GGT6_BOVIN
ID GGT6_BOVIN Reviewed; 490 AA.
AC A7YWM1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Glutathione hydrolase 6 {ECO:0000305};
DE EC=3.4.19.13 {ECO:0000250|UniProtKB:P19440};
DE AltName: Full=Gamma-glutamyltransferase 6;
DE Short=GGT 6;
DE EC=2.3.2.2 {ECO:0000250|UniProtKB:P19440};
DE AltName: Full=Gamma-glutamyltranspeptidase 6;
DE Contains:
DE RecName: Full=Glutathione hydrolase 6 heavy chain;
DE Contains:
DE RecName: Full=Glutathione hydrolase 6 light chain;
DE Flags: Precursor;
GN Name=GGT6 {ECO:0000250|UniProtKB:Q6P531};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Hydrolyzes and transfers gamma-glutamyl moieties from
CC glutathione and other gamma-glutamyl compounds to acceptors.
CC {ECO:0000250|UniProtKB:P19440}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an alpha-amino acid + an N-terminal (5-L-glutamyl)-[peptide] =
CC 5-L-glutamyl amino acid + N-terminal L-alpha-aminoacyl-[peptide];
CC Xref=Rhea:RHEA:23904, Rhea:RHEA-COMP:9780, Rhea:RHEA-COMP:9795,
CC ChEBI:CHEBI:77644, ChEBI:CHEBI:78597, ChEBI:CHEBI:78599,
CC ChEBI:CHEBI:78608; EC=2.3.2.2;
CC Evidence={ECO:0000250|UniProtKB:P19440};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23905;
CC Evidence={ECO:0000250|UniProtKB:P19440};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + H2O = L-cysteinylglycine + L-glutamate;
CC Xref=Rhea:RHEA:28807, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:61694; EC=3.4.19.13;
CC Evidence={ECO:0000250|UniProtKB:P19440};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28808;
CC Evidence={ECO:0000250|UniProtKB:P19440};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an S-substituted glutathione + H2O = an S-substituted L-
CC cysteinylglycine + L-glutamate; Xref=Rhea:RHEA:59468,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:90779,
CC ChEBI:CHEBI:143103; EC=3.4.19.13;
CC Evidence={ECO:0000250|UniProtKB:P19440};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59469;
CC Evidence={ECO:0000250|UniProtKB:P19440};
CC -!- PATHWAY: Sulfur metabolism; glutathione metabolism.
CC {ECO:0000250|UniProtKB:P19440}.
CC -!- SUBUNIT: Heterodimer composed of the light and heavy chains. The active
CC site is located in the light chain. {ECO:0000250|UniProtKB:P19440}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P19440}; Single-
CC pass type II membrane protein {ECO:0000250|UniProtKB:P07314}.
CC -!- PTM: Cleaved by autocatalysis into a large and a small subunit and the
CC autocatalytic cleavage is essential to the functional activation of the
CC enzyme. {ECO:0000250|UniProtKB:P19440}.
CC -!- SIMILARITY: Belongs to the gamma-glutamyltransferase family.
CC {ECO:0000305}.
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DR EMBL; BC134652; AAI34653.1; -; mRNA.
DR RefSeq; NP_001098904.1; NM_001105434.1.
DR AlphaFoldDB; A7YWM1; -.
DR SMR; A7YWM1; -.
DR STRING; 9913.ENSBTAP00000034988; -.
DR MEROPS; T03.024; -.
DR PaxDb; A7YWM1; -.
DR GeneID; 613919; -.
DR KEGG; bta:613919; -.
DR CTD; 124975; -.
DR eggNOG; KOG2410; Eukaryota.
DR HOGENOM; CLU_049993_0_0_1; -.
DR InParanoid; A7YWM1; -.
DR OrthoDB; 1209764at2759; -.
DR TreeFam; TF338758; -.
DR UniPathway; UPA00204; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0036374; F:glutathione hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0102953; F:hypoglycin A gamma-glutamyl transpeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0103068; F:leukotriene C4 gamma-glutamyl transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006750; P:glutathione biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.60.20.40; -; 1.
DR InterPro; IPR043137; GGT_ssub.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR SUPFAM; SSF56235; SSF56235; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Glutathione biosynthesis; Glycoprotein; Hydrolase;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix; Zymogen.
FT CHAIN 1..?
FT /note="Glutathione hydrolase 6 heavy chain"
FT /id="PRO_0000314952"
FT CHAIN ?..490
FT /note="Glutathione hydrolase 6 light chain"
FT /id="PRO_0000314953"
FT TOPO_DOM 1..52
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P07314"
FT TRANSMEM 53..73
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..490
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P07314"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 374
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 490 AA; 49626 MW; 52764AEA59A4D50A CRC64;
MEPEAGPVLY QKLRVWEPSL ESEEEEEEIS EQLILDASGP HDSSGNKAGR LPGAWAQLVA
ALLLLAIGFS LAVRQLCSSG ASPGALGSGA PPASGHSHRP GVYHHGAIIS PAAECSRLGR
ELFVAGGNIV DAGVGAALCL AVVHPHTTGL GATYWGLFHN SSSGNSTALT SGPAQTLAPG
LGLPSALPAL HMLHTHFGRL PWPHLLVGPI SLAQKGFLVD TSLASALAAQ DTKGLCPLLC
HANGTPLGPG TQVTNTKLAA VLHKASLAPT PDLSGDALLS LLAEDLGLEG PSVGPRPTLE
PALQLPLPQG ILFTTPSPSA GPELLELLEA SLQSAGPSPA PCPALPQAAA APRSSVLATV
DSSGSVLLLT SSLNSSFGSG HLSPSTGVLL SNLVAESAAG AWACPLIFRD ISDDTEVDVL
GLVASGTPAA ARVMTHALLS HLARPQTPDQ QGPTESPRAC AQGTLLQVAA HTEHAHVSSV
PSGCCPFQGF
