ID A0A023D0I6_ACIMT Unreviewed; 612 AA.
AC A0A023D0I6;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=Amme_005_025 {ECO:0000313|EMBL:GAJ27637.1};
OS Acidomonas methanolica NBRC 104435.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acidomonas.
OX NCBI_TaxID=1231351 {ECO:0000313|EMBL:GAJ27637.1, ECO:0000313|Proteomes:UP000019760};
RN [1] {ECO:0000313|Proteomes:UP000019760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB58 {ECO:0000313|Proteomes:UP000019760};
RX PubMed=24330138; DOI=10.1111/1574-6968.12357;
RA Higashiura N., Hadano H., Hirakawa H., Matsutani M., Takabe S.,
RA Matsushita K., Azuma Y.;
RT "Draft Genomic DNA Sequence of the Facultatively Methylotrophic Bacterium
RT Acidomonas methanolica type strain MB58.";
RL FEMS Microbiol. Lett. 351:9-13(2014).
RN [2] {ECO:0000313|EMBL:GAJ27637.1, ECO:0000313|Proteomes:UP000019760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB58 {ECO:0000313|EMBL:GAJ27637.1,
RC ECO:0000313|Proteomes:UP000019760};
RA Higashiura N., Hadano H., Hirakawa H., Matsutani M., Takabe S.,
RA Matsushita K., Azuma Y.;
RT "Draft genomic DNA sequence of the facultatively methylotrophic bacterium
RT Acidomonas methanolica type strain MB58.";
RL FEMS Microbiol. Lett. 351:9-13(2014).
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:GAJ27637.1}.
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DR EMBL; BAND01000005; GAJ27637.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A023D0I6; -.
DR UniPathway; UPA00204; -.
DR Proteomes; UP000019760; 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; PTHR43199; GLUTATHIONE HYDROLASE; 1.
DR PANTHER; PTHR43199:SF6; GLUTATHIONE HYDROLASE PROENZYME; 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:RU368036};
KW Glutathione biosynthesis {ECO:0000256|RuleBase:RU368036};
KW Hydrolase {ECO:0000256|RuleBase:RU368036};
KW Reference proteome {ECO:0000313|Proteomes:UP000019760};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|RuleBase:RU368036};
KW Zymogen {ECO:0000256|RuleBase:RU368036}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..612
FT /note="Glutathione hydrolase proenzyme"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030001241"
FT ACT_SITE 411
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR600101-1"
SQ SEQUENCE 612 AA; 64213 MW; 8716AB342DE37220 CRC64;
MVLSEMLKPC LVGIVLSAAV LAFPSAHAAP ALSSAHDPLA FGASVTHLQP LPPAMGRHGM
VATAQHLATD VGVRVMQEGG NAVDAAVAVA YALAVVYPAA GNLGGGGFMT LRMPNGESAF
IDFREHAPLA ATPTMYQDAQ GNVIPRLSIK GWKAVAVPGT VAGMELIHAR WGKLSREKVM
APAIALARDG FVVNEADVEL LHTSTSAFAQ DPYARKIFLH PDGTPFQAGE RLVQTDLAHT
LELIAANGAR AFYDGPIARA VVAASRQGGG ILQMADFAAY KTRQLKPLQC VYRGYLVETA
PPPSGGGVAL CEMLNILSGY DLEHLGLRSV AGAHDQIEAM RHAYSDRRGL GDPAFVHDPV
ELLVNPGYAA AIRAAIPADR AIPSDALVLD QAAPHYGDAQ PSAGEPEKHE TTQFSVMDGK
GMAVSVTYTL NGWFGAGVMG GPTGFFLNDE MDDFSTKPGV PNMFGIVGSK ANAVAPGKTP
LSSMTPTILS RDGRTVMVIG SPGGSRIPTI TLAVILGVVD GGMNIQQAID LPRIHEQWKP
APVEAELGAL DDTVTAGLQR EGYQITLHKP WGSAEGIFAV RPDRRSSPSA PLTEVLYGGF
DRRHGGGSAR GF
//
