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Q8Y3R3 (GSHAB_LISMO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 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:lmo2770
OrganismListeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e) [Reference proteome] [HAMAP]
Taxonomic identifier169963 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria

Protein attributes

Sequence length769 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Synthesizes glutathione from L-glutamate and L-cysteine via gamma-L-glutamyl-L-cysteine. 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 CAD00983.1 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_0000192555

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
Q8Y3R3 [UniParc].

Last modified July 5, 2005. Version 2.
Checksum: B60DA05A3D8B43FD

FASTA76987,728
        10         20         30         40         50         60 
MLDSFKEDPN LRKLLFSGHF GLEKENIRVT SDGKLALTPH PAIFGPKEDN PYIKTDFSES 

        70         80         90        100        110        120 
QIEMITPVTD SIDSVYEWLE NLHNIVSLRS ENELLWPSSN PPILPAEEDI PIAEYKTPDS 

       130        140        150        160        170        180 
PDRKYREHLA KGYGKKIQLL SGIHYNFSFP EALIDGLYAN ISLPEESKQD FKNRLYLKVA 

       190        200        210        220        230        240 
KYFMKNRWLL IYLTGASPVY LADFSKTKHE ESLPDGSSAL RDGISLRNSN AGYKNKEALF 

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

       310        320        330        340        350        360 
LNPLEPNGIS KDELDFIHLF LIKGLLSEDR ELCANNQQLA DENENNIALN GLAQPSIKNC 

       370        380        390        400        410        420 
DNEDIPLADA GLLELDKMSD FIKSLRPEDT KLRAIIEKQK ERLLHPEKTI AAQVKQQVTK 

       430        440        450        460        470        480 
EGYVDFHLNQ AKTYMEETEA LAYKLIGAED MELSTQIIWK DAIARGIKVD VLDRAENFLR 

       490        500        510        520        530        540 
FQKGDHIEYV KQASKTSKDN YVSVLMMENK VVTKLVLAEH DIRVPFGDSF SDQALALEAF 

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

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

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

       730        740        750        760 
DIIVPRETID RDKHAIIELN FNPAMHMHCF PYQGEQKKIG DKILDFLFD 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL591984 Genomic DNA. Translation: CAD00983.1. Different initiation.
PIRAI1420.
RefSeqNP_466292.1. NC_003210.1.

3D structure databases

ProteinModelPortalQ8Y3R3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING169963.lmo2770.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD00983; CAD00983; CAD00983.
GeneID986798.
KEGGlmo:lmo2770.
PATRIC20314847. VBILisMon69206_2839.

Organism-specific databases

GenoListLMO2770.

Phylogenomic databases

eggNOGCOG1181.
HOGENOMHOG000156471.
KOK01919.
OrthoDBEOG6BKJ7H.

Enzyme and pathway databases

BioCycLMON169963:LMO2770-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.
IPR020561. PRibGlycinamid_synth_ATP-grasp.
[Graphical view]
PfamPF01071. GARS_A. 1 hit.
PF04262. 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_LISMO
AccessionPrimary (citable) accession number: Q8Y3R3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: July 5, 2005
Last modified: May 14, 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