreviewed;       264 AA.
AC   B6HGE8;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   05-JUL-2017, entry version 48.
DE   RecName: Full=Gamma-glutamylcyclotransferase {ECO:0000256|RuleBase:RU363081};
DE            EC=2.3.2.- {ECO:0000256|RuleBase:RU363081};
GN   ORFNames=Pc20g03500 {ECO:0000313|EMBL:CAP85679.1}, PCH_Pc20g03500
GN   {ECO:0000313|EMBL:CAP85679.1};
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 /
OS   Wisconsin 54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP85679.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP85679.1, ECO:0000313|Proteomes:UP000000724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC   {ECO:0000313|Proteomes:UP000000724};
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A.,
RA   van der Klei I.J., van Peij N.N.M.E., Veenhuis M., von Doehren H.,
RA   Wagner C., Wortman J.R., Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
CC   -!- FUNCTION: Catalyzes the cleavage glutathione into 5-oxoproline and
CC       a Cys-Gly dipeptide. Acts specifically on glutathione, but not on
CC       other gamma-glutamyl peptides. {ECO:0000256|RuleBase:RU363081}.
CC   -!- CATALYTIC ACTIVITY: Glutathione = 5-oxoproline + cysteinylglycine.
CC       {ECO:0000256|RuleBase:RU363081}.
CC   -!- SIMILARITY: Belongs to the gamma-glutamylcyclotransferase family.
CC       {ECO:0000256|RuleBase:RU363081}.
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DR   EMBL; AM920435; CAP85679.1; -; Genomic_DNA.
DR   RefSeq; XP_002562901.1; XM_002562855.1.
DR   EnsemblFungi; CAP85679; CAP85679; PCH_Pc20g03500.
DR   GeneID; 8309955; -.
DR   KEGG; pcs:Pc20g03500; -.
DR   eggNOG; KOG3182; Eukaryota.
DR   eggNOG; COG3703; LUCA.
DR   HOGENOM; HOG000264264; -.
DR   OMA; DFPYEEK; -.
DR   OrthoDB; EOG092C4Q9H; -.
DR   BioCyc; PCHR:PC20G03500-MONOMER; -.
DR   Proteomes; UP000000724; Contig Pc00c20.
DR   GO; GO:0003839; F:gamma-glutamylcyclotransferase activity; IEA:InterPro.
DR   GO; GO:0006751; P:glutathione catabolic process; IEA:InterPro.
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.
DR   SUPFAM; SSF110857; SSF110857; 1.
PE   3: Inferred from homology;
DR   PRODOM; B6HGE8.
DR   SWISS-2DPAGE; B6HGE8.
KW   Acyltransferase {ECO:0000256|RuleBase:RU363081};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000724};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000724};
KW   Transferase {ECO:0000256|RuleBase:RU363081}.
FT   COILED      218    248       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   264 AA;  29342 MW;  A6A16ED2983C5F54 CRC64;
     MAAIAQGHKV HPDGRTWKSH FPKGDLWVFG YGSLIWKPPP HYDQRIPGYI SGYVRRFWQA
     STDHRGTPEQ PGRVVTVIER TFWETLDDPI AHLESELSST GKVWGAAYHI PASHAEEVHD
     YLDEREIDGY SAHYTPFHPT VDVEGAGDST GSSPIICMVY IGQPTNPQFL RDAAHREPQH
     VAQVISAGHG LSGKGSEYLF MLEKGLEGLG LGTADVHVTD LVKRVKAIEA ELAEAEEEEA
     EIKVTRSLEI PAEEVDRDGR ETIE
//

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