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Glutathione hydrolase proenzyme (EC 3.4.19.13) (Gamma-glutamyltranspeptidase proenzyme) (GGT) (EC 2.3.2.2) [Cleaved into: Glutathione hydrolase large chain; Glutathione hydrolase small chain]

 GGT_ECOLI               Reviewed;         580 AA.
P18956; Q2M7B0;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
01-NOV-1990, sequence version 1.
12-SEP-2018, entry version 160.
RecName: Full=Glutathione hydrolase proenzyme;
EC=3.4.19.13 {ECO:0000305|PubMed:2877974};
AltName: Full=Gamma-glutamyltranspeptidase proenzyme {ECO:0000303|PubMed:2570061};
Short=GGT;
EC=2.3.2.2 {ECO:0000269|PubMed:1360205};
Contains:
RecName: Full=Glutathione hydrolase large chain;
Contains:
RecName: Full=Glutathione hydrolase small chain;
Flags: Precursor;
Name=ggt; OrderedLocusNames=b3447, JW3412;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 26-41 AND
391-403.
STRAIN=K12;
PubMed=2570061; DOI=10.1128/jb.171.9.5169-5172.1989;
Suzuki H., Kumagai H., Echigo T., Tochikura T.;
"DNA sequence of the Escherichia coli K-12 gamma-
glutamyltranspeptidase gene, ggt.";
J. Bacteriol. 171:5169-5172(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-362.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=8041620; DOI=10.1093/nar/22.13.2576;
Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
"Analysis of the Escherichia coli genome. V. DNA sequence of the
region from 76.0 to 81.5 minutes.";
Nucleic Acids Res. 22:2576-2586(1994).
[5]
FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
AND SUBCELLULAR LOCATION.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=2877974; DOI=10.1128/jb.168.3.1325-1331.1986;
Suzuki H., Kumagai H., Tochikura T.;
"gamma-Glutamyltranspeptidase from Escherichia coli K-12: purification
and properties.";
J. Bacteriol. 168:1325-1331(1986).
[6]
CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, SUBUNIT, MUTAGENESIS OF
ARG-513 AND ARG-571, AND AUTOCATALYTIC CLEAVAGE.
PubMed=1360205; DOI=10.1016/0006-291X(92)91540-7;
Hashimoto W., Suzuki H., Nohara S., Kumagai H.;
"Escherichia coli gamma-glutamyltranspeptidase mutants deficient in
processing to subunits.";
Biochem. Biophys. Res. Commun. 189:173-178(1992).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=8104180; DOI=10.1128/jb.175.18.6038-6040.1993;
Suzuki H., Hashimoto W., Kumagai H.;
"Escherichia coli K-12 can utilize an exogenous gamma-glutamyl peptide
as an amino acid source, for which gamma-glutamyltranspeptidase is
essential.";
J. Bacteriol. 175:6038-6040(1993).
[8]
X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 25-580 IN COMPLEX WITH
GLUTAMATE, SUBUNIT, ACTIVE SITE, AND AUTOCATALYTIC CLEAVAGE.
PubMed=16618936; DOI=10.1073/pnas.0511020103;
Okada T., Suzuki H., Wada K., Kumagai H., Fukuyama K.;
"Crystal structures of gamma-glutamyltranspeptidase from Escherichia
coli, a key enzyme in glutathione metabolism, and its reaction
intermediate.";
Proc. Natl. Acad. Sci. U.S.A. 103:6471-6476(2006).
[9]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 25-580 OF MUTANT ALA-391,
SUBUNIT, AUTOCATALYTIC CLEAVAGE, AND MUTAGENESIS OF THR-391.
PubMed=17135273; DOI=10.1074/jbc.M607490200;
Okada T., Suzuki H., Wada K., Kumagai H., Fukuyama K.;
"Crystal structure of the gamma-glutamyltranspeptidase precursor
protein from Escherichia coli. Structural changes upon autocatalytic
processing and implications for the maturation mechanism.";
J. Biol. Chem. 282:2433-2439(2007).
[10]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 25-580 IN COMPLEXES WITH
AZASERINE AND ACIVICIN, ACTIVE SITE, SUBUNIT, AND AUTOCATALYTIC
CLEAVAGE.
PubMed=18555071; DOI=10.1016/j.jmb.2008.05.007;
Wada K., Hiratake J., Irie M., Okada T., Yamada C., Kumagai H.,
Suzuki H., Fukuyama K.;
"Crystal structures of Escherichia coli gamma-glutamyltranspeptidase
in complex with azaserine and acivicin: novel mechanistic implication
for inhibition by glutamine antagonists.";
J. Mol. Biol. 380:361-372(2008).
-!- FUNCTION: Cleaves the gamma-glutamyl bond of periplasmic
glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other
gamma-glutamyl compounds. The metabolism of glutathione releases
free glutamate and the dipeptide cysteinyl-glycine, which is
hydrolyzed to cysteine and glycine by dipeptidases; it may
function in amino acid uptake/salvage, or possibly in
peptidoglycan linkage. Catalyzes the hydrolysis and
transpeptidation of many gamma-glutamyl compounds (including some
D-gamma-glutamyl substrates), with a preference for basic and
aromatic amino acids as acceptors (PubMed:2877974). The KM values
for gamma-glutamyl acceptors are so high that it has been proposed
transpeptidation is not the physiological role in E.coli
(PubMed:2877974, PubMed:8104180). {ECO:0000269|PubMed:2877974,
ECO:0000305|PubMed:8104180}.
-!- CATALYTIC ACTIVITY: A (5-L-glutamyl)-peptide + an amino acid = a
peptide + a 5-L-glutamyl amino acid. {ECO:0000269|PubMed:1360205}.
-!- CATALYTIC ACTIVITY: Glutathione + H(2)O = L-cysteinylglycine + L-
glutamate. {ECO:0000305|PubMed:2877974}.
-!- ACTIVITY REGULATION: Transferase and hydrolase activities are
inhibited by L-Ala and L-Gln, and also by GGT affinity labeling
reagents such as azaserine and 6-diazo-5-oxo-nor-leucine.
{ECO:0000269|PubMed:2877974}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=35 uM for glutathione transfer to glycylglycine (gly-gly)
{ECO:0000269|PubMed:2877974};
KM=35 uM for gamma-glutamyl-p-nitroanilide (gamma-GpNA) transfer
to gly-gly {ECO:0000269|PubMed:2877974};
KM=29 uM for glutathione hydrolysis
{ECO:0000269|PubMed:2877974};
KM=68 uM for gamma-GpNA hydrolysis {ECO:0000269|PubMed:2877974};
pH dependence:
Optimum pH is 8.73 for transfer of p-nitroanilide from gamma-
GpNA to gly-gly and 9.25 for hydrolysis of gamma-GpNA.
{ECO:0000269|PubMed:2877974};
Temperature dependence:
Optimum temperature is 50 degrees Celsius for both transferase
and hydrolase activities. {ECO:0000269|PubMed:2877974};
-!- PATHWAY: Sulfur metabolism; glutathione metabolism.
-!- SUBUNIT: This enzyme consists of two polypeptide chains, which are
synthesized in precursor form from a single polypeptide.
{ECO:0000269|PubMed:1360205, ECO:0000269|PubMed:16618936,
ECO:0000269|PubMed:17135273, ECO:0000269|PubMed:18555071,
ECO:0000269|PubMed:2877974}.
-!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:1360205,
ECO:0000269|PubMed:2877974}.
-!- PTM: Cleaved by autocatalysis into a large and a small subunit.
{ECO:0000269|PubMed:1360205, ECO:0000269|PubMed:16618936,
ECO:0000269|PubMed:17135273, ECO:0000269|PubMed:18555071,
ECO:0000269|PubMed:2570061}.
-!- DISRUPTION PHENOTYPE: Loss of growth using exogenous gamma-
glutamyl peptides as amino acid sources.
{ECO:0000269|PubMed:8104180}.
-!- SIMILARITY: Belongs to the gamma-glutamyltransferase family.
{ECO:0000305}.
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EMBL; M28722; AAA23869.1; -; Genomic_DNA.
EMBL; U18997; AAA58245.1; -; Genomic_DNA.
EMBL; U00096; AAC76472.1; -; Genomic_DNA.
EMBL; AP009048; BAE77846.1; -; Genomic_DNA.
EMBL; U00039; AAB18422.1; -; Genomic_DNA.
PIR; JV0028; EKECEX.
RefSeq; NP_417904.1; NC_000913.3.
RefSeq; WP_000595082.1; NZ_LN832404.1.
PDB; 2DBU; X-ray; 1.95 A; A/C=25-390, B/D=391-580.
PDB; 2DBW; X-ray; 1.80 A; A/C=25-390, B/D=391-580.
PDB; 2DBX; X-ray; 1.70 A; A/C=25-390, B/D=391-580.
PDB; 2DG5; X-ray; 1.60 A; A/C=25-390, B/D=391-580.
PDB; 2E0W; X-ray; 2.55 A; A/B=25-580.
PDB; 2E0X; X-ray; 1.95 A; A/C=25-390, B/D=391-580.
PDB; 2E0Y; X-ray; 2.02 A; A/C=25-390, B/D=391-580.
PDB; 2Z8I; X-ray; 1.65 A; A/C=25-390, B/D=391-580.
PDB; 2Z8J; X-ray; 2.05 A; A/C=25-390, B/D=391-580.
PDB; 2Z8K; X-ray; 1.65 A; A/C=25-390, B/D=391-580.
PDB; 5B5T; X-ray; 1.70 A; A/C=25-390, B/D=391-580.
PDBsum; 2DBU; -.
PDBsum; 2DBW; -.
PDBsum; 2DBX; -.
PDBsum; 2DG5; -.
PDBsum; 2E0W; -.
PDBsum; 2E0X; -.
PDBsum; 2E0Y; -.
PDBsum; 2Z8I; -.
PDBsum; 2Z8J; -.
PDBsum; 2Z8K; -.
PDBsum; 5B5T; -.
ProteinModelPortal; P18956; -.
SMR; P18956; -.
BioGrid; 4261666; 434.
DIP; DIP-9758N; -.
IntAct; P18956; 1.
STRING; 316385.ECDH10B_3621; -.
MEROPS; T03.001; -.
PaxDb; P18956; -.
PRIDE; P18956; -.
EnsemblBacteria; AAC76472; AAC76472; b3447.
EnsemblBacteria; BAE77846; BAE77846; BAE77846.
GeneID; 947947; -.
KEGG; ecj:JW3412; -.
KEGG; eco:b3447; -.
PATRIC; fig|511145.12.peg.3544; -.
EchoBASE; EB0369; -.
EcoGene; EG10374; ggt.
eggNOG; ENOG4105CFB; Bacteria.
eggNOG; COG0405; LUCA.
HOGENOM; HOG000175617; -.
InParanoid; P18956; -.
KO; K00681; -.
OMA; TKNMFLD; -.
PhylomeDB; P18956; -.
BioCyc; EcoCyc:EG10374-MONOMER; -.
BioCyc; MetaCyc:EG10374-MONOMER; -.
BRENDA; 2.3.2.2; 2026.
BRENDA; 3.4.19.13; 2026.
SABIO-RK; P18956; -.
UniPathway; UPA00204; -.
EvolutionaryTrace; P18956; -.
PRO; PR:P18956; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
GO; GO:0042597; C:periplasmic space; IDA:EcoliWiki.
GO; GO:0034722; F:gamma-glutamyl-peptidase activity; IDA:EcoCyc.
GO; GO:0036374; F:glutathione hydrolase activity; IDA:EcoCyc.
GO; GO:0102953; F:hypoglycin A gamma-glutamyl transpeptidase activity; IEA:UniProtKB-EC.
GO; GO:0103068; F:leukotriene C4 gamma-glutamyl transferase activity; IEA:UniProtKB-EC.
GO; GO:0043102; P:amino acid salvage; IMP:EcoCyc.
GO; GO:0006750; P:glutathione biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0006751; P:glutathione catabolic process; IEA:InterPro.
GO; GO:0097264; P:self proteolysis; IDA:EcoCyc.
InterPro; IPR000101; GGT_peptidase.
InterPro; IPR029055; Ntn_hydrolases_N.
SUPFAM; SSF56235; SSF56235; 1.
TIGRFAMs; TIGR00066; g_glut_trans; 1.
PROSITE; PS00462; G_GLU_TRANSPEPTIDASE; 1.
1: Evidence at protein level;
3D-structure; Acyltransferase; Complete proteome;
Direct protein sequencing; Glutathione biosynthesis; Hydrolase;
Periplasm; Protease; Reference proteome; Signal; Transferase; Zymogen.
SIGNAL 1 25 {ECO:0000269|PubMed:2570061}.
CHAIN 26 390 Glutathione hydrolase large chain.
/FTId=PRO_0000011052.
CHAIN 391 580 Glutathione hydrolase small chain.
/FTId=PRO_0000011053.
REGION 462 463 Glutamate binding.
REGION 483 484 Glutamate binding.
ACT_SITE 391 391 Nucleophile.
{ECO:0000269|PubMed:16618936,
ECO:0000269|PubMed:18555071}.
BINDING 114 114 Glutamate. {ECO:0000269|PubMed:16618936}.
BINDING 409 409 Glutamate. {ECO:0000269|PubMed:16618936}.
BINDING 411 411 Glutamate. {ECO:0000269|PubMed:16618936}.
BINDING 430 430 Glutamate. {ECO:0000269|PubMed:16618936}.
BINDING 433 433 Glutamate. {ECO:0000269|PubMed:16618936}.
MUTAGEN 391 391 T->A: Abolishes autocatalytic cleavage,
loss of enzymatic activity.
{ECO:0000269|PubMed:17135273}.
MUTAGEN 513 513 R->A: Not processed into its subunits,
loss of enzymatic activity.
{ECO:0000269|PubMed:1360205}.
MUTAGEN 571 571 R->G: Not processed into its subunits,
loss of enzymatic activity.
{ECO:0000269|PubMed:1360205}.
STRAND 39 41 {ECO:0000244|PDB:2DBU}.
STRAND 44 48 {ECO:0000244|PDB:2DG5}.
STRAND 50 54 {ECO:0000244|PDB:2DG5}.
HELIX 56 67 {ECO:0000244|PDB:2DG5}.
HELIX 72 86 {ECO:0000244|PDB:2DG5}.
TURN 88 90 {ECO:0000244|PDB:2DG5}.
STRAND 93 102 {ECO:0000244|PDB:2DG5}.
STRAND 108 113 {ECO:0000244|PDB:2DG5}.
TURN 123 126 {ECO:0000244|PDB:2DG5}.
STRAND 129 131 {ECO:0000244|PDB:2E0Y}.
HELIX 135 139 {ECO:0000244|PDB:2DG5}.
HELIX 142 144 {ECO:0000244|PDB:2DG5}.
HELIX 150 161 {ECO:0000244|PDB:2DG5}.
HELIX 166 179 {ECO:0000244|PDB:2DG5}.
HELIX 185 193 {ECO:0000244|PDB:2DG5}.
HELIX 195 197 {ECO:0000244|PDB:2DG5}.
HELIX 199 201 {ECO:0000244|PDB:2DG5}.
HELIX 203 209 {ECO:0000244|PDB:2DG5}.
HELIX 225 237 {ECO:0000244|PDB:2DG5}.
HELIX 240 243 {ECO:0000244|PDB:2DG5}.
HELIX 246 257 {ECO:0000244|PDB:2DG5}.
HELIX 264 269 {ECO:0000244|PDB:2DG5}.
STRAND 273 275 {ECO:0000244|PDB:2DG5}.
STRAND 278 282 {ECO:0000244|PDB:2DG5}.
STRAND 285 289 {ECO:0000244|PDB:2DG5}.
HELIX 296 307 {ECO:0000244|PDB:2DG5}.
HELIX 312 315 {ECO:0000244|PDB:2DG5}.
HELIX 320 340 {ECO:0000244|PDB:2DG5}.
TURN 344 346 {ECO:0000244|PDB:2DG5}.
HELIX 351 354 {ECO:0000244|PDB:2DG5}.
HELIX 357 364 {ECO:0000244|PDB:2DG5}.
HELIX 375 377 {ECO:0000244|PDB:2DG5}.
HELIX 384 386 {ECO:0000244|PDB:2DG5}.
STRAND 392 397 {ECO:0000244|PDB:2DG5}.
STRAND 403 409 {ECO:0000244|PDB:2DG5}.
TURN 413 416 {ECO:0000244|PDB:2DG5}.
HELIX 421 423 {ECO:0000244|PDB:2DG5}.
HELIX 430 433 {ECO:0000244|PDB:2DG5}.
STRAND 434 437 {ECO:0000244|PDB:2DG5}.
STRAND 467 471 {ECO:0000244|PDB:2DG5}.
STRAND 474 479 {ECO:0000244|PDB:2DG5}.
HELIX 484 486 {ECO:0000244|PDB:2DG5}.
HELIX 487 499 {ECO:0000244|PDB:2DG5}.
HELIX 505 510 {ECO:0000244|PDB:2DG5}.
STRAND 518 520 {ECO:0000244|PDB:2DG5}.
STRAND 523 525 {ECO:0000244|PDB:2DG5}.
HELIX 531 539 {ECO:0000244|PDB:2DG5}.
STRAND 544 546 {ECO:0000244|PDB:2DG5}.
STRAND 554 558 {ECO:0000244|PDB:2DG5}.
STRAND 564 568 {ECO:0000244|PDB:2DG5}.
STRAND 576 579 {ECO:0000244|PDB:2DG5}.
SEQUENCE 580 AA; 61768 MW; 772F652EBA2A5F00 CRC64;
MIKPTFLRRV AIAALLSGSC FSAAAAPPAP PVSYGVEEDV FHPVRAKQGM VASVDATATQ
VGVDILKEGG NAVDAAVAVG YALAVTHPQA GNLGGGGFML IRSKNGNTTA IDFREMAPAK
ATRDMFLDDQ GNPDSKKSLT SHLASGTPGT VAGFSLALDK YGTMPLNKVV QPAFKLARDG
FIVNDALADD LKTYGSEVLP NHENSKAIFW KEGEPLKKGD TLVQANLAKS LEMIAENGPD
EFYKGTIAEQ IAQEMQKNGG LITKEDLAAY KAVERTPISG DYRGYQVYSM PPPSSGGIHI
VQILNILENF DMKKYGFGSA DAMQIMAEAE KYAYADRSEY LGDPDFVKVP WQALTNKAYA
KSIADQIDIN KAKPSSEIRP GKLAPYESNQ TTHYSVVDKD GNAVAVTYTL NTTFGTGIVA
GESGILLNNQ MDDFSAKPGV PNVYGLVGGD ANAVGPNKRP LSSMSPTIVV KDGKTWLVTG
SPGGSRIITT VLQMVVNSID YGLNVAEATN APRFHHQWLP DELRVEKGFS PDTLKLLEAK
GQKVALKEAM GSTQSIMVGP DGELYGASDP RSVDDLTAGY


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