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P35669 (GSHB_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 116. 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 synthetase large chain

Short name=GSH synthetase large chain
Short name=GSH-S
EC=6.3.2.3
Alternative name(s):
Glutathione synthase large chain
Phytochelatin synthetase
Gene names
Name:gsa1
Synonyms:gsh2
ORF Names:SPAC3F10.04
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length498 AA.
Sequence statusComplete.
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

Heterodimer composed of a large and a small chain.

Sequence similarities

Belongs to the eukaryotic GSH synthase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 498498Glutathione synthetase large chain
PRO_0000211265

Regions

Nucleotide binding387 – 39610ATP By similarity
Nucleotide binding420 – 4234ATP By similarity
Region150 – 1534Substrate binding By similarity
Region233 – 2353Substrate binding By similarity
Region291 – 2944Substrate binding By similarity
Region484 – 4852Substrate binding By similarity

Sites

Metal binding1461Magnesium By similarity
Metal binding1481Magnesium By similarity
Metal binding3911Magnesium By similarity
Binding site1281Substrate By similarity
Binding site1461ATP By similarity
Binding site2391Substrate By similarity
Binding site3301ATP By similarity
Binding site3981ATP By similarity
Binding site4461ATP By similarity
Binding site4731Substrate By similarity
Binding site4751ATP By similarity
Binding site4811ATP; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue3561Phosphoserine Ref.5

Experimental info

Sequence conflict1321M → T in AAL41009. Ref.2
Sequence conflict2631N → T in AAA35307. Ref.4
Sequence conflict3041A → R in AAA35307. Ref.4
Sequence conflict3301K → E in AAA35307. Ref.4
Sequence conflict4581K → N in AAA35307. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P35669 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: AD2921C5AD667ABF

FASTA49856,153
        10         20         30         40         50         60 
MEIEKYTPEQ IEELGKGARD FAFAHGVVFT ELSVSKEGRN IATQIPITLF PSVIPHGAFV 

        70         80         90        100        110        120 
EAVSVQKAYN KLYAKIANDY EFLRLHLQSI TKYDEFMNKL WNLYQKHREA VAHLKENQFQ 

       130        140        150        160        170        180 
PLSLGVFRSD YMVHQDDSFI GCKQVEFNTI SVSFGGVSKA VSNLHAYCSQ SGLYRKPLTT 

       190        200        210        220        230        240 
NYLTVNTSVS GICTGISNAV DAYRDYVKNI TSKMNIASDN TKPIVLFVVK GGERNITDQR 

       250        260        270        280        290        300 
TLEYELLNRF HVISKRIDIA ELNSLIHDKS SNKLYMKTSF TTYEVAVVYY RVGYALDDYP 

       310        320        330        340        350        360 
SQEAWDMRLT IENTLAIKCP SISTHLAGSK KIQQVLAESN ALERFLEGDE LQAVRSTFAD 

       370        380        390        400        410        420 
MYPLDDTPRG KEGIKLAFEK PEDFVLKPQR EGGGNNTYGK DIPGLLSKMP QEEWDSYILM 

       430        440        450        460        470        480 
RYINAVPSQN YILKGERPEK FDVVDEIGIL GTIVWNIKTD EVVQNGQSGF ICRTKPKKTN 

       490 
EGGVATGYAS LSSIELSE 

« Hide

References

« Hide 'large scale' references
[1]"Biosynthesis of phytochelatins in the fission yeast. Phytochelatin synthesis: a second role for the glutathione synthetase gene of Schizosaccharomyces pombe."
Al-Lahham A., Rohde V., Heim P., Leuchter R., Veeck J., Wunderlich C., Wolf K., Zimmermann M.
Yeast 15:385-396(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: SP011.
[2]Shin Y.H., Lim C.-J.
Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[4]"Cloning and sequencing of the gene encoding the large subunit of glutathione synthetase of Schizosaccharomyces pombe."
Mutoh N., Nakagawa C.W., Ando S., Tanabe K., Hayashi Y.
Biochem. Biophys. Res. Commun. 181:430-436(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 214-498, PROTEIN SEQUENCE OF 218-229 AND 392-403.
Strain: 972 / ATCC 24843.
[5]"Phosphoproteome analysis of fission yeast."
Wilson-Grady J.T., Villen J., Gygi S.P.
J. Proteome Res. 7:1088-1097(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329670 Genomic DNA. Translation: CAA93302.1.
AF448236 Genomic DNA. Translation: AAL41009.1.
Y08414 Genomic DNA. Translation: CAA69691.1.
M85179 Genomic DNA. Translation: AAA35307.1.
PIRJT0961.
T38705.
RefSeqNP_593936.1. NM_001019364.2.

3D structure databases

ProteinModelPortalP35669.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid279340. 8 interactions.
MINTMINT-4688612.
STRING4896.SPAC3F10.04-1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC3F10.04.1; SPAC3F10.04.1:pep; SPAC3F10.04.
GeneID2542896.
KEGGspo:SPAC3F10.04.

Organism-specific databases

PomBaseSPAC3F10.04.

Phylogenomic databases

eggNOGNOG329040.
HOGENOMHOG000172641.
KOK01920.
OMASARIAMI.
OrthoDBEOG7GBG71.
PhylomeDBP35669.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-10022.
UniPathwayUPA00142; UER00210.

Family and domain databases

Gene3D1.10.1080.10. 2 hits.
3.30.1490.50. 1 hit.
3.30.1490.80. 1 hit.
3.30.470.20. 1 hit.
3.40.50.1760. 1 hit.
InterProIPR013816. ATP_grasp_subdomain_2.
IPR004887. 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

NextBio20803935.
PROP35669.

Entry information

Entry nameGSHB_SCHPO
AccessionPrimary (citable) accession number: P35669
Secondary accession number(s): Q8X1A1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways