ID F1A1W6_DICPU Unreviewed; 262 AA.
AC F1A1W6;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=Gamma-glutamylcyclotransferase {ECO:0000256|RuleBase:RU363081};
DE EC=4.3.2.7 {ECO:0000256|RuleBase:RU363081};
GN ORFNames=DICPUDRAFT_99725 {ECO:0000313|EMBL:EGC29811.1};
OS Dictyostelium purpureum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC29811.1, ECO:0000313|Proteomes:UP000001064};
RN [1] {ECO:0000313|Proteomes:UP000001064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QSDP1 {ECO:0000313|Proteomes:UP000001064};
RX PubMed=21356102; DOI=10.1186/gb-2011-12-2-r20;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Sucgang R., Kuo A., Tian X., Salerno W., Parikh A., Feasley C.L., Dalin E.,
RA Tu H., Huang E., Barry K., Lindquist E., Shapiro H., Bruce D., Schmutz J.,
RA Salamov A., Fey P., Gaudet P., Anjard C., Babu M.M., Basu S.,
RA Bushmanova Y., van der Wel H., Katoh-Kurasawa M., Dinh C., Coutinho P.M.,
RA Saito T., Elias M., Schaap P., Kay R.R., Henrissat B., Eichinger L.,
RA Rivero F., Putnam N.H., West C.M., Loomis W.F., Chisholm R.L., Shaulsky G.,
RA Strassmann J.E., Queller D.C., Kuspa A., Grigoriev I.V.;
RT "Comparative genomics of the social amoebae Dictyostelium discoideum and
RT Dictyostelium purpureum.";
RL Genome Biol. 12:R20.1-R20.23(2011).
CC -!- FUNCTION: Catalyzes the cleavage of glutathione into 5-oxo-L-proline
CC and a Cys-Gly dipeptide. Acts specifically on glutathione, but not on
CC other gamma-glutamyl peptides. {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; GL871389; EGC29811.1; -; Genomic_DNA.
DR RefSeq; XP_003293659.1; XM_003293611.1.
DR AlphaFoldDB; F1A1W6; -.
DR STRING; 5786.F1A1W6; -.
DR EnsemblProtists; EGC29811; EGC29811; DICPUDRAFT_99725.
DR GeneID; 10504975; -.
DR KEGG; dpp:DICPUDRAFT_99725; -.
DR eggNOG; KOG3182; Eukaryota.
DR InParanoid; F1A1W6; -.
DR OMA; MCEDMFV; -.
DR OrthoDB; 5472321at2759; -.
DR Proteomes; UP000001064; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0003839; F:gamma-glutamylcyclotransferase activity; IBA:GO_Central.
DR GO; GO:0061928; F:glutathione specific gamma-glutamylcyclotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0006751; P:glutathione catabolic process; IBA:GO_Central.
DR CDD; cd06661; GGCT_like; 1.
DR CDD; cd21157; PUA_G5K; 1.
DR Gene3D; 3.10.490.10; Gamma-glutamyl cyclotransferase-like; 1.
DR Gene3D; 2.30.130.10; PUA domain; 1.
DR InterPro; IPR006840; ChaC.
DR InterPro; IPR013024; GGCT-like.
DR InterPro; IPR036568; GGCT-like_sf.
DR InterPro; IPR002478; PUA.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR036974; PUA_sf.
DR PANTHER; PTHR12192; CATION TRANSPORT PROTEIN CHAC-RELATED; 1.
DR PANTHER; PTHR12192:SF2; GLUTATHIONE-SPECIFIC GAMMA-GLUTAMYLCYCLOTRANSFERASE 2; 1.
DR Pfam; PF04752; ChaC; 1.
DR Pfam; PF01472; PUA; 1.
DR SMART; SM00359; PUA; 1.
DR SUPFAM; SSF110857; Gamma-glutamyl cyclotransferase-like; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR PROSITE; PS50890; PUA; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|RuleBase:RU363081};
KW Reference proteome {ECO:0000313|Proteomes:UP000001064}.
FT DOMAIN 171..243
FT /note="PUA"
FT /evidence="ECO:0000259|SMART:SM00359"
SQ SEQUENCE 262 AA; 29601 MW; 496EDC005B9A489A CRC64;
MCEDMFVYLF GYGSLIWRPG FPYSKKFNAF IKGYKRMFVT KSRDHRGTEE LPGRVVTLVK
KPEDDPSDEE WIAWGTVYSI ADDVAQPILK NLDYREKGGY ERHELDVFLA EGEESYGKAI
VYLVSPDNID YVSENETTST IADTIFRSVG ASDKSLELLN RHKRFYAKPL GQIWVDDGAV
QAISQRAKSL LPVGIIKMVG DFSKNSLVSI LDANSNPISR GITNYSSNEI LNIIGKQSKD
YFNTLDGYTN EAVIDHNNLI LL
//
