ID A0A210RVD8_9BURK Unreviewed; 532 AA.
AC A0A210RVD8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 08-NOV-2023, entry version 22.
DE RecName: Full=Glutathione hydrolase proenzyme {ECO:0000256|RuleBase:RU368036};
DE EC=2.3.2.2 {ECO:0000256|RuleBase:RU368036};
DE EC=3.4.19.13 {ECO:0000256|RuleBase:RU368036};
DE Contains:
DE RecName: Full=Glutathione hydrolase large chain {ECO:0000256|RuleBase:RU368036};
DE Contains:
DE RecName: Full=Glutathione hydrolase small chain {ECO:0000256|RuleBase:RU368036};
GN ORFNames=B6A14_09900 {ECO:0000313|EMBL:OWF64975.1};
OS Polynucleobacter hirudinilacicola.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Polynucleobacter.
OX NCBI_TaxID=1743166 {ECO:0000313|EMBL:OWF64975.1, ECO:0000313|Proteomes:UP000196880};
RN [1] {ECO:0000313|EMBL:OWF64975.1, ECO:0000313|Proteomes:UP000196880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MWH-EgelM1-30-B4 {ECO:0000313|EMBL:OWF64975.1,
RC ECO:0000313|Proteomes:UP000196880};
RA Hahn M.W.;
RT "New species Polynucleobacter sp. MWH-EgelM1-30-B4.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00001049,
CC ECO:0000256|RuleBase:RU368036};
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|ARBA:ARBA00000250,
CC ECO:0000256|RuleBase:RU368036};
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|ARBA:ARBA00001089,
CC ECO:0000256|RuleBase:RU368036};
CC -!- PATHWAY: Sulfur metabolism; glutathione metabolism.
CC {ECO:0000256|RuleBase:RU368036}.
CC -!- SUBUNIT: This enzyme consists of two polypeptide chains, which are
CC synthesized in precursor form from a single polypeptide.
CC {ECO:0000256|RuleBase:RU368036}.
CC -!- PTM: Cleaved by autocatalysis into a large and a small subunit.
CC {ECO:0000256|RuleBase:RU368036}.
CC -!- SIMILARITY: Belongs to the gamma-glutamyltransferase family.
CC {ECO:0000256|RuleBase:RU368036}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OWF64975.1}.
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DR EMBL; NAIA01000004; OWF64975.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A210RVD8; -.
DR OrthoDB; 5297205at2; -.
DR UniPathway; UPA00204; -.
DR Proteomes; UP000196880; Unassembled WGS sequence.
DR GO; GO:0036374; F:glutathione hydrolase activity; IEA:UniProtKB-UniRule.
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 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; PTHR43881:SF5; GAMMA-GLUTAMYLTRANSPEPTIDASE; 1.
DR PANTHER; PTHR43881; GAMMA-GLUTAMYLTRANSPEPTIDASE (AFU_ORTHOLOGUE AFUA_4G13580); 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|RuleBase:RU368036};
KW Glutathione biosynthesis {ECO:0000256|RuleBase:RU368036};
KW Hydrolase {ECO:0000256|RuleBase:RU368036};
KW Transferase {ECO:0000256|RuleBase:RU368036, ECO:0000313|EMBL:OWF64975.1};
KW Zymogen {ECO:0000256|RuleBase:RU368036}.
FT ACT_SITE 346
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR600101-1"
SQ SEQUENCE 532 AA; 57320 MW; 4CC712192AB9AA48 CRC64;
MQAKWGIQGM AVAPHSLASE SALAVLREGG NALEAMVAAA ATIAVVYPHM NSIGGDSFWV
IHSPGKAMGG IDACGAAAGL ASKQWYAERG ITKAIPFRGP VAANTVAGTI SGWGAAHKLS
KQGLGGKIPL SRLLADAIHY AEAGVPVTHS QSSLTAKKRE ELSSIPGFSK TFLVNGKAPA
VGSIFKQERL AKTLRQIASK GTDDFYRGDL ADLLAKELTD IGSPLRLSDL HRHHAKLIDP
LELKHSTGKV YNMIPPTQGV VSLMIIGILD QLNLKRFKVD STEYVHHCVE ATKQAFKIRD
QFVTDPAYMT KNAQAFLSPA FLKTLAKNIN PKKALPWGQG KGPADTIWMG VIDGDGNCVS
FIQSIYHEFG AGIVLPKSGV NWQNRGCSFS LDPKVLNHLE PYRKPFHTLN PAMALFKDGR
SMVYGTMGGD GQPQTQCAVF TRTATYGLDP QDAISRPRWL LGRTWGQTSD SLKLESRFSP
WVAKELHAMG HDIEMLDAFD ETVGHAGCII RDPSGTLRGG WDPRSDGAVS AF
//
