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Q7TUK9 (GSHB_PROMM) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 65. 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 synthetase

EC=6.3.2.3
Alternative name(s):
GSH synthetase
Short name=GSH-S
Short name=GSHase
Glutathione synthase
Gene names
Name:gshB
Ordered Locus Names:PMT_2061
OrganismProchlorococcus marinus (strain MIT 9313) [Complete proteome] [HAMAP]
Taxonomic identifier74547 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length308 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione. HAMAP-Rule MF_00162

Cofactor

Binds 1 magnesium or manganese ion per subunit By similarity.

Pathway

Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 2/2. HAMAP-Rule MF_00162

Sequence similarities

Belongs to the prokaryotic GSH synthase family.

Contains 1 ATP-grasp domain.

Sequence caution

The sequence CAE22235.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processGlutathione biosynthesis
   LigandATP-binding
Magnesium
Manganese
Metal-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Gene Ontology (GO)
   Cellular_componentcytosol

Inferred from electronic annotation. Source: InterPro

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

glutathione synthase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

manganese ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 308308Glutathione synthetase HAMAP-Rule MF_00162
PRO_0000197474

Regions

Domain120 – 304185ATP-grasp
Nucleotide binding146 – 20257ATP By similarity

Sites

Metal binding2751Magnesium or manganese By similarity
Metal binding2771Magnesium or manganese By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7TUK9 [UniParc].

Last modified December 15, 2003. Version 2.
Checksum: C5D44F7E79D83F49

FASTA30833,316
        10         20         30         40         50         60 
MRQLFVLDPL QCIQPAKDSS AALMQAAQRA SIEVWACTPA DLQARGDQLS AIAVPVVAEP 

        70         80         90        100        110        120 
WISTGEPRSL PLTDFACIWM RKDPPVDEGY LYATHLLELA ERAGVCVLNR PAALRAWNEK 

       130        140        150        160        170        180 
LGALRFNNLM APTLVASRVS ELAAFAREQE EVVLKPLGGR AGQGLVRVAG AAPGLEALLE 

       190        200        210        220        230        240 
LVTDQEQLPV MVQRFLPAVI EGDKRILLVD GEPLGAVNRR PKAGDFRSNL AMGGRPEPTE 

       250        260        270        280        290        300 
LDSRELQICA ELAPVLREQG LFFVGIDVID GLLSEINVTS PTGIREVERL KGVPLADQVI 


ARLLVSLG 

« Hide

References

[1]"Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche differentiation."
Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C. expand/collapse author list , Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R., Chisholm S.W.
Nature 424:1042-1047(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MIT 9313.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX548175 Genomic DNA. Translation: CAE22235.1. Different initiation.
RefSeqNP_895886.1. NC_005071.1.

3D structure databases

ProteinModelPortalQ7TUK9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING74547.PMT2061.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE22235; CAE22235; PMT_2061.
GeneID1729231.
KEGGpmt:PMT2061.
PATRIC23012973. VBIProMar135351_2609.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0189.
KOK01920.
OrthoDBEOG6WMHWB.
ProtClustDBPRK05246.

Enzyme and pathway databases

UniPathwayUPA00142; UER00210.

Family and domain databases

Gene3D3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
HAMAPMF_00162. GSH_S.
InterProIPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR006284. Glut_synth_pro.
IPR004218. GSHS_ATP-bd.
IPR004215. GSHS_N.
IPR016185. PreATP-grasp_dom.
[Graphical view]
PfamPF02955. GSH-S_ATP. 1 hit.
PF02951. GSH-S_N. 1 hit.
[Graphical view]
SUPFAMSSF52440. SSF52440. 1 hit.
TIGRFAMsTIGR01380. glut_syn. 1 hit.
PROSITEPS50975. ATP_GRASP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGSHB_PROMM
AccessionPrimary (citable) accession number: Q7TUK9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: December 15, 2003
Last modified: February 19, 2014
This is version 65 of the entry and version 2 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