A0AMA3 · GSHAB_LISW6
- ProteinGlutathione biosynthesis bifunctional protein GshAB
- GenegshAB
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids776 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Synthesizes glutathione from L-glutamate and L-cysteine via gamma-L-glutamyl-L-cysteine.
Catalytic activity
- ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-cysteine + H+ + phosphate
Cofactor
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Note: Binds 2 magnesium or manganese ions per subunit.
Pathway
Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 1/2.
Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 2/2.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 548-606 | ATP (UniProtKB | ChEBI) | ||||
Sequence: SLFKDKQIVVKPKSTNYGWGISIFKNKFTTEDYQEALNIAFSYDSSVIIEEFIPGDEFR | ||||||
Binding site | 728 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 728 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 745 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 745 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 745 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 745 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 747 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 747 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: N |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | ATP binding | |
Molecular Function | glutamate-cysteine ligase activity | |
Molecular Function | glutathione synthase activity | |
Molecular Function | metal ion binding |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGlutathione biosynthesis bifunctional protein GshAB
- Alternative names
Including 2 domains:
- Recommended nameGlutamate--cysteine ligase
- EC number
- Alternative names
- Recommended nameGlutathione synthetase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Listeriaceae > Listeria
Accessions
- Primary accessionA0AMA3
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000133720 | 1-776 | Glutathione biosynthesis bifunctional protein GshAB | |||
Sequence: MIKLDMTILDSLKENKALRKLLFSGHFGLEKENIRVTSDGKLALTPHPAIFGPKEDNPYIKTDFSESQIEMITPVTDSIDDVYNWLENLHNIVSLRSKNELLWPSSNPPILPAEKDIPIAEYKTPDSPDRKYREHLAQGYGKKIQLLSGIHYNFSFPEALIDGLYDEISLPNESKRDFKNRLYLKVAKYFMKNRWLLIYLTGASPVYLADFTKTKQEEKLRDGSSALHDGISLRNSNAGYKNKESLYVDYNSFDAYISSISNYIEAGKIESMREFYNPIRLKNAHTDQTVESLAKHGVEYLEIRSIDLNPLEPNGISKEALHFIHLFLIKGLLSEDRELCENNQQLADENENNIALNGLSKPAIKNCDNEEMALADAGLLELDKMNDFIQSLRPEDTYFQAIIEKQKERLLHPEKTIAAQVKEQSATAGFIEFHLNQAKTYMEETEALAYKLIGAEDMELSTQIIWKDAIARGIKVDVLDRAENFLRFQKGDHVEYVKQASKTSKDNYVSVLMMENKVVTKLVLAENNIRVPFGDSFSDQALALEAFSLFKDKQIVVKPKSTNYGWGISIFKNKFTTEDYQEALNIAFSYDSSVIIEEFIPGDEFRFLVINDKVEAVLKRVPANVTGDGIHTVRELVEEKNMDPLRGTDHLKPLEKIRTGPEETLMLSMQKLSWDSIPKANETIYLRENSNVSTGGDSIDYTAEMDDYFKEIAIRATQVLDAKICGVDIIVPRETIDRDKHAIIELNFNPAMHMHCFPYQGEQKKIGDKILDFLFE |
Interaction
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-354 | Glutamate--cysteine ligase | ||||
Sequence: MIKLDMTILDSLKENKALRKLLFSGHFGLEKENIRVTSDGKLALTPHPAIFGPKEDNPYIKTDFSESQIEMITPVTDSIDDVYNWLENLHNIVSLRSKNELLWPSSNPPILPAEKDIPIAEYKTPDSPDRKYREHLAQGYGKKIQLLSGIHYNFSFPEALIDGLYDEISLPNESKRDFKNRLYLKVAKYFMKNRWLLIYLTGASPVYLADFTKTKQEEKLRDGSSALHDGISLRNSNAGYKNKESLYVDYNSFDAYISSISNYIEAGKIESMREFYNPIRLKNAHTDQTVESLAKHGVEYLEIRSIDLNPLEPNGISKEALHFIHLFLIKGLLSEDRELCENNQQLADENENNI | ||||||
Domain | 521-775 | ATP-grasp | ||||
Sequence: KLVLAENNIRVPFGDSFSDQALALEAFSLFKDKQIVVKPKSTNYGWGISIFKNKFTTEDYQEALNIAFSYDSSVIIEEFIPGDEFRFLVINDKVEAVLKRVPANVTGDGIHTVRELVEEKNMDPLRGTDHLKPLEKIRTGPEETLMLSMQKLSWDSIPKANETIYLRENSNVSTGGDSIDYTAEMDDYFKEIAIRATQVLDAKICGVDIIVPRETIDRDKHAIIELNFNPAMHMHCFPYQGEQKKIGDKILDFLF |
Sequence similarities
In the N-terminal section; belongs to the glutamate--cysteine ligase type 1 family. Type 2 subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length776
- Mass (Da)88,615
- Last updated2006-11-28 v1
- Checksum9DDA45402F88588D
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AM263198 EMBL· GenBank· DDBJ | CAK22135.1 EMBL· GenBank· DDBJ | Genomic DNA |