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Protein

Glutathione synthetase large chain

Gene

gsa1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity

Pathway: glutathione biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes glutathione from L-cysteine and L-glutamate.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Putative glutamate--cysteine ligase regulatory subunit (SPCC737.06c), Glutamate--cysteine ligase (gcs1)
  2. Glutathione synthetase large chain (gsa1)
This subpathway is part of the pathway glutathione biosynthesis, which is itself part of Sulfur metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes glutathione from L-cysteine and L-glutamate, the pathway glutathione biosynthesis and in Sulfur metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei128 – 1281SubstrateBy similarity
Metal bindingi146 – 1461MagnesiumBy similarity
Binding sitei146 – 1461ATPBy similarity
Metal bindingi148 – 1481MagnesiumBy similarity
Binding sitei239 – 2391SubstrateBy similarity
Binding sitei330 – 3301ATPBy similarity
Metal bindingi391 – 3911MagnesiumBy similarity
Binding sitei398 – 3981ATPBy similarity
Binding sitei446 – 4461ATPBy similarity
Binding sitei473 – 4731SubstrateBy similarity
Binding sitei475 – 4751ATPBy similarity
Binding sitei481 – 4811ATP; via carbonyl oxygenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi387 – 39610ATPBy similarity
Nucleotide bindingi420 – 4234ATPBy similarity

GO - Molecular functioni

GO - Biological processi

  • cellular response to cadmium ion Source: PomBase
  • detoxification of cadmium ion Source: PomBase
  • glutathione biosynthetic process Source: PomBase
  • glutathione transport Source: PomBase
  • phytochelatin biosynthetic process Source: PomBase
  • phytochelatin-metal complex formation Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Glutathione biosynthesis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-10022.
BRENDAi6.3.2.3. 5613.
ReactomeiREACT_313682. Glutathione synthesis and recycling.
UniPathwayiUPA00142; UER00210.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione synthetase large chain (EC:6.3.2.3)
Short name:
GSH synthetase large chain
Short name:
GSH-S
Alternative name(s):
Glutathione synthase large chain
Phytochelatin synthetase
Gene namesi
Name:gsa1
Synonyms:gsh2
ORF Names:SPAC3F10.04
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC3F10.04.
PomBaseiSPAC3F10.04. gsa1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: PomBase
  • glutathione synthase complex Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 498498Glutathione synthetase large chainPRO_0000211265Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei356 – 3561Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP35669.

Interactioni

Subunit structurei

Heterodimer composed of a large and a small chain.

Protein-protein interaction databases

BioGridi279340. 8 interactions.
MINTiMINT-4688612.
STRINGi4896.SPAC3F10.04.1.

Structurei

3D structure databases

ProteinModelPortaliP35669.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni150 – 1534Substrate bindingBy similarity
Regioni233 – 2353Substrate bindingBy similarity
Regioni291 – 2944Substrate bindingBy similarity
Regioni484 – 4852Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the eukaryotic GSH synthase family.Curated

Phylogenomic databases

eggNOGiNOG329040.
HOGENOMiHOG000172641.
InParanoidiP35669.
KOiK01920.
OMAiEGRNIAT.
OrthoDBiEOG7GBG71.
PhylomeDBiP35669.

Family and domain databases

Gene3Di1.10.1080.10. 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.
InterProiIPR013816. 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]
PANTHERiPTHR11130. PTHR11130. 1 hit.
PfamiPF03917. GSH_synth_ATP. 1 hit.
PF03199. GSH_synthase. 1 hit.
[Graphical view]
PIRSFiPIRSF001558. GSHase. 1 hit.
SUPFAMiSSF52440. SSF52440. 1 hit.
TIGRFAMsiTIGR01986. glut_syn_euk. 1 hit.

Sequencei

Sequence statusi: Complete.

P35669-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEIEKYTPEQ IEELGKGARD FAFAHGVVFT ELSVSKEGRN IATQIPITLF
60 70 80 90 100
PSVIPHGAFV EAVSVQKAYN KLYAKIANDY EFLRLHLQSI TKYDEFMNKL
110 120 130 140 150
WNLYQKHREA VAHLKENQFQ PLSLGVFRSD YMVHQDDSFI GCKQVEFNTI
160 170 180 190 200
SVSFGGVSKA VSNLHAYCSQ SGLYRKPLTT NYLTVNTSVS GICTGISNAV
210 220 230 240 250
DAYRDYVKNI TSKMNIASDN TKPIVLFVVK GGERNITDQR TLEYELLNRF
260 270 280 290 300
HVISKRIDIA ELNSLIHDKS SNKLYMKTSF TTYEVAVVYY RVGYALDDYP
310 320 330 340 350
SQEAWDMRLT IENTLAIKCP SISTHLAGSK KIQQVLAESN ALERFLEGDE
360 370 380 390 400
LQAVRSTFAD MYPLDDTPRG KEGIKLAFEK PEDFVLKPQR EGGGNNTYGK
410 420 430 440 450
DIPGLLSKMP QEEWDSYILM RYINAVPSQN YILKGERPEK FDVVDEIGIL
460 470 480 490
GTIVWNIKTD EVVQNGQSGF ICRTKPKKTN EGGVATGYAS LSSIELSE
Length:498
Mass (Da):56,153
Last modified:October 1, 1996 - v2
Checksum:iAD2921C5AD667ABF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti132 – 1321M → T in AAL41009 (Ref. 2) Curated
Sequence conflicti263 – 2631N → T in AAA35307 (PubMed:1958212).Curated
Sequence conflicti304 – 3041A → R in AAA35307 (PubMed:1958212).Curated
Sequence conflicti330 – 3301K → E in AAA35307 (PubMed:1958212).Curated
Sequence conflicti458 – 4581K → N in AAA35307 (PubMed:1958212).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAA93302.1.
AF448236 Genomic DNA. Translation: AAL41009.1.
Y08414 Genomic DNA. Translation: CAA69691.1.
M85179 Genomic DNA. Translation: AAA35307.1.
PIRiJT0961.
T38705.
RefSeqiNP_593936.1. NM_001019364.2.

Genome annotation databases

EnsemblFungiiSPAC3F10.04.1; SPAC3F10.04.1:pep; SPAC3F10.04.
GeneIDi2542896.
KEGGispo:SPAC3F10.04.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAA93302.1.
AF448236 Genomic DNA. Translation: AAL41009.1.
Y08414 Genomic DNA. Translation: CAA69691.1.
M85179 Genomic DNA. Translation: AAA35307.1.
PIRiJT0961.
T38705.
RefSeqiNP_593936.1. NM_001019364.2.

3D structure databases

ProteinModelPortaliP35669.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi279340. 8 interactions.
MINTiMINT-4688612.
STRINGi4896.SPAC3F10.04.1.

Proteomic databases

MaxQBiP35669.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC3F10.04.1; SPAC3F10.04.1:pep; SPAC3F10.04.
GeneIDi2542896.
KEGGispo:SPAC3F10.04.

Organism-specific databases

EuPathDBiFungiDB:SPAC3F10.04.
PomBaseiSPAC3F10.04. gsa1.

Phylogenomic databases

eggNOGiNOG329040.
HOGENOMiHOG000172641.
InParanoidiP35669.
KOiK01920.
OMAiEGRNIAT.
OrthoDBiEOG7GBG71.
PhylomeDBiP35669.

Enzyme and pathway databases

UniPathwayiUPA00142; UER00210.
BioCyciMetaCyc:MONOMER-10022.
BRENDAi6.3.2.3. 5613.
ReactomeiREACT_313682. Glutathione synthesis and recycling.

Miscellaneous databases

NextBioi20803935.
PROiP35669.

Family and domain databases

Gene3Di1.10.1080.10. 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.
InterProiIPR013816. 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]
PANTHERiPTHR11130. PTHR11130. 1 hit.
PfamiPF03917. GSH_synth_ATP. 1 hit.
PF03199. GSH_synthase. 1 hit.
[Graphical view]
PIRSFiPIRSF001558. GSHase. 1 hit.
SUPFAMiSSF52440. SSF52440. 1 hit.
TIGRFAMsiTIGR01986. glut_syn_euk. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiGSHB_SCHPO
AccessioniPrimary (citable) accession number: P35669
Secondary accession number(s): Q8X1A1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: October 1, 1996
Last modified: June 24, 2015
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.