ID A0A1C2HB59_9RHOB Unreviewed; 527 AA.
AC A0A1C2HB59;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Gamma-glutamyltransferase {ECO:0000313|EMBL:OCX60994.1};
GN ORFNames=BFP70_16150 {ECO:0000313|EMBL:OCX60994.1};
OS Thioclava sp. SK-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Thioclava.
OX NCBI_TaxID=1889770 {ECO:0000313|EMBL:OCX60994.1, ECO:0000313|Proteomes:UP000094269};
RN [1] {ECO:0000313|EMBL:OCX60994.1, ECO:0000313|Proteomes:UP000094269}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK-1 {ECO:0000313|EMBL:OCX60994.1,
RC ECO:0000313|Proteomes:UP000094269};
RA Wong S.-K., Hamasaki K., Yoshizawa S.;
RT "Draft genome of Thioclava sp. strain SK-1.";
RL Submitted (AUG-2016) 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 -!- 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 -!- 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 -!- 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:OCX60994.1}.
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DR EMBL; MDHA01000069; OCX60994.1; -; Genomic_DNA.
DR RefSeq; WP_066012729.1; NZ_MDHA01000069.1.
DR AlphaFoldDB; A0A1C2HB59; -.
DR STRING; 1889770.BFP70_16150; -.
DR OrthoDB; 9781342at2; -.
DR Proteomes; UP000094269; Unassembled WGS sequence.
DR GO; GO:0036374; F:glutathione hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0103068; F:leukotriene C4 gamma-glutamyl transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006751; P:glutathione catabolic process; IEA:InterPro.
DR Gene3D; 3.60.20.40; -; 1.
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; 2.
DR PRINTS; PR01210; GGTRANSPTASE.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Reference proteome {ECO:0000313|Proteomes:UP000094269};
KW Transferase {ECO:0000313|EMBL:OCX60994.1}.
FT ACT_SITE 340
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR600101-1"
SQ SEQUENCE 527 AA; 55085 MW; 62917FBD859134B9 CRC64;
MSGSFAPSQT TRKPGVTATS GGVVAAQHAL AAQAGADILA QGGDAVDAAV AVSFVIGVLE
PWMSGPLGGG AMMLWREGEG AKALHYGMRS SAALDPSYYP LSGHGKAGDL FPWEHLVDDR
NIIGGSSVAV PGTVDGLAKA HGRYGTLPWK ELLAPAIAHA KLGLHVDYYA ALIIASSARE
LAQDPDAAAL FLDDGQWPKG SGWTALADQR LDQSRHADTL DHLANAGPRD LYEGDIAAAL
VRDVTDKGGF LTAQDLAGYS AAWQEALHIP FRNGALWAVP ELSAGPTLAD AMARWQTSYA
PDQAQTPAAH LARAQGLYDA YDARLTQMGD HENPKAPGCT THFSIVDRHG NMVAMTQTLL
SIFGSRAVSP STGMLLNNGI MWFDPEQGKP NSLGPDKGCL MNVCPIVGQA GPRRFALGAS
GGRKIMPAVA QISGQLIEQG ATMQDAIEAP RLDVSGGDLV VLDERLRGPV SDAVASVFPV
AHAQRLPFPF AFACPAGVMR EGVVNSGTTE TFSPWGDGIA ETCKAAR
//
