GGT_PSEAE
ID GGT_PSEAE Reviewed; 557 AA.
AC Q9I406;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Glutathione hydrolase proenzyme;
DE EC=3.4.19.13;
DE AltName: Full=Gamma-glutamyltranspeptidase proenzyme;
DE EC=2.3.2.2;
DE Contains:
DE RecName: Full=Glutathione hydrolase large chain;
DE Contains:
DE RecName: Full=Glutathione hydrolase small chain;
DE Flags: Precursor;
GN Name=ggt; OrderedLocusNames=PA1338;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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 -!- 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 -!- 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 -!- PATHWAY: Sulfur metabolism; glutathione metabolism.
CC -!- SUBUNIT: This enzyme consists of two polypeptide chains, which are
CC synthesized in precursor form from a single polypeptide. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC -!- PTM: Cleaved by autocatalysis into a large and a small subunit.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the gamma-glutamyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AE004091; AAG04727.1; -; Genomic_DNA.
DR PIR; D83478; D83478.
DR RefSeq; NP_250029.1; NC_002516.2.
DR RefSeq; WP_003086881.1; NZ_QZGE01000005.1.
DR AlphaFoldDB; Q9I406; -.
DR SMR; Q9I406; -.
DR STRING; 287.DR97_456; -.
DR MEROPS; T03.001; -.
DR PaxDb; Q9I406; -.
DR PRIDE; Q9I406; -.
DR EnsemblBacteria; AAG04727; AAG04727; PA1338.
DR GeneID; 882262; -.
DR KEGG; pae:PA1338; -.
DR PATRIC; fig|208964.12.peg.1390; -.
DR PseudoCAP; PA1338; -.
DR HOGENOM; CLU_014813_0_3_6; -.
DR InParanoid; Q9I406; -.
DR OMA; KATKNMF; -.
DR PhylomeDB; Q9I406; -.
DR BioCyc; PAER208964:G1FZ6-1364-MON; -.
DR UniPathway; UPA00204; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0036374; F:glutathione hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0102953; F:hypoglycin A gamma-glutamyl transpeptidase activity; IEA:UniProtKB-EC.
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:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 SUPFAM; SSF56235; SSF56235; 1.
DR TIGRFAMs; TIGR00066; g_glut_trans; 1.
DR PROSITE; PS00462; G_GLU_TRANSPEPTIDASE; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Glutathione biosynthesis; Hydrolase; Periplasm; Protease;
KW Reference proteome; Signal; Transferase; Zymogen.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..363
FT /note="Glutathione hydrolase large chain"
FT /id="PRO_0000287773"
FT CHAIN 364..557
FT /note="Glutathione hydrolase small chain"
FT /id="PRO_0000287774"
FT ACT_SITE 364
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 94
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 382
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 384
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 403
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 406
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 435..436
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 456..457
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
SQ SEQUENCE 557 AA; 59874 MW; FDE0DFE595665510 CRC64;
MQPVLFRTLS LGVAIAAASS SAFAATLDGG AVAAPDEYGA KVAAQILKAG GNAVDAAVAT
AFTLAVTYPE AGNIGGGGFM TLYMDGKPYF LDYREVAPKA ASKTMYLDDK GEVIENLSLV
GAKAAGVPGT VMGLWEAHKR FGKLPWSELL TPAIGYAQKG FKVADKQFQY RQDAVALFNG
KTNFGDYFGH MKAGEAFLQP DLAKTLERIA DKGPDEFYKG HTADLLVAQM QQDKGLITHQ
DLADYKVRWR EPMRVDWQGN TLYTAPLPSS GGIALAQLLG IKENRAADFK GVELNSARYI
HLLAEIEKRV FADRADYLGD PDFSKVPVAR LTDPAYLKQR AAEVNPTAIS PTEKVRPGLE
PHQTTHFSIV DADGNAVSNT YTLNWDFGSG VVVKGAGFLL NDEMDDFSAK PGVANAFGVV
GSDANAIEPG KRMLSSMSPS IVTRDGKVSL VVGTPGGSRI FTSIFQVLNN IYDFHLPLEK
AVAAQRVHHQ LLPKDTIYYD AYAPLAGKVA EELKAMGYTL EDQGWNMGDI QAIRVDGKAL
ETASDPRGRG VGLVVKP
