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Reviewed, UniProtKB/Swiss-Prot Q88UW5 (GSHAB_LACPL)

Last modified June 16, 2009. Version 36. 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:
    Glutathione biosynthesis bifunctional protein gshAB
Alternative name(s):
    Gamma-GCS-GS
      Short name=GCS-GS
Including the following 2 domains:
    1- Recommended name:
            Glutamate--cysteine ligase
              EC=6.3.2.2
        Alternative name(s):
            Gamma-glutamylcysteine synthetase
            Gamma-ECS
              Short name=GCS
    2- Recommended name:
            Glutathione synthetase
              EC=6.3.2.3
        Alternative name(s):
            Glutathione synthase
            GSH synthetase
              Short name=GSH-S
              Short name=GSHase
              Short name=GS
Gene names
Name: gshAB
Synonyms: gshF
Ordered Locus Names: lp_2336
OrganismLactobacillus plantarum [Complete proteome] [HAMAP]
Taxonomic identifier1590 [NCBI]
Taxonomic lineageBacteriaFirmicutesLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length751 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Synthesizes glutathione from L-glutamate and L-cysteine via gamma-L-glutamyl-L-cysteine By similarity.

Catalytic activity

ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine. HAMAP MF_00782

ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione. HAMAP MF_00782

Pathway

Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 1/2. HAMAP MF_00782

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

Subunit structure

Monomer By similarity.

Sequence similarities

In the N-terminal section; belongs to the glutamate--cysteine ligase type 1 family. Type 2 subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 751751Glutathione biosynthesis bifunctional protein gshAB HAMAP MF_00782
PRO_0000192552

Regions

Region1 – 336336Glutamate--cysteine ligase HAMAP MF_00782

Sequences

Sequence LengthMass (Da)Tools
Q88UW5-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 605A494E7A7DCBF7

FASTA75183,018
        10         20         30         40         50         60 
MELDAVGKAI VQYHLVPLVH QANLGLEVTM HRVDAHGHLA TTAHPQAFGS AQQNHQLRPG 

        70         80         90        100        110        120 
FSASALKFTT PVRRDIPALM AYLKGLNTAA RRSLDADERL WPLSSTPVLP DDLTNVPLAD 

       130        140        150        160        170        180 
VDQVSYQRRR DLARKYELQR LMTTGSHVNM SLNEALFTRL YTETFHQQYH SYVDFRNAIY 

       190        200        210        220        230        240 
LKVAQGLVRM NWLIQYLFGA SPRLAVTDTT SRPQRSSVQH PDGRYSQVTG DYTSIDRYVA 

       250        260        270        280        290        300 
KLTAAVRQQQ LLSVNDFDGP VRLRSNGQLA MMARQGVYYL EYRGLDLDPT SPVGVDANAV 

       310        320        330        340        350        360 
AFVRLLASYF VMMPALPAKM VSQVNAQADQ LTRQVLGENP TTASAQAVPA VQVLDALADF 

       370        380        390        400        410        420 
VKTYGLPNED AVLLKQLKSW VTDPKKTLSA QIAMQADPLA WALERAARYQ ESSNERPFEL 

       430        440        450        460        470        480 
AGFTALDLSS QQLAQQALTR GVQVDVVDPH ANILRLTKLG RSQLVVNGSG TDLNPQALTT 

       490        500        510        520        530        540 
VLTHKAAAKQ ILAEHGVPVP ASQTYHTANQ LIADYDRYVQ AGGIVLKAAD ESHKVIVFRI 

       550        560        570        580        590        600 
MPERGLFEQV VRQLFEQTSA VMAEEVVVAS SYRFLVIDSR VQAIVERIPA NIVGDGRSTV 

       610        620        630        640        650        660 
KTLLDRKNGR ALRGTAFKWP QSALQLGTIE RYRLDSYHLT LDSVVSRGTQ ILLREDATFG 

       670        680        690        700        710        720 
NGADVLDATA DMHQSYVQAV EKLVADLHLA VAGVDVMIPN LYAELVPEHP EMAVYLGIHA 

       730        740        750 
APYLYPHLFP MFGTAQPVAG QLLDALFKNE D 

« Hide

Cross-references

Sequence databases

AL935258 Genomic DNA. Translation: CAD64659.1.
RefSeqNP_785808.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID1062357.
GenomeReviewsGene locus lp_2336 in contig AL935263_GR.
KEGGlpl:lp_2336.
NMPDRfig|220668.1.peg.1942.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ88UW5.
OMAQ88UW5. PKSTNYG.

Enzyme and pathway databases

BioCycLPLA220668:LP_2336-MON.
BRENDA6.3.2.2. 593.
6.3.2.3. 593.

Family and domain databases

HAMAPMF_00782. Divergent sequence.
[Tree]
InterProIPR007370. Glu_cys_ligase.
[Graphical view]
PfamPF04262. Glu_cys_ligase. 1 hit.
[Graphical view]
PROSITEPS50975. ATP_GRASP. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGSHAB_LACPL
AccessionPrimary (citable) accession number: Q88UW5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: June 1, 2003
Last modified: June 16, 2009
This is version 36 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