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Q9CM00 (GSHAB_PASMU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:PM1048
OrganismPasteurella multocida (strain Pm70) [Complete proteome] [HAMAP]
Taxonomic identifier272843 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaePasteurella

Protein attributes

Sequence length757 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 – 757757Glutathione biosynthesis bifunctional protein GshAB HAMAP-Rule MF_00782
PRO_0000192557

Regions

Domain494 – 753260ATP-grasp
Nucleotide binding521 – 58060ATP By similarity
Region1 – 337337Glutamate--cysteine ligase HAMAP-Rule MF_00782

Sites

Metal binding7021Magnesium or manganese 1 By similarity
Metal binding7231Magnesium or manganese 1 By similarity
Metal binding7231Magnesium or manganese 2 By similarity
Metal binding7251Magnesium or manganese 2 By similarity

Secondary structure

....................................................................................................................................... 757
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9CM00 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: CF0E49A661C14336

FASTA75785,862
        10         20         30         40         50         60 
MKIQHIIHEN QLGLLFQQGS FGLEKESQRV TADGAIVTTP HPAVFGNRRY HPYIQTDFAE 

        70         80         90        100        110        120 
SQLELITPPT KKLEDTFRWL SVIHEVVQRS LPEEEYIFPL SMPAGLPAEE QIRVAQLDNP 

       130        140        150        160        170        180 
EDVAYREYLV KIYGKNKQMV SGIHYNFQLS PDLITRLFRL QNEYQSAVDF QNDLYLKMAK 

       190        200        210        220        230        240 
NFLRYQWILL YLLAATPTVE SAYFKDGSPL AKGQFVRSLR SSQYGYVNDP EINVSFDSVE 

       250        260        270        280        290        300 
KYVESLEHWV STGKLIAEKE FYSNVRLRGA KKAREFLTTG IQYLEFRLFD LNPFEIYGIS 

       310        320        330        340        350        360 
LKDAKFIHVF ALFMIWMDHT ADQEEVELGK ARLAEVAFEH PLEKTAYAVE GELVLLELLS 

       370        380        390        400        410        420 
MLEQIGAEPE LFEIVKEKLT QFTDPSKTVA GRLVRAIEQA GSDQQLGAQL AQQYKAQAFE 

       430        440        450        460        470        480 
RFYALSAFDN MELSTQALLF DVIQKGIHTE ILDENDQFLC LKYGDHIEYV KNGNMTSHDS 

       490        500        510        520        530        540 
YISPLIMENK VVTKKVLQKA GFNVPQSVEF TSLEKAVASY ALFENRAVVI KPKSTNYGLG 

       550        560        570        580        590        600 
ITIFQQGVQN REDFAKALEI AFREDKEVMV EDYLVGTEYR FFVLGDETLA VLLRVPANVV 

       610        620        630        640        650        660 
GDSVHSVAEL VAMKNDHPLR GDGSRTPLKK IALGEIEQLQ LKEQGLTIDS IPAKDQLVQL 

       670        680        690        700        710        720 
RANSNISTGG DSIDMTDEMH ESYKQLAVGI TKAMGAAVCG VDLIIPDLKQ PATPNLTSWG 

       730        740        750 
VIEANFNPMM MMHIFPYAGK SRRLTQNVIK MLFPELE 

« Hide

References

[1]"Complete genomic sequence of Pasteurella multocida Pm70."
May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.
Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Pm70.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE004439 Genomic DNA. Translation: AAK03132.1.
RefSeqNP_245985.1. NC_002663.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3LN7X-ray3.20A/B1-757[»]
ProteinModelPortalQ9CM00.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272843.PM1048.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK03132; AAK03132; PM1048.
GeneID1244395.
KEGGpmu:PM1048.
PATRIC22871339. VBIPasMul88067_1062.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1181.
HOGENOMHOG000156471.
KOK01919.
OMAPYIQTDF.
OrthoDBEOG6BKJ7H.
ProtClustDBPRK02471.

Enzyme and pathway databases

BioCycPMUL272843:GC8W-1090-MONOMER.
SABIO-RKQ9CM00.
UniPathwayUPA00142; UER00209.
UPA00142; UER00210.

Family and domain databases

Gene3D3.30.1490.20. 1 hit.
3.30.470.20. 3 hits.
HAMAPMF_00782. Glut_biosynth.
InterProIPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
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_PASMU
AccessionPrimary (citable) accession number: Q9CM00
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: June 1, 2001
Last modified: February 19, 2014
This is version 78 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways