Q71VZ1 (GSHAB_LISMF) 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:	LMOf2365_2760

Organism

Listeria monocytogenes serotype 4b (strain F2365) [Complete proteome] [HAMAP]

Taxonomic identifier

265669 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Listeriaceae › Listeria › Listeria monocytogenes

Protein attributes

Sequence length	769 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
Cofactor	Binds 2 magnesium or manganese ions per subunit By similarity.
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. HAMAP-Rule MF_00782
Sequence similarities	In the N-terminal section; belongs to the glutamate--cysteine ligase type 1 family. Type 2 subfamily. Contains 1 ATP-grasp domain.
Sequence caution	The sequence AAT05525.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Glutathione biosynthesis
Ligand	ATP-binding Magnesium Manganese Metal-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP glutamate-cysteine ligase activity Inferred from electronic annotation. Source: HAMAP glutathione synthase activity Inferred from electronic annotation. Source: HAMAP magnesium ion binding Inferred from electronic annotation. Source: HAMAP manganese ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 769	769	Glutathione biosynthesis bifunctional protein GshAB HAMAP-Rule MF_00782		PRO_0000192554
Regions
	Domain	514 – 768	255	ATP-grasp
	Nucleotide binding	541 – 599	59	ATP By similarity
	Region	1 – 347	347	Glutamate--cysteine ligase HAMAP-Rule MF_00782
Sites
	Metal binding	721	1	Magnesium or manganese 1 By similarity
	Metal binding	738	1	Magnesium or manganese 1 By similarity
	Metal binding	738	1	Magnesium or manganese 2 By similarity
	Metal binding	740	1	Magnesium or manganese 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q71VZ1 [UniParc]. Last modified July 5, 2005. Version 2. Checksum: 94140E0923FCD379	FASTA	769	87,751
	10 20 30 40 50 60 MLDSFKEDPK LRKLLFSGHF GLEKENIRVT SDGKLALTPH PAIFGPKEDN PYIKTDFSES 70 80 90 100 110 120 QIEMITPVTD SIDSVYEWLE NLHNIVSLRS ENELLWPSSN PPILPAEEDI PIAEYKTPDS 130 140 150 160 170 180 PDRKYREHLA KGYGKKIQLL SGIHYNFSFP EALIDGLYDK ISLPEESKQD FKNRLYLKVA 190 200 210 220 230 240 KYFMKNRWLL IYLTGASPVY LADFSKTKHD ESLPDGSSAL RDGISLRNSN AGYKNKEALY 250 260 270 280 290 300 VDYNSFDAYI SSISNYIEAG KIESMREFYN PIRLKNAHTD QTVESLAEHG VEYLEIRSID 310 320 330 340 350 360 LNPLESNGIS KDELAFIHLF LIKGLLSEDR ELCSNNQQLA DENENNIALN GLAQPALKNC 370 380 390 400 410 420 DNEEISVVEA GLLELNKMSD FIQSLRPEDT KLQAIIEKQK ERLLHPEKTI AAQVKQQVTK 430 440 450 460 470 480 EGYVDFHLNQ AKTYMEETEA LAYKLIGAED MELSTQIIWK DAIARGIKVD VLDRAENFLR 490 500 510 520 530 540 FQKGDHVEYV KQASKTSKDN YVSVLMMENK VVTKLVLAEH DIRVPFGDSF SDQALALEAF 550 560 570 580 590 600 SLFEDKQIVV KPKSTNYGWG ISIFKNKFTL EDYQEALNIA FSYDSSVIIE EFIPGDEFRF 610 620 630 640 650 660 LVINDKVEAV LKRVPANVTG DGIHTVRELV EEKNTDPLRG TDHLKPLEKI RTGPEETLML 670 680 690 700 710 720 SMQNLSWDSI PKAEEIIYLR ENSNVSTGGD SIDYTEEMDD YFKEIAIRAT QVLDAKICGV 730 740 750 760 DIIVPRETID RDKHAIIELN FNPAMHMHCF PYQGEKKKIG DKILDFLFE

References

[1]

"Whole genome comparisons of serotype 4b and 1/2a strains of the food-borne pathogen Listeria monocytogenes reveal new insights into the core genome components of this species." Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T., Kolonay J.F., Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T., Peterson J.D., White O., Nelson W.C., Nierman W.C., Beanan M.J., Brinkac L.M., Daugherty S.C., Dodson R.J. , Durkin A.S., Madupu R., Haft D.H., Selengut J., Van Aken S.E., Khouri H.M., Fedorova N., Forberger H.A., Tran B., Kathariou S., Wonderling L.D., Uhlich G.A., Bayles D.O., Luchansky J.B., Fraser C.M. Nucleic Acids Res. 32:2386-2395(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: F2365.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017262 Genomic DNA. Translation: AAT05525.1. Different initiation.
RefSeq	YP_015348.1. NC_002973.6.
3D structure databases
ProteinModelPortal	Q71VZ1.
ModBase	Search...
Protein-protein interaction databases
STRING	265669.LMOf2365_2760.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAT05525; AAT05525; LMOf2365_2760.
GeneID	2797638.
KEGG	lmf:LMOf2365_2760.
PATRIC	20326908. VBILisMon105049_2779.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1181.
HOGENOM	HOG000156471.
KO	K01919.
ProtClustDB	PRK02471.
Enzyme and pathway databases
UniPathway	UPA00142; UER00209. UPA00142; UER00210.
Family and domain databases
Gene3D	3.30.1490.20. 1 hit. 3.30.470.20. 3 hits.
HAMAP	MF_00782. Glut_biosynth.
InterPro	IPR011761. ATP-grasp. IPR013815. ATP_grasp_subdomain_1. IPR013816. ATP_grasp_subdomain_2. IPR007370. Glu_cys_ligase. IPR006335. Glut_cys-rel. IPR020561. PRibGlycinamid_synth_ATP-grasp. [Graphical view]
Pfam	PF01071. GARS_A. 1 hit. PF04262. Glu_cys_ligase. 1 hit. [Graphical view]
TIGRFAMs	TIGR01435. glu_cys_lig_rel. 1 hit.
PROSITE	PS50975. ATP_GRASP. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GSHAB_LISMF

Accession

Primary (citable) accession number: Q71VZ1

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	July 5, 2005
Last modified:	May 1, 2013
This is version 60 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program