CHAC_SCHPO
ID CHAC_SCHPO Reviewed; 203 AA.
AC P87305;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Glutathione-specific gamma-glutamylcyclotransferase {ECO:0000250|UniProtKB:P32656};
DE Short=Gamma-GCG {ECO:0000250|UniProtKB:P32656};
DE EC=4.3.2.7 {ECO:0000250|UniProtKB:P32656};
GN ORFNames=SPBC31F10.03 {ECO:0000312|PomBase:SPBC31F10.03};
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Gamma-glutamylcyclotransferase acting specifically on
CC glutathione, but not on other gamma-glutamyl peptides. Allows
CC utilization of gluthathione through subsequent cleavage of the Cys-Gly
CC dipeptide by Cys-Gly metallodipeptidase dug1.
CC {ECO:0000250|UniProtKB:P32656}.
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:0000250|UniProtKB:P32656};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the gamma-glutamylcyclotransferase family. ChaC
CC subfamily. {ECO:0000305}.
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DR EMBL; CU329671; CAB10080.1; -; Genomic_DNA.
DR PIR; T40206; T40206.
DR RefSeq; NP_596565.1; NM_001022486.2.
DR AlphaFoldDB; P87305; -.
DR SMR; P87305; -.
DR BioGRID; 276901; 13.
DR STRING; 4896.SPBC31F10.03.1; -.
DR MaxQB; P87305; -.
DR PaxDb; P87305; -.
DR EnsemblFungi; SPBC31F10.03.1; SPBC31F10.03.1:pep; SPBC31F10.03.
DR GeneID; 2540372; -.
DR KEGG; spo:SPBC31F10.03; -.
DR PomBase; SPBC31F10.03; -.
DR VEuPathDB; FungiDB:SPBC31F10.03; -.
DR eggNOG; KOG3182; Eukaryota.
DR HOGENOM; CLU_070703_0_1_1; -.
DR InParanoid; P87305; -.
DR OMA; LLWYTDF; -.
DR PhylomeDB; P87305; -.
DR Reactome; R-SPO-174403; Glutathione synthesis and recycling.
DR PRO; PR:P87305; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0003839; F:gamma-glutamylcyclotransferase activity; IBA:GO_Central.
DR GO; GO:0016603; F:glutaminyl-peptide cyclotransferase activity; ISS:PomBase.
DR GO; GO:0061928; F:glutathione specific gamma-glutamylcyclotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:1990748; P:cellular detoxification; NAS:PomBase.
DR GO; GO:0006751; P:glutathione catabolic process; IBA:GO_Central.
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;
KW Cytoplasm; Lyase; Nucleus; Reference proteome.
FT CHAIN 1..203
FT /note="Glutathione-specific gamma-glutamylcyclotransferase"
FT /id="PRO_0000339309"
FT ACT_SITE 105
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:O75223"
FT BINDING 12..17
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O75223"
SQ SEQUENCE 203 AA; 23568 MW; 5187F87566FBDD0C CRC64;
MKTLSPEGSL WVFGYGSLIW HPPPHYDYSI PCFIKGYVRR FWMRSEDHRG TVNSPGLVLT
LIPYEEWKQF SDWSFTPFDE GCWGMAFRIP AKYATQVREY LDDREVNGYT AHSVPVYAHT
GDEIPVLENC LVYVGTSKSP QFQPSDDLTQ MAKIISTRRG KSGDNFVYLF ELAKCLRHLS
PESKDIHVFE LEAEVRKQMQ KTR