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Q926X7 (GSHAB_LISIN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 76. 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:lin2913
OrganismListeria innocua serovar 6a (strain CLIP 11262) [Complete proteome] [HAMAP]
Taxonomic identifier272626 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria

Protein attributes

Sequence length769 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 caution

The sequence CAC98138.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 769769Glutathione biosynthesis bifunctional protein GshAB HAMAP-Rule MF_00782
PRO_0000192553

Regions

Domain514 – 768255ATP-grasp
Nucleotide binding541 – 59959ATP By similarity
Region1 – 347347Glutamate--cysteine ligase HAMAP-Rule MF_00782

Sites

Metal binding7211Magnesium 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
Q926X7 [UniParc].

Last modified July 5, 2005. Version 2.
Checksum: 70EBC5926351E309

FASTA76987,659
        10         20         30         40         50         60 
MLDSFKENEA LRKYLFSGHF GLEKENIRVT SDGKLALTPH PAIFGPKEDN PYIKTDFSES 

        70         80         90        100        110        120 
QIEMITPVTD SIDAVYEWLE NLHNIVSLRA ENELLWPSSN PPILPAEEDI PIAEYKTPDS 

       130        140        150        160        170        180 
PDRKYREHLA KGYGKKIQLL SGIHYNFSFP EALIDGLYAE ISHPNESKRD FKNRLYLKVA 

       190        200        210        220        230        240 
KYFMKNRWLL IYLTGASPVY LADFTKTNSE EVLNDGSKAL HRGISLRNSN AGYKNKESLF 

       250        260        270        280        290        300 
VDYNSFDAYI SSISNYIEAG KIESMREFYN PIRLKNAHTD QTVESLAKHG VEYLEIRSID 

       310        320        330        340        350        360 
LNPLEPNGIS KDELIFIHLF LIKGLLSEDR ELCANNQQLA DENENNIALN GLAQPAIKNC 

       370        380        390        400        410        420 
DNEEMSLADA GLLELDKMSD FIQSLIPNDN HFQAIIEKQK ERLLHPEKTI AAQVQAQSAK 

       430        440        450        460        470        480 
EGYVEFHLNQ AKTYMEETEA LAYKLVGAED MELSTQIIWK DAIARGIKVD VLDRAENFLR 

       490        500        510        520        530        540 
FQKGDHVEYV KQASKTSKDN YVSVLMMENK VVTKLVLAEH GIRVPFGDSF SDQALALEAF 

       550        560        570        580        590        600 
SLFEDKQIVV KPKSTNYGWG ISIFKNKFTL EDYQEALNIA FSYDSSVIIE EFIPGDEFRF 

       610        620        630        640        650        660 
LVINDKVEAV LKRVPANVTG DGIHTVRQLV EEKNTDPLRG TDHLKPLEKI RTGPEETLML 

       670        680        690        700        710        720 
SMQNLSWDSI PKAEEIIYLR ENSNVSTGGD SIDYTEEMDD YFKEIAIRAT QVLDAKICGV 

       730        740        750        760 
DIIVPRETID RDKHAIIELN FNPAMHMHCF PYQGEKKKIG DKILDFLFE 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL596174 Genomic DNA. Translation: CAC98138.1. Different initiation.
PIRAB1796.
RefSeqNP_472240.1. NC_003212.1.

3D structure databases

ProteinModelPortalQ926X7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272626.lin2913.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC98138; CAC98138; CAC98138.
GeneID1131790.
KEGGlin:lin2913.
PATRIC20302766. VBILisInn102668_2988.

Organism-specific databases

GenoListLIN2913.
CMRSearch...

Phylogenomic databases

eggNOGCOG1181.
HOGENOMHOG000156471.
KOK01919.
OrthoDBEOG6BKJ7H.
ProtClustDBPRK02471.

Enzyme and pathway databases

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_LISIN
AccessionPrimary (citable) accession number: Q926X7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: July 5, 2005
Last modified: February 19, 2014
This is version 76 of the entry and version 2 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