ID A0A0U4BC98_9ACTN Unreviewed; 609 AA.
AC A0A0U4BC98;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=AERYTH_12725 {ECO:0000313|EMBL:ALX05497.1};
OS Aeromicrobium erythreum.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Aeromicrobium.
OX NCBI_TaxID=2041 {ECO:0000313|EMBL:ALX05497.1, ECO:0000313|Proteomes:UP000067689};
RN [1] {ECO:0000313|EMBL:ALX05497.1, ECO:0000313|Proteomes:UP000067689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR18 {ECO:0000313|EMBL:ALX05497.1,
RC ECO:0000313|Proteomes:UP000067689};
RX PubMed=1883712;
RA Miller E.S., Woese C.R., Brenner S.;
RT "Description of the erythromycin-producing bacterium Arthrobacter sp.
RT strain NRRL B-3381 as Aeromicrobium erythreum gen. nov., sp. nov.";
RL Int. J. Syst. Bacteriol. 41:363-368(1991).
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|ARBA:ARBA00009381, ECO:0000256|RuleBase:RU368036}.
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DR EMBL; CP011502; ALX05497.1; -; Genomic_DNA.
DR RefSeq; WP_067859319.1; NZ_CP011502.1.
DR AlphaFoldDB; A0A0U4BC98; -.
DR STRING; 2041.AERYTH_12725; -.
DR KEGG; aer:AERYTH_12725; -.
DR PATRIC; fig|2041.4.peg.2645; -.
DR OrthoDB; 9781342at2; -.
DR UniPathway; UPA00204; -.
DR Proteomes; UP000067689; Chromosome.
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:SF1; 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|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368036};
KW Reference proteome {ECO:0000313|Proteomes:UP000067689};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368036};
KW Zymogen {ECO:0000256|RuleBase:RU368036}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..609
FT /note="Glutathione hydrolase proenzyme"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006846824"
FT REGION 28..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 416
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR600101-1"
SQ SEQUENCE 609 AA; 63597 MW; DD7CFD733CF44D55 CRC64;
MTARLTVRAV TGLAAGALAA SALVATTTPA DAGPRPSRPP VASPTAYGSG GAVASVDAEA
SKVGLEVLRR GGNAADAAVA TASALGVTEP YSAGIGGGGY FVYYDAKRKK VSTIDGRETA
PAGITRDAFI DPSTGKPYRF TPELVSSGVA VGVPGTPATW EAALRDHGRW SLRQALAPSI
KLAERGFMVD RTFRSQTLDN KDRFAAFPDT ARLFLPGGDA PQVGSTFRNP ELARTLSLIA
AKGPRAFYTG SVARDVARTV QAPPKDPASD LPAPPGSLTE RDLATYRVDR QAPTHARYRG
LDVYGMAPSS SGGIAVGEAL NILEGYRLGG GARLGSSLHL FLEASARAFA DRAAYVGDVP
DVPVRTLLSQ RFADSRACSI DPTQASQRPV AAGALDGDPC TTRAAEEKPD TENISTTHLS
VVDRWGNAAS YTLTIEQTGG SAITVPGRGF LLNNELTDFT AVYDPKDPNR IEPGKRPRSS
MSPTIVLDRG RVKYVVGSPG GATIITTVLQ VLLNRIDLGM TLPQAVAAPR ASQRNAAVTP
AEPAFIEQYG GLLAPFGQQL TPSGDAFTSQ AEIGAVAAIE QDRRGRLTAV AEPQRRGGGT
ALVVRPDRR
//
