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Q1LTQ6 (GSH1_BAUCH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 33. 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:
Glutamate--cysteine ligase

EC=6.3.2.2
Alternative name(s):
Gamma-ECS
Short name=GCS
Gamma-glutamylcysteine synthetase
Gene names
Name:gshA
Ordered Locus Names:BCI_0201
OrganismBaumannia cicadellinicola subsp. Homalodisca coagulata [Complete proteome] [HAMAP]
Taxonomic identifier374463 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaCandidatus Baumannia

Protein attributes

Sequence length523 AA.
Sequence statusComplete.
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: UniProtKB-KW

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

glutamate-cysteine ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 523523Glutamate--cysteine ligase HAMAP MF_00578
PRO_1000025168

Sequences

Sequence LengthMass (Da)Tools
Q1LTQ6 [UniParc].

Last modified May 30, 2006. Version 1.
Checksum: B91B940CE326C55B

FASTA52360,200
        10         20         30         40         50         60 
MIPDVSSDTL FWLKANPQAL QGIYRGVERE TLRINTQGHL AQTPHPKKLG AALTHKWITT 

        70         80         90        100        110        120 
DFAETLLEFI TPVAQDIDHM LTLLRDIHRH VARHLCNEWM WPMSMPCFID SQQQIKLAQY 

       130        140        150        160        170        180 
GPSNMGRMKT LYRKGLKNRY SAMMQIISGV HYNFSLPLTF WQVYAGVSDM NSNKDIISAG 

       190        200        210        220        230        240 
YLGLIRNYYR FGWIIPYIFG ASPGVCQSFM KNRDTDLPFI KASSGFLYLP YATSLRMSDL 

       250        260        270        280        290        300 
GYANKSQSQL DITFNSLKEY VFRLKHAIRT PYADYQRIGL KKNGSYLQLN TNILQSENEL 

       310        320        330        340        350        360 
YAPIRPKRIT KNEESPLDAL LRRGIEYIEV RALDINPFSP VGIDEEQVRF LDLFLIWCTL 

       370        380        390        400        410        420 
APAPKMSTRE LLYTRLNWTK VILEGRKPGL TLIVDGGSSK KPLATIGKEL FSAMQALAET 

       430        440        450        460        470        480 
LDSHNGNIQY QQVCHKLRAC IDQPELTLSA RILKEMKKYG IRGLGLTLAN QYFQILLEEP 

       490        500        510        520 
LEMFNELTFD KEQIRSWHRQ LELEALDILS FDDFLAHINS HQQ 

« Hide

References

[1]"Metabolic complementarity and genomics of the dual bacterial symbiosis of sharpshooters."
Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A.
PLoS Biol. 4:1079-1092(2006) [PubMed: 16729848] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000238 Genomic DNA. Translation: ABF13792.1.
RefSeqYP_588658.1. NC_007984.1.

3D structure databases

ProteinModelPortalQ1LTQ6.
SMRQ1LTQ6. Positions 1-511.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1LTQ6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4056732.
GenomeReviewsGene locus BCI_0201 in contig CP000238_GR.
KEGGbci:BCI_0201.
PATRIC21073901. VBIBauCic75062_0191.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2918.
HOGENOMHBG289023.
OMAFGLIRNY.
PhylomeDBQ1LTQ6.

Enzyme and pathway databases

BioCycBCIC186490:BCI_0201-MONOMER.

Family and domain databases

HAMAPMF_00578. Glu_cys_ligase.
[Tree]
InterProIPR007370. Glu_cys_ligase.
IPR006334. Glut_cys_ligase.
[Graphical view]
KOK01919.
PfamPF04262. Glu_cys_ligase. 1 hit.
[Graphical view]
TIGRFAMsTIGR01434. Glu_cys_ligase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGSH1_BAUCH
AccessionPrimary (citable) accession number: Q1LTQ6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 30, 2006
Last modified: January 25, 2012
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families