ID A0A091UB21_PHALP Unreviewed; 610 AA.
AC A0A091UB21;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 24.
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};
DE Flags: Fragment;
GN ORFNames=N335_07355 {ECO:0000313|EMBL:KFQ71223.1};
OS Phaethon lepturus (White-tailed tropicbird).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Eurypygimorphae; Phaethontiformes;
OC Phaethontidae; Phaethon.
OX NCBI_TaxID=97097 {ECO:0000313|EMBL:KFQ71223.1, ECO:0000313|Proteomes:UP000053638};
RN [1] {ECO:0000313|EMBL:KFQ71223.1, ECO:0000313|Proteomes:UP000053638}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N335 {ECO:0000313|EMBL:KFQ71223.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00005115, 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}.
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DR EMBL; KK444427; KFQ71223.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091UB21; -.
DR PhylomeDB; A0A091UB21; -.
DR UniPathway; UPA00204; -.
DR Proteomes; UP000053638; Unassembled WGS sequence.
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 PANTHER; PTHR11686; GAMMA GLUTAMYL TRANSPEPTIDASE; 1.
DR PANTHER; PTHR11686:SF9; GLUTATHIONE HYDROLASE 7; 1.
DR Pfam; PF01019; G_glu_transpept; 1.
DR PRINTS; PR01210; GGTRANSPTASE.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU368068}; Hydrolase {ECO:0000256|RuleBase:RU368068};
KW Membrane {ECO:0000256|RuleBase:RU368068};
KW Reference proteome {ECO:0000313|Proteomes:UP000053638};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368068};
KW Transmembrane {ECO:0000256|RuleBase:RU368068};
KW Transmembrane helix {ECO:0000256|RuleBase:RU368068}.
FT TRANSMEM 55..79
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368068"
FT REGION 19..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ71223.1"
FT NON_TER 610
FT /evidence="ECO:0000313|EMBL:KFQ71223.1"
SQ SEQUENCE 610 AA; 65568 MW; 61DCE1E9F2741CF1 CRC64;
FLPAAHKDPD SFLKSARLQR LPSSSSEMGS QDVSPLRETS KDPFSGDCSC RQDGLTVIIT
ACLTFATGVT VALIMQIYFG DPQIFHRGAV VTDAARCTAL GIEVLNKQGS SVDAAIASAL
CAGVVNPHTS GIGGGGVMLV HDIRKNRSWV IDFREVAPLG IPLEGDLQKD TKPGLLVGVP
GMIQGMHQAH QLHGRRTVAP APRHVPAPWL FCMSFPFSPA AKAISELKAL NYSDRFREIF
LPDGQPLLPG MFVRRLDLAA VLELVGAEGV SAFYSGNLTQ EIISEVHNYG GVLVEEDFSN
YSVTVENPVH TVYRGHLVFS PPPPHAGPAL ITALNILEGF NITSQVSKGN ILHWMAETLK
IALSLASNLG DPSDDVSVTH AAEGMVSKSE ATSLRQLIND SQSFSSDLHM PHFSVESGPA
ASQVLVMGPD DFIVAVVSSL NRPFGSGIIT PSGVLLNSQM LDFSWQNKTM NHSIPRPQNL
IQPRKRPLSF LLPTIVRPSE GMCGTYLCLG ANNGDKALSS IVQVLVNVLT LNKNLSESLS
LGRLHPQLQS NTLQVDSEFP EEDIEFLVAR GHQVDKVKVV SLVHGARRTN SFIIGLKDPR
SVDAAGATIL
//
