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A0AMA3 (GSHAB_LISW6) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 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:lwe2717
OrganismListeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 / SLCC5334) [Complete proteome] [HAMAP]
Taxonomic identifier386043 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria

Protein attributes

Sequence length776 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 – 776776Glutathione biosynthesis bifunctional protein GshAB HAMAP-Rule MF_00782
PRO_1000133720

Regions

Domain521 – 775255ATP-grasp
Nucleotide binding548 – 60659ATP By similarity
Region1 – 354354Glutamate--cysteine ligase HAMAP-Rule MF_00782

Sites

Metal binding7281Magnesium or manganese 1 By similarity
Metal binding7451Magnesium or manganese 1 By similarity
Metal binding7451Magnesium or manganese 2 By similarity
Metal binding7471Magnesium or manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
A0AMA3 [UniParc].

Last modified November 28, 2006. Version 1.
Checksum: 9DDA45402F88588D

FASTA77688,615
        10         20         30         40         50         60 
MIKLDMTILD SLKENKALRK LLFSGHFGLE KENIRVTSDG KLALTPHPAI FGPKEDNPYI 

        70         80         90        100        110        120 
KTDFSESQIE MITPVTDSID DVYNWLENLH NIVSLRSKNE LLWPSSNPPI LPAEKDIPIA 

       130        140        150        160        170        180 
EYKTPDSPDR KYREHLAQGY GKKIQLLSGI HYNFSFPEAL IDGLYDEISL PNESKRDFKN 

       190        200        210        220        230        240 
RLYLKVAKYF MKNRWLLIYL TGASPVYLAD FTKTKQEEKL RDGSSALHDG ISLRNSNAGY 

       250        260        270        280        290        300 
KNKESLYVDY NSFDAYISSI SNYIEAGKIE SMREFYNPIR LKNAHTDQTV ESLAKHGVEY 

       310        320        330        340        350        360 
LEIRSIDLNP LEPNGISKEA LHFIHLFLIK GLLSEDRELC ENNQQLADEN ENNIALNGLS 

       370        380        390        400        410        420 
KPAIKNCDNE EMALADAGLL ELDKMNDFIQ SLRPEDTYFQ AIIEKQKERL LHPEKTIAAQ 

       430        440        450        460        470        480 
VKEQSATAGF IEFHLNQAKT YMEETEALAY KLIGAEDMEL STQIIWKDAI ARGIKVDVLD 

       490        500        510        520        530        540 
RAENFLRFQK GDHVEYVKQA SKTSKDNYVS VLMMENKVVT KLVLAENNIR VPFGDSFSDQ 

       550        560        570        580        590        600 
ALALEAFSLF KDKQIVVKPK STNYGWGISI FKNKFTTEDY QEALNIAFSY DSSVIIEEFI 

       610        620        630        640        650        660 
PGDEFRFLVI NDKVEAVLKR VPANVTGDGI HTVRELVEEK NMDPLRGTDH LKPLEKIRTG 

       670        680        690        700        710        720 
PEETLMLSMQ KLSWDSIPKA NETIYLRENS NVSTGGDSID YTAEMDDYFK EIAIRATQVL 

       730        740        750        760        770 
DAKICGVDII VPRETIDRDK HAIIELNFNP AMHMHCFPYQ GEQKKIGDKI LDFLFE 

« Hide

References

[1]"Whole-genome sequence of Listeria welshimeri reveals common steps in genome reduction with Listeria innocua as compared to Listeria monocytogenes."
Hain T., Steinweg C., Kuenne C.T., Billion A., Ghai R., Chatterjee S.S., Domann E., Kaerst U., Goesmann A., Bekel T., Bartels D., Kaiser O., Meyer F., Puehler A., Weisshaar B., Wehland J., Liang C., Dandekar T. expand/collapse author list , Lampidis R., Kreft J., Goebel W., Chakraborty T.
J. Bacteriol. 188:7405-7415(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35897 / DSM 20650 / SLCC5334.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM263198 Genomic DNA. Translation: CAK22135.1.
RefSeqYP_850914.1. NC_008555.1.

3D structure databases

ProteinModelPortalA0AMA3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING386043.lwe2717.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAK22135; CAK22135; lwe2717.
GeneID4466025.
KEGGlwe:lwe2717.
PATRIC20332701. VBILisWel39304_2724.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1181.
HOGENOMHOG000156471.
KOK01919.
OMAHVEYVKN.
OrthoDBEOG6BKJ7H.

Enzyme and pathway databases

BioCycLWEL386043:GI5X-2800-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_LISW6
AccessionPrimary (citable) accession number: A0AMA3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: November 28, 2006
Last modified: May 14, 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