Q88UW5 (GSHAB_LACPL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutathione biosynthesis bifunctional protein GshAB

Alternative name(s):
Gamma-GCS-GS
Short name=GCS-GS

Including the following 2 domains:

1. Glutamate--cysteine ligase
   EC=6.3.2.2
   Alternative name(s):
   Gamma-ECS
   Short name=GCS
   Gamma-glutamylcysteine synthetase
2. Glutathione synthetase
   EC=6.3.2.3
   Alternative name(s):
   GSH synthetase
   Short name=GS
   Short name=GSH-S
   Short name=GSHase
   Glutathione synthase

Gene names

Name:	gshAB
Synonyms:	gshF
Ordered Locus Names:	lp_2336

Organism

Lactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1) [Reference proteome] [HAMAP]

Taxonomic identifier

220668 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Lactobacillales › Lactobacillaceae › Lactobacillus › Lactobacillus plantarum

Protein attributes

Sequence length	751 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Synthesizes glutathione from L-glutamate and L-cysteine via gamma-L-glutamyl-L-cysteine By similarity. HAMAP-Rule MF_00782
Catalytic activity	ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine. HAMAP-Rule MF_00782 ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione. HAMAP-Rule MF_00782
Pathway	Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 1/2. HAMAP-Rule 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.

Ontologies

Keywords
Biological process	Glutathione biosynthesis
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW glutamate-cysteine ligase activity Inferred from electronic annotation. Source: EC glutathione synthase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 751	751	Glutathione biosynthesis bifunctional protein GshAB HAMAP-Rule MF_00782		PRO_0000192552
Regions
	Region	1 – 336	336	Glutamate--cysteine ligase HAMAP-Rule MF_00782

Sequences

	Sequence		Length	Mass (Da)
	Q88UW5 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 605A494E7A7DCBF7	FASTA	751	83,018
	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

References

[1]

"Complete genome sequence of Lactobacillus plantarum WCFS1." 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. Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-793 / NCIMB 8826 / WCFS1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL935263 Genomic DNA. Translation: CCC79530.1.
RefSeq	YP_004890044.1. NC_004567.2.
3D structure databases
ProteinModelPortal	Q88UW5.
ModBase	Search...
Protein-protein interaction databases
STRING	220668.lp_2336.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CCC79530; CCC79530; lp_2336.
GeneID	1062357.
KEGG	lpl:lp_2336.
PATRIC	22250719. VBILacPla27411_1975.
Phylogenomic databases
eggNOG	COG1181.
HOGENOM	HOG000112828.
KO	K01919.
OMA	PYIQTDF.
ProtClustDB	PRK02471.
Enzyme and pathway databases
UniPathway	UPA00142; UER00209. UPA00142; UER00210.
Family and domain databases
HAMAP	MF_00782. Glut_biosynth. Divergent sequence.
InterPro	IPR007370. Glu_cys_ligase. [Graphical view]
Pfam	PF04262. Glu_cys_ligase. 2 hits. [Graphical view]
PROSITE	PS50975. ATP_GRASP. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GSHAB_LACPL

Accession

Primary (citable) accession number: Q88UW5
Secondary accession number(s): F9UQP1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2005
Last sequence update:	June 1, 2003
Last modified:	May 1, 2013
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program