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Q8XK30 (GSHAB_CLOPE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismClostridium perfringens (strain 13 / Type A) [Complete proteome] [HAMAP]
Taxonomic identifier195102 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length778 AA.
Sequence statusComplete.
Protein existenceInferred 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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 778778Glutathione biosynthesis bifunctional protein GshAB HAMAP-Rule MF_00782
PRO_0000192549

Regions

Domain521 – 777257ATP-grasp
Nucleotide binding548 – 60659ATP By similarity
Region1 – 354354Glutamate--cysteine ligase HAMAP-Rule MF_00782

Sites

Metal binding7281Magnesium or manganese 1 By similarity
Metal binding7471Magnesium or manganese 1 By similarity
Metal binding7471Magnesium or manganese 2 By similarity
Metal binding7491Magnesium or manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8XK30 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 2008FF46AF06423E

FASTA77890,463
        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 

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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.
RefSeqNP_562489.1. NC_003366.1.

3D structure databases

ProteinModelPortalQ8XK30.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING195102.CPE1573.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB81279; BAB81279; BAB81279.
GeneID989883.
KEGGcpe:CPE1573.
PATRIC19497095. VBICloPer59675_1643.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1181.
HOGENOMHOG000156471.
KOK01919.
OMAHVEYVKN.
OrthoDBEOG6BKJ7H.

Enzyme and pathway databases

BioCycCPER195102:GJFM-1619-MONOMER.
UniPathwayUPA00142; UER00209.
UPA00142; UER00210.

Family and domain databases

Gene3D3.30.470.20. 2 hits.
HAMAPMF_00782. Glut_biosynth.
InterProIPR011761. ATP-grasp.
IPR013816. ATP_grasp_subdomain_2.
IPR007370. Glu_cys_ligase.
IPR006335. Glut_biosynth.
[Graphical view]
PfamPF04262. Glu_cys_ligase. 1 hit.
[Graphical view]
TIGRFAMsTIGR01435. glu_cys_lig_rel. 1 hit.
PROSITEPS50975. ATP_GRASP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGSHAB_CLOPE
AccessionPrimary (citable) accession number: Q8XK30
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: March 1, 2002
Last modified: May 14, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways