Glutamate--cysteine ligase
     (EC 6.3.2.2)
     (Gamma-glutamylcysteine synthetase)
     (Gamma-ECS)
     (GCS)
Glutathione synthetase
     (EC 6.3.2.3)
     (Glutathione synthase)
     (GSH synthetase)
     (GSH-S)
     (GSHase)
     (GS)

Gene name

	Name:	gshAB
	Synonyms:	gshF
	OrderedLocusNames:	lp_2336

From

Lactobacillus plantarum

[TaxID: 1590]

[HAMAP proteome]

Taxonomy

Bacteria; Firmicutes; Lactobacillales; Lactobacillaceae; Lactobacillus.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
DOI=10.1073/pnas.0337704100; PubMed=12566566 [NCBI, ExPASy, EBI, Israel, Japan]
Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P., Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J., Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M., Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M., Siezen R.J.;
"Complete genome sequence of Lactobacillus plantarum WCFS1.";
Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).

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.
CATALYTIC ACTIVITY: ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione.
PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 1/2 .
PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 2/2 .
SUBUNIT: Monomer (By similarity).
SIMILARITY: In the N-terminal section; belongs to the glutamate--cysteine ligase type 1 family. Type 2 subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AL935258; CAD64659.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_785808.1; -.

3D structure databases

ModBase

Q88UW5.

Enzyme and pathway databases

BioCyc

LPLA220668:LP_2336-MON; -.

Ontologies

GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from HAMAP).
GO:0004357;	Molecular function: glutamate-cysteine ligase activity (inferred from electronic annotation from HAMAP).
GO:0004363;	Molecular function: glutathione synthase activity (inferred from electronic annotation from HAMAP).
GO:0006750;	Biological process: glutathione biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00782; atypical; 1.
PBIL [Tree]

InterPro

IPR011761; ATP-grasp.
IPR007370; Glu_cys_ligase.
Graphical view of domain structure.

Pfam

PF04262; Glu_cys_ligase; 2.
Pfam graphical view of domain structure.

PROSITE

PS50975; ATP_GRASP; FALSE_NEG.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

GeneID

1062357; -.

GenomeReviews

AL935263_GR; lp_2336.

KEGG

lpl:lp_2336; -.

NMPDR

fig|220668.1.peg.1942; -.

Phylogenomic databases

HOGENOM

Q88UW5; -.

Genome annotation databases

CMR

Q88UW5; lp_2336.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ATP-binding; Complete proteome; Glutathione biosynthesis; Ligase; Multifunctional enzyme; Nucleotide-binding.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 751`	`751`	`Glutathione biosynthesis bifunctional protein gshAB.`	`PRO_0000192552`
`REGION`	`1 336`	`336`	`Glutamate--cysteine ligase.`

Sequence information

Length: 751 AA [This is the length of the unprocessed precursor]

Molecular weight: 83018 Da [This is the MW of the unprocessed precursor]

CRC64: 605A494E7A7DCBF7 [This is a checksum on the sequence]

        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

Q88UW5 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools