UniProtKB - P63186 (GGT_BACNA)
Glutathione hydrolase proenzyme
ggt
Functioni
Cleaves the gamma-glutamyl bond of extracellular 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. Uses glutamine as a gamma-glutamyl donor and acceptor for gamma-polyglutamic acid synthesis. Dipeptides are better gamma-glutamyl acceptors than free amino acids (PubMed:1371053).
1 PublicationCatalytic activityi
- an α-amino acid + an N-terminal (5-L-glutamyl)-[peptide] = 5-L-glutamyl amino acid + N-terminal L-α-aminoacyl-[peptide]1 PublicationEC:2.3.2.21 Publication
- EC:3.4.19.13
- EC:3.4.19.13
Activity regulationi
pH dependencei
Temperature dependencei
: glutathione metabolism Pathwayi
This protein is involved in the pathway glutathione metabolism, which is part of Sulfur metabolism.View all proteins of this organism that are known to be involved in the pathway glutathione metabolism and in Sulfur metabolism.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 113 | GlutamateBy similarity | 1 | |
Active sitei | 403 | NucleophileBy similarity | 1 | |
Binding sitei | 421 | GlutamateBy similarity | 1 | |
Binding sitei | 423 | GlutamateBy similarity | 1 | |
Binding sitei | 442 | GlutamateBy similarity | 1 | |
Binding sitei | 445 | GlutamateBy similarity | 1 |
GO - Molecular functioni
- glutathione hydrolase activity Source: UniProtKB-EC
- hypoglycin A gamma-glutamyl transpeptidase activity Source: UniProtKB-EC
- leukotriene C4 gamma-glutamyl transferase activity Source: UniProtKB-EC
GO - Biological processi
- glutathione biosynthetic process Source: UniProtKB-KW
- glutathione catabolic process Source: InterPro
Keywordsi
Molecular function | Acyltransferase, Hydrolase, Protease, Transferase |
Biological process | Glutathione biosynthesis |
Enzyme and pathway databases
UniPathwayi | UPA00204 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:ggt |
Organismi | Bacillus subtilis subsp. natto |
Taxonomic identifieri | 86029 [NCBI] |
Taxonomic lineagei | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › |
Subcellular locationi
Extracellular region or secreted
- Secreted 1 Publication
Extracellular region or secreted
- extracellular region Source: UniProtKB-SubCell
Keywords - Cellular componenti
SecretedPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 28 | Sequence analysisAdd BLAST | 28 | |
PropeptideiPRO_0000011046 | 29 – 35 | Sequence analysis | 7 | |
ChainiPRO_0000011047 | 36 – 402 | Glutathione hydrolase large chainAdd BLAST | 367 | |
ChainiPRO_0000011048 | 403 – 587 | Glutathione hydrolase small chainAdd BLAST | 185 |
Post-translational modificationi
Keywords - PTMi
ZymogenInteractioni
Subunit structurei
This enzyme consists of two polypeptide chains, which are synthesized in precursor form from a single polypeptide.
1 PublicationFamily & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 464 – 465 | Glutamate bindingBy similarity | 2 | |
Regioni | 485 – 486 | Glutamate bindingBy similarity | 2 |
Sequence similaritiesi
Keywords - Domaini
SignalFamily and domain databases
Gene3Di | 1.10.246.130, 1 hit 3.60.20.40, 1 hit |
InterProi | View protein in InterPro IPR043138, GGT_lsub_C IPR000101, GGT_peptidase IPR043137, GGT_ssub IPR029055, Ntn_hydrolases_N |
SUPFAMi | SSF56235, SSF56235, 1 hit |
TIGRFAMsi | TIGR00066, g_glut_trans, 1 hit |
PROSITEi | View protein in PROSITE PS00462, G_GLU_TRANSPEPTIDASE, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
10 20 30 40 50
MKRTWNVCLT ALLSVLLVAG SVPFHAEAKK PPKSYDEYKQ VDVGKDGMVA
60 70 80 90 100
TAHALASEIG ADVLKKGGNA IDAAVAIQFA LNVTEPMMSG IGGGGFMMVY
110 120 130 140 150
DGKTKDTTII DSRERAPAGA TPDMFLDENG KAIPFSERVT KGTAVGVPGT
160 170 180 190 200
LKGLEEALDK WGTRSMKLLI TLTIKLAEKG FPIDSVLADA ISDYQEKLSR
210 220 230 240 250
TAAKDVFLPN GEPLKEGDTL IQKDLAKTFK LIRSKGTDAF YKGKFAKTLS
260 270 280 290 300
DTVQDFGGSM TEKDLENYDI TIDEPIWGDY QGYQIATTPP PSSGGIFLLQ
310 320 330 340 350
MLKILDDFNL SQYDVRSWEK YQLLAETMHL SYADRASYAG DPEFVNVPLK
360 370 380 390 400
GLLHPDYIKE RQQLINLDQV NKKPKAGDPW KYQEGSANYK QVEQPKDKVE
410 420 430 440 450
GQTTHFTVAD RWGNVVSYTT TIEQLFGTGI MVPDYGVILN NELTDFDAIP
460 470 480 490 500
GGANEVQPNK RPLSSMTPTI LFKDDKPVLT VGSPGGATII SSVLQTILYH
510 520 530 540 550
IEYGMGLKAA VEEPRIYTTS MSSYRYEDGV PKDVLSKLNG MGHRFGTSPV
560 570 580
DIGNVQSISI DHENGTFKGV VISGSNDAAI GINLKRK
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 46 | D → V AA sequence (PubMed:1371053).Curated | 1 |
Sequence databases
PIRi | F69631 |
Similar proteinsi
Cross-referencesi
Sequence databases
PIRi | F69631 |
3D structure databases
AlphaFoldDBi | P63186 |
SMRi | P63186 |
ModBasei | Search... |
Enzyme and pathway databases
UniPathwayi | UPA00204 |
Family and domain databases
Gene3Di | 1.10.246.130, 1 hit 3.60.20.40, 1 hit |
InterProi | View protein in InterPro IPR043138, GGT_lsub_C IPR000101, GGT_peptidase IPR043137, GGT_ssub IPR029055, Ntn_hydrolases_N |
SUPFAMi | SSF56235, SSF56235, 1 hit |
TIGRFAMsi | TIGR00066, g_glut_trans, 1 hit |
PROSITEi | View protein in PROSITE PS00462, G_GLU_TRANSPEPTIDASE, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | GGT_BACNA | |
Accessioni | P63186Primary (citable) accession number: P63186 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | September 27, 2004 |
Last sequence update: | September 27, 2004 | |
Last modified: | May 25, 2022 | |
This is version 69 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Direct protein sequencingDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families