Q8XK30 (GSHAB_CLOPE) 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:	CPE1573

Organism

Clostridium perfringens (strain 13 / Type A) [Complete proteome] [HAMAP]

Taxonomic identifier

195102 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium › Clostridium perfringens

Protein attributes

Sequence length	778 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.
Sequence similarities	In the N-terminal section; belongs to the glutamate--cysteine ligase type 1 family. Type 2 subfamily. Contains 1 ATP-grasp domain.

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 – 778	778	Glutathione biosynthesis bifunctional protein GshAB HAMAP-Rule MF_00782		PRO_0000192549
Regions
	Domain	521 – 777	257	ATP-grasp
	Nucleotide binding	548 – 606	59	ATP By similarity
	Region	1 – 354	354	Glutamate--cysteine ligase HAMAP-Rule MF_00782
Sites
	Metal binding	728	1	Magnesium or manganese 1 By similarity
	Metal binding	747	1	Magnesium or manganese 1 By similarity
	Metal binding	747	1	Magnesium or manganese 2 By similarity
	Metal binding	749	1	Magnesium or manganese 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8XK30 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 2008FF46AF06423E	FASTA	778	90,463
	10 20 30 40 50 60 MVNLDKGLLK IIKDESLEDY FIKANFGLEK ENVRVTESGN LALTPHPKAF GDREKNAYIK 70 80 90 100 110 120 TDFSESQLEM VTPVCNTLEE VYSFICNLNK VVSLEIMKNG EFLWPQSNPP ILPREEEIPI 130 140 150 160 170 180 AKLSNREDEL YRENLSYKYG KKKQVISGIH YNFSFKEEFI KLLYKELKVE KDFREFKDDI 190 200 210 220 230 240 YLRMARNFQK YHWLLIYLTG ASPVFHESYI EEIKEEGEKL GEDSYYIKDD TSLRNSSYGY 250 260 270 280 290 300 KNKKDYYVSY NSIEEYASDI KNLVKDKEIQ SIKEYYNPIR LKSLGSEDML ESLLHKGIDY 310 320 330 340 350 360 LEVRLLDLDP LSIQGVSKET LYLLHLFMIY TLLKENKEIT YKDQEEFFKN HDMVALKGRN 370 380 390 400 410 420 EEAVIYENGV PVLLKDKGRE ILSEMDEIVE ILFSNNEEFK NVIKRALEKI NNPHDTISEK 430 440 450 460 470 480 LIKDIKEEGY INFHMRLAKE YLNNFKNKEF NLVGYEDLEL STQILILDAI KRGIEFNIMD 490 500 510 520 530 540 RLENFISLSD GEKVEYVKQA TKTSKDSYIT ALIMENKLVT KDILRENNIR VPKGKDYDNI 550 560 570 580 590 600 DEAKKDFRLF KDEKIVIKPK STNFGLGISI FPGEYSREDY DKAVEIAFRE DSSILIEEFM 610 620 630 640 650 660 TGKEYRFLVI GEEVVGILHR EPANVIGNGE STIEELVSEK NKDPLRGKGY KTPLEKIKLG 670 680 690 700 710 720 EIEEMFLKNQ GLSFKSIPKN GEKIYLRENS NISTGGDSID FTDKIHPSYK EVALKSAKAV 730 740 750 760 770 KALICGVDMV IDNIEEEAKE KNHGIIELNF NPAIHIHCFP YKGENRKAGE KILDLLFN

References

[1]

"Complete genome sequence of Clostridium perfringens, an anaerobic flesh-eater." Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T., Ogasawara N., Hattori M., Kuhara S., Hayashi H. Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 13 / Type A.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000016 Genomic DNA. Translation: BAB81279.1.
RefSeq	NP_562489.1. NC_003366.1.
3D structure databases
ProteinModelPortal	Q8XK30.
ModBase	Search...
Protein-protein interaction databases
STRING	195102.CPE1573.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAB81279; BAB81279; BAB81279.
GeneID	989883.
KEGG	cpe:CPE1573.
PATRIC	19497095. VBICloPer59675_1643.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1181.
HOGENOM	HOG000156471.
KO	K01919.
OMA	PYIQTDF.
ProtClustDB	PRK02471.
Enzyme and pathway databases
BioCyc	CPER195102:GJFM-1619-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_CLOPE

Accession

Primary (citable) accession number: Q8XK30

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2002
Last sequence update:	March 1, 2002
Last modified:	May 1, 2013
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program