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Q82ZG8 (GSHAB_ENTFA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 80. 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:EF_3089
OrganismEnterococcus faecalis (strain ATCC 700802 / V583) [Reference proteome] [HAMAP]
Taxonomic identifier226185 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesEnterococcaceaeEnterococcus

Protein attributes

Sequence length756 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. HAMAP-Rule MF_00782

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 – 756756Glutathione biosynthesis bifunctional protein GshAB HAMAP-Rule MF_00782
PRO_0000192551

Regions

Domain493 – 751259ATP-grasp
Nucleotide binding520 – 57859ATP By similarity
Region1 – 338338Glutamate--cysteine ligase HAMAP-Rule MF_00782

Sites

Metal binding7001Magnesium or manganese 1 By similarity
Metal binding7211Magnesium or manganese 1 By similarity
Metal binding7211Magnesium or manganese 2 By similarity
Metal binding7231Magnesium or manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q82ZG8 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: D282F6561A9D07A4

FASTA75687,212
        10         20         30         40         50         60 
MNYRELMQKK NVRPYVLMAR FGLEKENQRS TREGLLATTE HPTVFGNRSY HPYIQTDFSE 

        70         80         90        100        110        120 
TQLELITPVA NSGTEMLRFL DAIHDVARRS IPEDEMLWPL SMPPQLPTKD EEIKIAKLDQ 

       130        140        150        160        170        180 
YDAVLYRRYL AKEYGKRKQM VSGIHFNFEY DQALIQQLYD EQSEVTDCKQ FKTKVYMKVA 

       190        200        210        220        230        240 
RNFLRYRWLI TYLFGASPVS EDRYFRVYDD QPQEPVRSIR NSTYGYRNHD NVKVSYASLE 

       250        260        270        280        290        300 
RYLEDIHRMV ENGLLSEEKE FYAPVRLRGG KQMSDLPKTG IRYIELRNLD LNPFSRLGIV 

       310        320        330        340        350        360 
EDTVDFLHYF MLYLLWTDEK EEADEWVKTG DIFNEQVALG HPHETIKLIA EGDRIFSEMI 

       370        380        390        400        410        420 
DMLDALGIRK GKEVVGKYYQ QLRNPQDTVS GKMWTIIQEN SNSELGNIFG NQYQSMAFER 

       430        440        450        460        470        480 
PYQLAGFREM ELSTQIFLFD AIQKGLEIEI LDEQEQFLKL QHGEHIEYVK NANMTSKDNY 

       490        500        510        520        530        540 
VVPLIMENKT VTKKILSAAG FHVPGGEEFS SFIEAQEAHL RYANKAFVVK PKSTNYGLGI 

       550        560        570        580        590        600 
TIFKEGASLE DFTEALRIAF KEDTAVLIEE FLPGTEYRFF VLDNDVKAIM LRVPANVTGD 

       610        620        630        640        650        660 
GKHTVEELVA AKNSDPLRGT NHRAPLELIQ LNDLEKLMLK EQGLTIYSVP EKEQIVYLRE 

       670        680        690        700        710        720 
NSNVSTGGDS IDMTDVIDDS YKQIAIEAVA ALGAKICGID LIIPDKDVKG TRDSLTYGII 

       730        740        750 
EANFNPAMHM HVYPYAGQGR RLTMDVLKLL YPEVVQ 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016830 Genomic DNA. Translation: AAO82770.1.
RefSeqNP_816700.1. NC_004668.1.

3D structure databases

ProteinModelPortalQ82ZG8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING226185.EF3089.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO82770; AAO82770; EF_3089.
GeneID1201934.
KEGGefa:EF3089.
PATRIC21856337. VBIEntFae7065_2881.

Phylogenomic databases

eggNOGCOG1181.
KOK01919.
OMARYLAKEY.
OrthoDBEOG6BKJ7H.

Enzyme and pathway databases

BioCycEFAE226185:GHI1-3016-MONOMER.
UniPathwayUPA00142; UER00209.
UPA00142; UER00210.

Family and domain databases

Gene3D3.30.1490.20. 1 hit.
3.30.470.20. 3 hits.
HAMAPMF_00782. Glut_biosynth.
InterProIPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR007370. Glu_cys_ligase.
IPR006335. Glut_biosynth.
[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_ENTFA
AccessionPrimary (citable) accession number: Q82ZG8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: June 1, 2003
Last modified: May 14, 2014
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways