Q5LYY5 (GSHAB_STRT1) 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:	str1413

Organism

Streptococcus thermophilus (strain CNRZ 1066) [Complete proteome] [HAMAP]

Taxonomic identifier

299768 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Streptococcus › Streptococcus thermophilus

Protein attributes

Sequence length	754 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 – 754	754	Glutathione biosynthesis bifunctional protein GshAB HAMAP-Rule MF_00782		PRO_0000192561
Regions
	Domain	488 – 746	259	ATP-grasp
	Nucleotide binding	515 – 573	59	ATP By similarity
	Region	1 – 332	332	Glutamate--cysteine ligase HAMAP-Rule MF_00782
Sites
	Metal binding	695	1	Magnesium or manganese 1 By similarity
	Metal binding	716	1	Magnesium or manganese 1 By similarity
	Metal binding	716	1	Magnesium or manganese 2 By similarity
	Metal binding	718	1	Magnesium or manganese 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5LYY5 [UniParc]. Last modified February 1, 2005. Version 1. Checksum: 83C856B2641FA2E3	FASTA	754	85,137
	10 20 30 40 50 60 MTLNQLLQKL EATSPILQAN FGIERESLRV DRQGQLVHTP HPSCLGARSF HPYIQTDFCE 70 80 90 100 110 120 FQMELITPVA KSTTEARRFL GAITDVAGRS IATDEVLWPL SMPPRLKAEE IQVAQLENDF 130 140 150 160 170 180 ERHYRNYLAE KYGTKLQAIS GIHYNMELGK DLVEALFQES DQTDMIAFKN ALYLKLAQNY 190 200 210 220 230 240 LRYRWVITYL FGASPIAEQG FFDQEVPEPM RSFRNSDHGY VNKEEIQVSF VSLEDYVSAI 250 260 270 280 290 300 ETYIEQGDLI AEKEFYSAVR FRGQKVNRSF LDKGITYLEF RNFDLNPFER IGISQTTMDT 310 320 330 340 350 360 VHLLILAFLW LDSPENVDQA LAQGHALNEK IALSHPLEPL PSEAKTQDIV TALDQLVQHF 370 380 390 400 410 420 GLGDYHQDLV KQVKAAFADP NQTLSAQLLP YIKDKSLAEF ALNKALAYHD YDWTAHYALK 430 440 450 460 470 480 GYEEMELSTQ MLLFDAIQKG IHFEILDEQD QFLKLWHQDH VEYVKNGNMT SKDNYVVPLA 490 500 510 520 530 540 MANKTVTKKI LADAGFPVPS GDEFTSLEEG LAYYPLIKDK QIVVKPKSTN FGLGISIFQE 550 560 570 580 590 600 PASLDNYQKA LEIAFAEDTS VLVEEFIPGT EYRFFILDGR CEAVLLRVAA NVIGDGKHTI 610 620 630 640 650 660 RELVAQKNAN PLRGRDHRSP LEIIELGDIE QLMLAQQGYT PDDILPEGKK VNLRRNSNIS 670 680 690 700 710 720 TGGDSIDVTE TMDSSYQELA AAMATSMGAW ACGVDLIIPD ETQIATKENP HCTCIELNFN 730 740 750 PSMYMHTYCA EGPGQAITTK ILDKLFPEIV AGQT

References

[1]

"Complete sequence and comparative genome analysis of the dairy bacterium Streptococcus thermophilus." Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D., Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M., Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D., Hancy F. , Burteau S., Boutry M., Delcour J., Goffeau A., Hols P. Nat. Biotechnol. 22:1554-1558(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CNRZ 1066.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000024 Genomic DNA. Translation: AAV62950.1.
RefSeq	YP_141765.1. NC_006449.1.
3D structure databases
ProteinModelPortal	Q5LYY5.
ModBase	Search...
Protein-protein interaction databases
STRING	299768.str1413.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAV62950; AAV62950; str1413.
GeneID	3167482.
KEGG	stc:str1413.
PATRIC	19795897. VBIStrThe135799_1404.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1181.
HOGENOM	HOG000156471.
KO	K01919.
OMA	PYIQTDF.
ProtClustDB	PRK02471.
Enzyme and pathway databases
UniPathway	UPA00142; UER00209. UPA00142; UER00210.
Family and domain databases
Gene3D	3.30.470.20. 1 hit.
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_STRT1

Accession

Primary (citable) accession number: Q5LYY5

Entry history

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

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program