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Q5M3J8 (GSHAB_STRT2) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 65. 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:stu1413
OrganismStreptococcus thermophilus (strain ATCC BAA-250 / LMG 18311) [Complete proteome] [HAMAP]
Taxonomic identifier264199 [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_0000192562

Regions

Domain488 – 746259ATP-grasp
Nucleotide binding515 – 57359ATP By similarity
Region1 – 332332Glutamate--cysteine ligase HAMAP-Rule MF_00782

Sites

Metal binding6951Magnesium or manganese 1 By similarity
Metal binding7161Magnesium or manganese 1 By similarity
Metal binding7161Magnesium or manganese 2 By similarity
Metal binding7181Magnesium or manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5M3J8 [UniParc].

Last modified February 1, 2005. Version 1.
Checksum: 5D0856B57EDFA2EF

FASTA75485,167
        10         20         30         40         50         60 
MTLNQLLQKL EATSPILQAN FGIERESLRV DRQGQLVHTP HPSCLGARSF HPYIQTDFCE 

        70         80         90        100        110        120 
FQMELITPVA KSTTEARRFL GAITDVAGRS IATDEVLWPL SMPPRLKAEE IQVAQLENDF 

       130        140        150        160        170        180 
ERHYRNYLAE KYGTKLQAIS GIHYNMELGK DLVEALFQES DQTDMIAFKN ALYLKLAQNY 

       190        200        210        220        230        240 
LRYRWVITYL FGASPIAEQG FFDQEVPEPM RSFRNSDHGY VNKEEIQVSF VSLEDYVSAI 

       250        260        270        280        290        300 
ETYIEQGDLI AEKEFYSAVR FRGQKVNRSF LDKGITYLEF RNFDLNPFER IGISQTTMDT 

       310        320        330        340        350        360 
VHLLILAFLW LDSPENVDQA LAQGHALNEK IALSHPLEPL PSEAKTQDIV TALDQLVQHF 

       370        380        390        400        410        420 
GLGDYHQDLV KQVKAAFADP NQTLSAQLLP YIKDKSLAEF ALNKALAYHD YDWTAHYALK 

       430        440        450        460        470        480 
GYEEMELSTQ MLLFDAIQKG IHFEILDEQD QFLKLWHQDH VEYVKNGNMT SKDNYVVPLA 

       490        500        510        520        530        540 
MANKTVTKKI LADASFPVPS GDEFTSLEEG LAYYPLIKDK QIVVKPKSTN FGLGISIFQE 

       550        560        570        580        590        600 
PASLDNYQKA LEIAFAEDTS VLVEEFIPGT EYRFFILDGR CEAVLLRVAA NVIGDGKHTI 

       610        620        630        640        650        660 
RELVAQKNAN PLRGRDHRSP LEIIELGDIE QLMLAQQGYT PDDILPEGKK VNLRRNSNIS 

       670        680        690        700        710        720 
TGGDSIDVTE TMDSSYQELA AAMATSMGAW ACGVDLIIPD ETQIATKENP HCTCIELNFN 

       730        740        750 
PSMYMHTYCA EGPGQAITTK ILDKLFPEIV AGQT 

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References

[1]"Complete sequence and comparative genome analysis of the dairy bacterium Streptococcus thermophilus."
Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D., Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M., Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D., Hancy F. expand/collapse author list , Burteau S., Boutry M., Delcour J., Goffeau A., Hols P.
Nat. Biotechnol. 22:1554-1558(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-250 / LMG 18311.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000023 Genomic DNA. Translation: AAV61026.1.
RefSeqYP_139841.1. NC_006448.1.

3D structure databases

ProteinModelPortalQ5M3J8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING264199.stu1413.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV61026; AAV61026; stu1413.
GeneID3165343.
KEGGstl:stu1413.
PATRIC19804374. VBIStrThe97850_1388.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycSTHE264199:GI6K-1366-MONOMER.
UniPathwayUPA00142; UER00209.
UPA00142; UER00210.

Family and domain databases

Gene3D3.30.470.20. 1 hit.
HAMAPMF_00782. Glut_biosynth.
InterProIPR011761. ATP-grasp.
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_STRT2
AccessionPrimary (citable) accession number: Q5M3J8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: February 1, 2005
Last modified: February 19, 2014
This is version 65 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