UniProt: A0A1S3NKT5

Database: UniProt
Entry: A0A1S3NKT5_SALSA

LinkDB:  A0A1S3NKT5_SALSA 
Original site:  A0A1S3NKT5_SALSA

All links

Ontology (4)   
   GO (4)   
Chemical reaction (2)   
   KEGG ENZYME (2)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
Protein domain (6)   
   InterPro (4)   
   Pfam (1)   
   PROSITE (1)   
All databases (15)   

Download RDF

ID   A0A1S3NKT5_SALSA        Unreviewed;       574 AA.
AC   A0A1S3NKT5;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Glutathione hydrolase {ECO:0000256|RuleBase:RU368068};
DE            EC=2.3.2.2 {ECO:0000256|RuleBase:RU368068};
DE            EC=3.4.19.13 {ECO:0000256|RuleBase:RU368068};
DE   AltName: Full=Gamma-glutamyltransferase {ECO:0000256|RuleBase:RU368068};
DE   AltName: Full=Gamma-glutamyltranspeptidase {ECO:0000256|RuleBase:RU368068};
GN   Name=LOC106579933 {ECO:0000313|RefSeq:XP_014015811.1};
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014015811.1};
RN   [1] {ECO:0000313|RefSeq:XP_014015811.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_014015811.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Cleaves the gamma-glutamyl peptide bond of glutathione and
CC       glutathione conjugates. {ECO:0000256|RuleBase:RU368068}.
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:0000256|RuleBase:RU368068};
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:0000256|RuleBase:RU368068};
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:0000256|RuleBase:RU368068};
CC   -!- PATHWAY: Sulfur metabolism; glutathione metabolism.
CC       {ECO:0000256|RuleBase:RU368068}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU368068}; Single-
CC       pass type II membrane protein {ECO:0000256|RuleBase:RU368068}.
CC   -!- SIMILARITY: Belongs to the gamma-glutamyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00009381}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   RefSeq; XP_014015811.1; XM_014160336.1.
DR   AlphaFoldDB; A0A1S3NKT5; -.
DR   STRING; 8030.ENSSSAP00000013493; -.
DR   PaxDb; 8030-ENSSSAP00000013493; -.
DR   GeneID; 106579933; -.
DR   KEGG; sasa:106579933; -.
DR   OrthoDB; 2910309at2759; -.
DR   UniPathway; UPA00204; -.
DR   Proteomes; UP000087266; Chromosome ssa20.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0036374; F:glutathione hydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006751; P:glutathione catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.246.130; -; 1.
DR   Gene3D; 3.60.20.40; -; 1.
DR   InterPro; IPR043138; GGT_lsub_C.
DR   InterPro; IPR000101; GGT_peptidase.
DR   InterPro; IPR043137; GGT_ssub.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   NCBIfam; TIGR00066; g_glut_trans; 1.
DR   PANTHER; PTHR11686; GAMMA GLUTAMYL TRANSPEPTIDASE; 1.
DR   PANTHER; PTHR11686:SF56; GLUTATHIONE HYDROLASE 1 PROENZYME-RELATED; 1.
DR   Pfam; PF01019; G_glu_transpept; 1.
DR   PRINTS; PR01210; GGTRANSPTASE.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR   PROSITE; PS00462; G_GLU_TRANSPEPTIDASE; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU368068};
KW   Hydrolase {ECO:0000256|RuleBase:RU368068};
KW   Membrane {ECO:0000256|RuleBase:RU368068};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW   Transferase {ECO:0000256|RuleBase:RU368068};
KW   Transmembrane {ECO:0000256|RuleBase:RU368068};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU368068}.
FT   TRANSMEM        7..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU368068"
FT   ACT_SITE        386
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600101-1"
SQ   SEQUENCE   574 AA;  62528 MW;  55212E72DC7015AF CRC64;
     MVRKSLVAGL VFLLVAAVGV FVGVFMGVGN KNPISPSDHF YSKAAVATDA GICSEVGRDI
     LKRNGSAVDA SIAALLCVGL LNAHSMGIGG GLFFNIYNAS TGKVETIDAR ETAPMNATED
     MFGDNTQLSQ KGGLSIAIPG EIRGYEMAHR RHGRLPWKEL FEPSIELARV GFRIGKALAK
     AIASNKDAIQ GDANMCEVFC DSQKKILKEN DIIKFPKLAD TYRRIAEEGP DVFYNGTMAQ
     TIVDDIQAAG GIITLEDLLD YRPVLNENPL KLTVGEYTMH VPDAPSSGPV LALILNIVDG
     YNFTCSSVST AEKKTLTYHR IVEAFRFAYA KRSKLGDPRY LNITDLIHNM TSDYFADGIR
     SKITDDTTHP DSYYEPDYFV KDNHGTAHLS VIAEDGSAVA ATSTINNYFG SKVMSQSTGI
     IFNDEMDDFS SPYINNGFGI PPSPNNFIQP GKRPLSSMCP TIISDKDNRV KMVVGASGGT
     KITTATALVI LNTLFFDYDL KKAVTLPRIH NQLNPSMTVV EDGFEKSVLD GLEKKNHVRT
     RPLYNDSVVQ AVVRQGERLC AESDHRKGGY PAGY
//

DBGET integrated database retrieval system