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Q8E399 (GSHAB_STRA3) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Glutathione biosynthesis bifunctional protein GshAB
Alternative name(s):
Gamma-GCS-GS
Short name=GCS-GS

Including the following 2 domains:

  1. Glutamate--cysteine ligase
    EC=6.3.2.2
    Alternative name(s):
    Gamma-ECS
    Short name=GCS
    Gamma-glutamylcysteine synthetase
  2. Glutathione synthetase
    EC=6.3.2.3
    Alternative name(s):
    GSH synthetase
    Short name=GS
    Short name=GSH-S
    Short name=GSHase
    Glutathione synthase
Gene names
Name:gshAB
Synonyms:gshF
Ordered Locus Names:gbs1862
OrganismStreptococcus agalactiae serotype III (strain NEM316) [Complete proteome] [HAMAP]
Taxonomic identifier211110 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Streptococcus ›

Protein attributes

Sequence length750 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Synthesizes glutathione from L-glutamate and L-cysteine via gamma-L-glutamyl-L-cysteine By similarity. HAMAP-Rule MF_00782

Catalytic activity

ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine. HAMAP-Rule MF_00782

ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione. HAMAP-Rule MF_00782

Cofactor

Binds 2 magnesium or manganese ions per subunit By similarity.

Pathway

Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 1/2. HAMAP-Rule MF_00782

Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 2/2.

Subunit structure

Monomer By similarity.

Sequence similarities

In the N-terminal section; belongs to the glutamate--cysteine ligase type 1 family. Type 2 subfamily.

Contains 1 ATP-grasp domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 750750Glutathione biosynthesis bifunctional protein GshAB HAMAP-Rule MF_00782
PRO_0000192558

Regions

Domain489 – 747259ATP-grasp
Nucleotide binding516 – 57459ATP By similarity
Region1 – 333333Glutamate--cysteine ligase HAMAP-Rule MF_00782

Sites

Metal binding6961Magnesium or manganese 1 By similarity
Metal binding7171Magnesium or manganese 1 By similarity
Metal binding7171Magnesium or manganese 2 By similarity
Metal binding7191Magnesium or manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8E399 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 97829C2C5B44174A

FASTA75085,603
        10         20         30         40         50         60 
MIIDRLLQRS HSHLPILQAT FGLERESLRI HQPTQRVAQT PHPKTLGSRN YHPYIQTDYS 

        70         80         90        100        110        120 
EPQLELITPI AKDSQEAIRF LKAISDVAGR SINHDEYLWP LSMPPKVREE DIQIAQLEDA 

       130        140        150        160        170        180 
FEYDYRKYLE KTYGKLIQSI SGIHYNLGLG QELLTSLFEL SQADNAIDFQ NQLYMKLSQN 

       190        200        210        220        230        240 
FLRYRWLLTY LYGASPVAEE DFLDQKLNNP VRSLRNSHLG YVNHKDIRIS YTSLKDYVND 

       250        260        270        280        290        300 
LENAVKSGQL IAEKEFYSPV RLRGSKACRN YLEKGITYLE FRTFDLNPFS PIGITQETVD 

       310        320        330        340        350        360 
TVHLFLLALL WIDSSSHIDQ DIKEANRLND LIALSHPLEK LPNQAPVSDL VDAMQSVIQH 

       370        380        390        400        410        420 
FNLSPYYQDL LESVKRQIQS PELTVAGQLL EMIEGLSLET FGQRQGQIYH DYAWEAPYAL 

       430        440        450        460        470        480 
KGYETMELST QLLLFDVIQK GVNFEVLDEQ DQFLKLWHNS HIEYVKNGNM TSKDNYIVPL 

       490        500        510        520        530        540 
AMANKVVTKK ILDEKHFPTP FGDEFTDRKE ALNYFSQIQD KPIVVKPKST NFGLGISIFK 

       550        560        570        580        590        600 
TSANLASYEK AIDIAFTEDS AILVEEYIEG TEYRFFVLEG DCIAVLLRVA ANVVGDGIHT 

       610        620        630        640        650        660 
ISQLVKLKNQ NPLRGYDHRS PLEVIELGEV EQLMLEQQGY TVNSIPPEGT KIELRRNSNI 

       670        680        690        700        710        720 
STGGDSIDVT NTMDPTYKQL AAEMAEAMGA WVCGVDLIIP NATQAYSKDK KNATCIELNF 

       730        740        750 
NPLMYMHTYC QEGPGQSITP RILAKLFPEL

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References

[1]"Genome sequence of Streptococcus agalactiae, a pathogen causing invasive neonatal disease."
Glaser P., Rusniok C., Buchrieser C., Chevalier F., Frangeul L., Msadek T., Zouine M., Couve E., Lalioui L., Poyart C., Trieu-Cuot P., Kunst F.
Mol. Microbiol. 45:1499-1513(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NEM316.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL766854 Genomic DNA. Translation: CAD47521.1.
RefSeqNP_736296.1. NC_004368.1.

3D structure databases

ProteinModelPortalQ8E399.
ModBaseSearch...

Protein-protein interaction databases

STRING211110.gbs1862.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD47521; CAD47521; CAD47521.
GeneID1030947.
KEGGsan:gbs1862.
PATRIC19639645. VBIStrAga3577_1909.

Organism-specific databases

GenoListgbs1862.
CMRSearch...

Phylogenomic databases

eggNOGCOG1181.
HOGENOMHOG000156471.
KOK01919.
OMAPYIQTDF.
ProtClustDBPRK02471.

Enzyme and pathway databases

UniPathwayUPA00142; UER00209.
UPA00142; UER00210.

Family and domain databases

Gene3D3.30.470.20. 1 hit.
HAMAPMF_00782. Glut_biosynth.
InterProIPR011761. ATP-grasp.
IPR013816. ATP_grasp_subdomain_2.
IPR007370. Glu_cys_ligase.
IPR006335. Glut_cys-rel.
[Graphical view]
PfamPF04262. Glu_cys_ligase. 1 hit.
[Graphical view]
TIGRFAMsTIGR01435. glu_cys_lig_rel. 1 hit.
PROSITEPS50975. ATP_GRASP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGSHAB_STRA3
AccessionPrimary (citable) accession number: Q8E399
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: March 1, 2003
Last modified: May 1, 2013
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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