Q65RX0 (GSHAB_MANSM) 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:	MS1683

Organism

Mannheimia succiniciproducens (strain MBEL55E) [Complete proteome] [HAMAP]

Taxonomic identifier

221988 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Basfia › Mannheimia succiniciproducens

Protein attributes

Sequence length	757 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 AAU38290.1 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 – 757	757	Glutathione biosynthesis bifunctional protein GshAB HAMAP-Rule MF_00782		PRO_0000192556
Regions
	Domain	494 – 757	264	ATP-grasp
	Nucleotide binding	521 – 580	60	ATP By similarity
	Region	1 – 337	337	Glutamate--cysteine ligase HAMAP-Rule MF_00782
Sites
	Metal binding	702	1	Magnesium or manganese 1 By similarity
	Metal binding	723	1	Magnesium or manganese 1 By similarity
	Metal binding	723	1	Magnesium or manganese 2 By similarity
	Metal binding	725	1	Magnesium or manganese 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q65RX0 [UniParc]. Last modified July 5, 2005. Version 2. Checksum: DCCBAE68513F5980	FASTA	757	85,101
	10 20 30 40 50 60 MNIQQIVKEK GLGLLFRQGT VGIEKESQRV HADGSIVTSE HPKAFGNRSY HPYIQTDFAE 70 80 90 100 110 120 SQLELITPPN KKIEDTLRWL SALHEVTLRT IDENEYIFPM SMPAGLPPEQ EIRVAQLDNA 130 140 150 160 170 180 ADVAYREHLV ASYGKAKQMV SGIHYNFQLD PKLVETLFNA QTDYKSAVDF QNNLYLKMAK 190 200 210 220 230 240 NFLRYQWIPL YLLSATPTVE ANYFKDGSPL KPNQYVRSLR SSKYGYVNAP DIIVSFDSIE 250 260 270 280 290 300 KYVETLEHWV NSGRLIAEKE FYSNVRLRGA KKAREFLHTG IQYLEFRLFD LNPFEAYGIN 310 320 330 340 350 360 LKDAKFIHHF ILLMIWLEET ADQDAVELGR ARLGEVAFED PHSETAYRDE GEQIINQLID 370 380 390 400 410 420 MLKAIGAEQS AVEFAEEKLA QFANPGQTLC ARLVDAIEQA GGYQQLGGEI AKRNKVQAFE 430 440 450 460 470 480 RFYALSAFDN MELSTQALMF DAIQKGLNME ILDENDQFLR LQFGDHFEYV KNGNMTSHDS 490 500 510 520 530 540 YISPLIMENK VVTKKVLAKA GFNVPQSLEF TSVEQAVASY PLFEGKAVVI KPKSTNFGLG 550 560 570 580 590 600 ISIFQQGVHD KADFAKAVEI AFREDKEVMV EDYLVGTEYR FFVLGNETLA VLLRVPANVM 610 620 630 640 650 660 GDGVHTVAEL VAAKNDHPLR GDGSRTPLKK IALGEIEQLQ LKEQGLTVDS VPAKDQLVQL 670 680 690 700 710 720 RANSNISTGG DSIDMTDEMH PSYKDLAVGI TKAMGAAVCG VDLIIPDLKK PAEPNLSSWG 730 740 750 VIEANFNPMM MMHIFPYSGK SRRLTLNVLG MLFPELV

References

[1]

"The genome sequence of the capnophilic rumen bacterium Mannheimia succiniciproducens." Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H., Jeong H., Hur C.G., Kim J.J. Nat. Biotechnol. 22:1275-1281(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MBEL55E.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016827 Genomic DNA. Translation: AAU38290.1. Different initiation.
RefSeq	YP_088875.1. NC_006300.1.
3D structure databases
ProteinModelPortal	Q65RX0.
ModBase	Search...
Protein-protein interaction databases
STRING	221988.MS1683.
Proteomic databases
PRIDE	Q65RX0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAU38290; AAU38290; MS1683.
GeneID	3075060.
KEGG	msu:MS1683.
PATRIC	22446639. VBIManSuc86752_1534.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1181.
HOGENOM	HOG000156471.
KO	K01919.
ProtClustDB	PRK02471.
Enzyme and pathway databases
BioCyc	BMAN221988:GHGM-1733-MONOMER.
UniPathway	UPA00142; UER00209. UPA00142; UER00210.
Family and domain databases
Gene3D	3.30.470.20. 2 hits.
HAMAP	MF_00782. Glut_biosynth.
InterPro	IPR011761. ATP-grasp. IPR013816. ATP_grasp_subdomain_2. IPR007370. Glu_cys_ligase. IPR006335. Glut_cys-rel. [Graphical view]
Pfam	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_MANSM

Accession

Primary (citable) accession number: Q65RX0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2005
Last sequence update:	July 5, 2005
Last modified:	May 29, 2013
This is version 54 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program