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Reviewed, UniProtKB/Swiss-Prot Q5PF10 (GSH1_SALPA)

Last modified June 16, 2009. Version 22. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Glutamate--cysteine ligase
    EC=6.3.2.2
Alternative name(s):
    Gamma-glutamylcysteine synthetase
    Gamma-ECS
      Short name=GCS
Gene names
Name: gshA
Ordered Locus Names: SPA2677
OrganismSalmonella paratyphi A [Complete proteome] [HAMAP]
Taxonomic identifier54388 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length518 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine. HAMAP MF_00578

Pathway

Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 1/2. HAMAP MF_00578

Sequence similarities

Belongs to the glutamate--cysteine ligase type 1 family. Type 1 subfamily.

Ontologies

Keywords
   Biological processGlutathione biosynthesis
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processglutathione biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

glutamate-cysteine ligase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 518518Glutamate--cysteine ligase HAMAP MF_00578
PRO_0000192537

Sequences

Sequence LengthMass (Da)Tools
Q5PF10-1 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: 9766882B28965C47

FASTA51858,384
        10         20         30         40         50         60 
MIPDVSQALA WLEKHPQALK GIQRGLERET LRVNADGTLA TTGHPEALGS ALTHKWITTD 

        70         80         90        100        110        120 
FAEALLEFIT PVDGDIQHML TFMRDLHRYT ARKLGDERMW PLSMPCYIAE GQDIELAQYG 

       130        140        150        160        170        180 
TSNTGRFKTL YREGLKNRYG ALMQTISGVH YNFSLPMAFW QAKCGVTEGE AAKEKISAGY 

       190        200        210        220        230        240 
FRLIRNYYRF GWVIPYLFGA SPAICSSFLQ GKPTTLPFEK TDCGMYYLPY ATSLRLSDLG 

       250        260        270        280        290        300 
YTNKSQSNLG ITFNDLHEYV AGLKRAIKTP SEEYARIGVE KDGKRLQINS NVLQIENELY 

       310        320        330        340        350        360 
APIRPKRVTR SGESPSDALL RGGIEYIEVR SLDINPFSPI GVDEQQVRFL DLFMVWCVLA 

       370        380        390        400        410        420 
DAPEMSSDEL LCTRTNWNRV ILEGRKPGLT LGIGCETAQF PLPKVGKDLF RDLKRVAQTL 

       430        440        450        460        470        480 
DSIHGGEEYQ KVCDELVACF DNPELTFSAR ILRSMIDEGI GGTGKAFGEA YRNLLREEPL 

       490        500        510 
EILQEEEFIA ERDASVRRQQ EIEAADTEPF AAWLAKHA 

« Hide

References

[1]"Comparison of genome degradation in Paratyphi A and Typhi, human-restricted serovars of Salmonella enterica that cause typhoid."
McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S., Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R., Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F. expand/collapse author list , Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W., Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M., Warren W., Florea L., Spieth J., Wilson R.K.
Nat. Genet. 36:1268-1274(2004) [PubMed: 15531882] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 9150 / SARB42.

Cross-references

Sequence databases

CP000026 Genomic DNA. Translation: AAV78538.1.
RefSeqYP_151850.1.

3D structure databases

SMRQ5PF10. Positions 1-514.
ModBaseSearch...

Genome annotation databases

GeneID3177337.
GenomeReviewsGene locus SPA2677 in contig CP000026_GR.
KEGGspt:SPA2677.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ5PF10.
OMAQ5PF10. EYIEVRA.

Enzyme and pathway databases

BioCycSENT295319:SPA2677-MON.

Family and domain databases

HAMAPMF_00578.
[Tree]
InterProIPR007370. Glu_cys_ligase.
IPR006334. Glut_cys_ligase.
[Graphical view]
PfamPF04262. Glu_cys_ligase. 1 hit.
[Graphical view]
TIGRFAMsTIGR01434. glu_cys_ligase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGSH1_SALPA
AccessionPrimary (citable) accession number: Q5PF10
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: January 4, 2005
Last modified: June 16, 2009
This is version 22 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents