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Q8DW15 (GSHAB_STRMU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 81. 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:SMU_267c
OrganismStreptococcus mutans serotype c (strain ATCC 700610 / UA159) [Complete proteome] [HAMAP]
Taxonomic identifier210007 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length754 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 – 754754Glutathione biosynthesis bifunctional protein GshAB HAMAP-Rule MF_00782
PRO_0000192560

Regions

Domain489 – 752264ATP-grasp
Nucleotide binding516 – 57459ATP By similarity
Region1 – 333333Glutamate--cysteine ligase HAMAP-Rule MF_00782

Sites

Metal binding6961Magnesium or manganese 1 By similarity
Metal binding7171Magnesium or manganese 1 By similarity
Metal binding7171Magnesium or manganese 2 By similarity
Metal binding7191Magnesium or manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8DW15 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 103479A8536A10CB

FASTA75486,187
        10         20         30         40         50         60 
MHINQLLQHA NSDLPLLQAN FGLERESLRI NKTNHRLAQT PHPTALGSRQ FHPYIQTDYS 

        70         80         90        100        110        120 
ESQMELITPV AHSSKEVLRF LGAITDVAER SIDQNQYLWP LSMPPQITED EIEIAQLEDD 

       130        140        150        160        170        180 
FEFSYRQYLD KKYGKILQSI SGIHYNMELG ADLMNELFEL SGYQSFIDFK NDLYLKVAQN 

       190        200        210        220        230        240 
FLNYRWFLTY LYGASPLAEK GFLNEELSQT VRSIRNSHLG YVNTDDIKVP FDSLENYISS 

       250        260        270        280        290        300 
IEHYVKSGAL SAEKEFYSAV RLRGSKHNRD YLTKGITYLE FRCFDLNPFN NRGITQETID 

       310        320        330        340        350        360 
SVHLFILAML WLDTPKKLNQ ALDKAQKLND KIALSHPLEK LPKENSASLI IEAMEALIKH 

       370        380        390        400        410        420 
FKLPSYYDDL LIAIKKQVEN PKLTLSGRLF EHIKHASLEH FGQKKGQDYH NYAWQNYYAL 

       430        440        450        460        470        480 
KGYENMELST QMLLFDTIQK GIHFEILDEN DQFLKLWHND HIEYVKNGNM TSKDNYVIPL 

       490        500        510        520        530        540 
AMANKVVTKK ILRENGYPVP AGAEFDNKDE ALRYYSQIKN KPIVVKPKTT NFGLGISIFE 

       550        560        570        580        590        600 
TAASHNDYEK ALDIAFIEDY SVLVEEFIPG TEYRFFILDG KCEAVLLRVA ANVVGDGHST 

       610        620        630        640        650        660 
VRQLVAQKNR DPLRGREHRS PLEIIDLGDI ELLMLQQEGY TLEDILPKGK KVNLRGNSNI 

       670        680        690        700        710        720 
STGGDSIDVT ETMDPSYKQL AANMATAMGA WVCGVDLIIP DTNLKASKGK PNCTCIELNF 

       730        740        750 
NPSMYMHTYC YQGPGQVITG KILAKLFPEI STKI 

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References

[1]"Genome sequence of Streptococcus mutans UA159, a cariogenic dental pathogen."
Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B., Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S., Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.
Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700610 / UA159.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014133 Genomic DNA. Translation: AAN58035.1.
RefSeqNP_720729.1. NC_004350.2.

3D structure databases

ProteinModelPortalQ8DW15.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING210007.SMU.267c.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN58035; AAN58035; SMU_267c.
GeneID1027852.
KEGGsmu:SMU_267c.
PATRIC19662795. VBIStrMut61772_0233.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1181.
KOK01919.
OMAPYIQTDF.
OrthoDBEOG6BKJ7H.
ProtClustDBPRK02471.

Enzyme and pathway databases

BioCycSMUT210007:GC7Z-281-MONOMER.
UniPathwayUPA00142; UER00209.
UPA00142; UER00210.

Family and domain databases

Gene3D3.30.1490.20. 1 hit.
HAMAPMF_00782. Glut_biosynth.
InterProIPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
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_STRMU
AccessionPrimary (citable) accession number: Q8DW15
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: March 1, 2003
Last modified: February 19, 2014
This is version 81 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