ID A0A1L7CIS2_CORFL Unreviewed; 661 AA.
AC A0A1L7CIS2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 32.
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 Name=ggt {ECO:0000313|EMBL:KAA8719587.1};
GN ORFNames=CFLV_00030 {ECO:0000313|EMBL:APT85760.1}, F4V60_12420
GN {ECO:0000313|EMBL:KAA8719587.1};
OS Corynebacterium flavescens.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=28028 {ECO:0000313|EMBL:APT85760.1, ECO:0000313|Proteomes:UP000185479};
RN [1] {ECO:0000313|EMBL:APT85760.1, ECO:0000313|Proteomes:UP000185479}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OJ8 {ECO:0000313|EMBL:APT85760.1,
RC ECO:0000313|Proteomes:UP000185479};
RA Ruckert C., Albersmeier A., Winkler A., Kalinowski J.;
RT "Complete genome sequence of Corynebacterium flavescens OJ8(T)(=DSM
RT 20296(T)), isolated from cheese.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAA8719587.1, ECO:0000313|Proteomes:UP000322697}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 28791T {ECO:0000313|EMBL:KAA8719587.1,
RC ECO:0000313|Proteomes:UP000322697};
RA Pineiro-Iglesias B., Tunovic T., Unosson C., Inganas E., Ohlen M.,
RA Cardew S., Jensie-Markopoulos S., Salva-Serra F., Jaen-Luchoro D.,
RA Karlsson R., Svensson-Stadler L., Chun J., Moore E.;
RT "Draft genome sequence of various Type strains from the CCUG.";
RL Submitted (SEP-2019) 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|ARBA:ARBA00009381, ECO:0000256|RuleBase:RU368036}.
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 EMBL; CP009246; APT85760.1; -; Genomic_DNA.
DR EMBL; VXKK01000046; KAA8719587.1; -; Genomic_DNA.
DR RefSeq; WP_075728772.1; NZ_VXKK01000046.1.
DR AlphaFoldDB; A0A1L7CIS2; -.
DR STRING; 28028.CFLV_00030; -.
DR GeneID; 82879125; -.
DR KEGG; cfc:CFLV_00030; -.
DR OrthoDB; 9781342at2; -.
DR UniPathway; UPA00204; -.
DR Proteomes; UP000185479; Chromosome.
DR Proteomes; UP000322697; 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: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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000185479};
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..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..661
FT /note="Glutathione hydrolase proenzyme"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5033277398"
FT REGION 26..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 462
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR600101-1"
SQ SEQUENCE 661 AA; 67623 MW; 0FADC3F1205D9E6C CRC64;
MKTVNHSLKA VVAATAAISL GLSLSSCTNN SDTPSTPSTS DTAAATAPAP QPCELPAGSE
ASGPATGTHS GEDISVAPEI ATGYRSGMEP VTTQSYAVAT ANPLASQAAC AVLLEGGTAA
DALVAAQFTL GLTEPQSSGI GGGGYIVYYD AQKDEVSAID ARETAPVAAD ENYLIHVSDQ
DTSAPVPDAR RSGRSIGVPG IVAGLGELHA EHGKTAWDQI LEPTADLASA GFEISPRMSA
SIASSAEDLA TDPEAAEYFL NEDGSAKEAG TLLKNPAYAD TVRKIATGGA DAFYTGDIAA
AIVDRATRNV EGFTPSLMST ADLAAYTPEK SEALCGPYRD RIICGMPPSS SGGIAVIETL
GILNNVDLAK YAPSDVGLDG GLPNVEAIHL ISEAERLAYA DRDAYVGDPA FVSVPGGGID
ELISPEYTRE RAGQINPDTS MGEAQPGLST AAAGPITPEH GTSHISVIDS YGNAASLTTS
VEAAFGSFHF TRGFILNNQL TDFSAEPTNE AGEPVANRVE SAKRPRSSMS PMLVFAGAGA
AGTDSTTDRG DLEMVVGSPG GSLIIQFVVK TLVNMIDWGM DPQQAVSAPN FGAMNKPETG
IGTEHPLLAE HESEIAEGLE QRGHEVNATD QSSGLSALVR SGEDIIGGAD PRREGVVLGG
T
//
