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P46413 (GSHB_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 104. 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

Short name=GSH synthetase
Short name=GSH-S
EC=6.3.2.3
Alternative name(s):
Glutathione synthase
Gene names
Name:Gss
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length474 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 1 magnesium ion per subunit By similarity.

Pathway

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

Subunit structure

Homodimer.

Sequence similarities

Belongs to the eukaryotic GSH synthase family.

Ontologies

Keywords
   Biological processGlutathione biosynthesis
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionLigase
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processaging

Inferred from expression pattern PubMed 18653662. Source: RGD

glutathione biosynthetic process

Inferred from direct assay PubMed 10964706. Source: RGD

response to amino acid

Inferred from expression pattern PubMed 19212806. Source: RGD

response to cadmium ion

Inferred from electronic annotation. Source: Ensembl

response to nutrient levels

Inferred from expression pattern PubMed 19212806. Source: RGD

response to tumor necrosis factor

Inferred from expression pattern PubMed 16011481. Source: RGD

response to xenobiotic stimulus

Inferred from expression pattern PubMed 18653662. Source: RGD

   Molecular_functionATP binding

Inferred from sequence or structural similarity. Source: UniProtKB

glutathione binding

Inferred from sequence or structural similarity. Source: UniProtKB

glutathione synthase activity

Inferred from direct assay PubMed 10964706. Source: RGD

glycine binding

Inferred from direct assay PubMed 10964706. Source: RGD

magnesium ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

peptide binding

Inferred from physical interaction PubMed 10964706. Source: RGD

protein homodimerization activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 474473Glutathione synthetase
PRO_0000211263

Regions

Nucleotide binding364 – 37310ATP By similarity
Nucleotide binding398 – 4014ATP By similarity
Region148 – 1514Substrate binding By similarity
Region214 – 2163Substrate binding By similarity
Region267 – 2704Substrate binding By similarity
Region461 – 4622Substrate binding By similarity

Sites

Metal binding1441Magnesium By similarity
Metal binding1461Magnesium By similarity
Metal binding3681Magnesium By similarity
Binding site1251Substrate By similarity
Binding site1441ATP By similarity
Binding site2201Substrate By similarity
Binding site3051ATP By similarity
Binding site3751ATP By similarity
Binding site4251ATP By similarity
Binding site4501Substrate By similarity
Binding site4521ATP By similarity
Binding site4581ATP; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity

Sequences

Sequence LengthMass (Da)Tools
P46413 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 962B742FD19851A4

FASTA47452,345
        10         20         30         40         50         60 
MATSWGSILQ DEKQLEELAQ QAIDRALAEG VLLRSAKNPS SSDVVTYAPF TLFPSPVPST 

        70         80         90        100        110        120 
LLEQAYAVQM DFNILVDAVS QNSAFLEQTL SSTIKKDEYT ARLFDIYKQV LKEGIAQTVF 

       130        140        150        160        170        180 
LGLNRSDYMF QCSADGSKAL KQIEINTISA SFGGLASRTP AVHRHVLNVL NKTNEASKIL 

       190        200        210        220        230        240 
SNNPSKGLAL GIAKAWELYG SANAVVLLIA QEKERNIFDQ RAIENELLDR KIHVIRRRFE 

       250        260        270        280        290        300 
DVSERGSLDQ NRRLFMEDQE VAVVYFRDGY MPSQYNAQNW EARLLLERSC AAKCPDIATQ 

       310        320        330        340        350        360 
LAGTKKVQQE LSRVGLLEAL LPGQPEAVAR LRATFAGLYS LDMGEEGDQA VAEALAAPSH 

       370        380        390        400        410        420 
FVLKPQREGG GNNFYGEEMV HALEQLKDSE ERASYILMEK IEPEPFRNCL LRPGSPAQVV 

       430        440        450        460        470 
QCISELGIFG VYVRQGTTLV MNKHVGHLLR TKAIEHADGG VAAGVAVLDN PYPV 

« Hide

References

« Hide 'large scale' references
[1]"Amino acid sequence of rat kidney glutathione synthetase."
Huang C.-S., He W., Meister A., Anderson M.E.
Proc. Natl. Acad. Sci. U.S.A. 92:1232-1236(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Kidney.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L38615 mRNA. Translation: AAA64618.1.
BC078700 mRNA. Translation: AAH78700.1.
PIRI59346.
RefSeqNP_037094.1. NM_012962.1.
XP_006235370.1. XM_006235308.1.
UniGeneRn.1692.

3D structure databases

ProteinModelPortalP46413.
SMRP46413. Positions 3-474.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000025657.

PTM databases

PhosphoSiteP46413.

Proteomic databases

PaxDbP46413.
PRIDEP46413.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000025657; ENSRNOP00000025657; ENSRNOG00000018964.
GeneID25458.
KEGGrno:25458.
UCSCRGD:2752. rat.

Organism-specific databases

CTD2937.
RGD2752. Gss.

Phylogenomic databases

eggNOGNOG329040.
GeneTreeENSGT00390000013764.
HOGENOMHOG000172641.
HOVERGENHBG002458.
InParanoidP46413.
KOK01920.
OMAFENCLLR.
OrthoDBEOG757CXD.
PhylomeDBP46413.
TreeFamTF105187.

Enzyme and pathway databases

UniPathwayUPA00142; UER00210.

Gene expression databases

GenevestigatorP46413.

Family and domain databases

Gene3D1.10.1080.10. 2 hits.
3.30.1490.50. 1 hit.
3.30.1490.80. 2 hits.
3.40.50.1760. 1 hit.
InterProIPR004887. Glutathione_synth_subst-bd_euk.
IPR014042. Glutathione_synthase_a-hlx_euk.
IPR014709. Glutathione_synthase_dom.
IPR005615. Glutathione_synthase_euk.
IPR014049. Glutathione_synthase_N_euk.
IPR016185. PreATP-grasp_dom.
[Graphical view]
PANTHERPTHR11130. PTHR11130. 1 hit.
PfamPF03917. GSH_synth_ATP. 1 hit.
PF03199. GSH_synthase. 1 hit.
[Graphical view]
PIRSFPIRSF001558. GSHase. 1 hit.
SUPFAMSSF52440. SSF52440. 1 hit.
TIGRFAMsTIGR01986. glut_syn_euk. 1 hit.
ProtoNetSearch...

Other

NextBio606725.
PROP46413.

Entry information

Entry nameGSHB_RAT
AccessionPrimary (citable) accession number: P46413
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 16, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways