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Reviewed, UniProtKB/Swiss-Prot Q21EP1 (GSH1_SACD2)

Last modified June 16, 2009. Version 20. 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: Sde_3583
OrganismSaccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024) [Complete proteome] [HAMAP]
Taxonomic identifier203122 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesAlteromonadaceaeSaccharophagus

Protein attributes

Sequence length530 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 – 530530Glutamate--cysteine ligase HAMAP MF_00578
PRO_1000025185

Sequences

Sequence LengthMass (Da)Tools
Q21EP1-1 [UniParc].

Last modified April 18, 2006. Version 1.
Checksum: C55176AC2B39CD30

FASTA53060,265
        10         20         30         40         50         60 
MYEIQSFHAG LYDSKNAPVL TGIMRGIERE GLRIDRDGKL AQTPHPVALG SALTHPQITT 

        70         80         90        100        110        120 
DFSEALLEFI TPPTHRVEDL FKQLYDIQGY TLSKLDDELI WSSSMPCVLN DDATIPVAQY 

       130        140        150        160        170        180 
GSSNNGTMKT VYRVGLGHRY GRAMQTVAGL HYNFSLPDAF WSFLHREEYS LLDLQDFKDQ 

       190        200        210        220        230        240 
KYFALIRNFR RYYWLLVYLF GASPALCGSF IKGREHNLQP LIDERTLHLP YATSLRMGDL 

       250        260        270        280        290        300 
GYQSSAQESL YVCYNDKQSY ITTLCAAITT PIDEYKAIGL QDEKGEFKQL NTSLLQIENE 

       310        320        330        340        350        360 
FYSSIRPKRT AKHGETALSA LRNRGVEYIE VRCLDIDPFD PLGVNKPQVR FLDTFLLYCA 

       370        380        390        400        410        420 
LQDSPDTSPE ESANILRNQK TVVTEGRSPK ALIESFTKGK IPLKQAGEAL IKAMRPVAEL 

       430        440        450        460        470        480 
LDIAHETEEH TQSLETQLAA ILNPELTPSA RIISHLSAKK LPYAHYALAQ SRHHHETLLA 

       490        500        510        520        530 
KKPSNNTMQQ FEKMAAESLD KQTRLEQKNS GNFSEFLQEY YKQYQMCCDK 

« Hide

References

[1]"Complete sequence of Saccharophagus degradans 2-40."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Saunders E.H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. expand/collapse author list , Kyrpides N., Lykidis A., Richardson P., Weiner R.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000282 Genomic DNA. Translation: ABD82838.1.
RefSeqYP_529050.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3966445.
GenomeReviewsGene locus Sde_3583 in contig CP000282_GR.
KEGGsde:Sde_3583.
NMPDRfig|203122.1.peg.1595.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ21EP1.
OMAQ21EP1. DTLYLPY.

Enzyme and pathway databases

BioCycSDEG203122:SDE_3583-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_SACD2
AccessionPrimary (citable) accession number: Q21EP1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: April 18, 2006
Last modified: June 16, 2009
This is version 20 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