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Q6ANW2 (GSHAB_DESPS) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:DP1233
OrganismDesulfotalea psychrophila (strain LSv54 / DSM 12343) [Complete proteome] [HAMAP]
Taxonomic identifier177439 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfobacteralesDesulfobulbaceaeDesulfotalea

Protein attributes

Sequence length779 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 – 779779Glutathione biosynthesis bifunctional protein GshAB HAMAP-Rule MF_00782
PRO_0000192550

Regions

Domain512 – 768257ATP-grasp
Nucleotide binding539 – 59759ATP By similarity
Region1 – 346346Glutamate--cysteine ligase HAMAP-Rule MF_00782

Sites

Metal binding7191Magnesium or manganese 1 By similarity
Metal binding7381Magnesium or manganese 1 By similarity
Metal binding7381Magnesium or manganese 2 By similarity
Metal binding7401Magnesium or manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6ANW2 [UniParc].

Last modified September 13, 2004. Version 1.
Checksum: 1985FBD93F20889E

FASTA77989,336
        10         20         30         40         50         60 
MAFSKNILDS LPPLISKQIF EGFFGFEKEN IRVDSRGKLA LTPHPRELGE KTSHPYITTD 

        70         80         90        100        110        120 
FSESQIEIIT PPLPSIAESL GFLETLHDLV SIELKDEYLW PQSAPPILPE REEDIPIAHF 

       130        140        150        160        170        180 
GGEFREQEEY RLQLAKIYGR KRQMFSGIHF NISLPERFLE LLHEEGKQEQ PFAEFREDIY 

       190        200        210        220        230        240 
MKTVRNFLRH RWFLICLLGA SPVIHKSYRK HCIDMLSPFA KDAYHFPYAT SIRNNICGYR 

       250        260        270        280        290        300 
NTQDFHLNYS TLTDYRESLQ ELVEKKVLRD IRENYAPIRI KTTTDPKRIN HLEIRLLDLN 

       310        320        330        340        350        360 
PFFKTGVNPL HAEIIHIFLI YCLLCPEETS FTSKEQETAN RNQEQAATEG LNPGAIICDA 

       370        380        390        400        410        420 
DGNEQRLDKQ LAHCLQEIQQ TVSPHLPPEY RAGMEELERL VQNQASRPTD TLLKEIKQEG 

       430        440        450        460        470        480 
FTEWHMKQAL KFLKKSHDEQ FIFHGLRDME LSTQLLLRRA ALRGVSFEIM DRQENFVCLE 

       490        500        510        520        530        540 
QAGKREYVMQ ASRTSLDNYI SVLSMENKVI TKKILDQAGI NTPKGRSYSS PSEALADYPY 

       550        560        570        580        590        600 
YRGRAIVIKP KSTNFGIGIT IIKENNRHDF FAQGIAQAFK HEATVLIENF SSGKEYRFFI 

       610        620        630        640        650        660 
VNDQVVGILH RVPANVTGDG TSSVQVLVTE KNKNPLRGRG YRTPLEKIKL EETEEMFLAS 

       670        680        690        700        710        720 
QGYSFATVPA KDQRIYLREN SNISTGGDSI DFTDKVPQSY KDIAVRAAQA LQVKITGLDM 

       730        740        750        760        770 
MIDSLEEDAA EDNFSIIELN FNPAIHIHCH PYIGKNRHLD DKILDALGFT GAEEAGEKA 

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References

[1]"The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from permanently cold Arctic sediments."
Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., Bauer M., Zibat A., Lombardot T., Becker I., Amann J., Gellner K., Teeling H., Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R., Klenk H.-P.
Environ. Microbiol. 6:887-902(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LSv54 / DSM 12343.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR522870 Genomic DNA. Translation: CAG35962.1.
RefSeqYP_064969.1. NC_006138.1.

3D structure databases

ProteinModelPortalQ6ANW2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING177439.DP1233.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAG35962; CAG35962; DP1233.
GeneID2944854.
KEGGdps:DP1233.
PATRIC21712227. VBIDesPsy67261_1331.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1181.
HOGENOMHOG000156471.
KOK01919.
OMAPYIQTDF.
OrthoDBEOG6BKJ7H.
ProtClustDBPRK02471.

Enzyme and pathway databases

BioCycDPSY177439:GJW5-1272-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.
IPR013651. ATP-grasp_RimK-type.
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.
PF08443. RimK. 1 hit.
[Graphical view]
PROSITEPS50975. ATP_GRASP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGSHAB_DESPS
AccessionPrimary (citable) accession number: Q6ANW2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: September 13, 2004
Last modified: February 19, 2014
This is version 59 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