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Protein

Glyceraldehyde-3-phosphate dehydrogenase 1

Gene

tdh1

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

D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH.PROSITE-ProRule annotation

Pathwayi: glycolysis

This protein is involved in step 1 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Glyceraldehyde-3-phosphate dehydrogenase 2 (gpd3), Glyceraldehyde-3-phosphate dehydrogenase 1 (tdh1)
  2. Phosphoglycerate kinase (pgk1)
  3. Phosphoglycerate mutase (gpm1)
  4. Enolase 1-2 (eno102), Enolase 1-1 (eno101)
  5. Pyruvate kinase (pyk1)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei35 – 351NADBy similarity
Binding sitei80 – 801NAD; via carbonyl oxygenBy similarity
Active sitei152 – 1521NucleophilePROSITE-ProRule annotation
Sitei179 – 1791Activates thiol group during catalysisBy similarity
Binding sitei182 – 1821Glyceraldehyde 3-phosphateBy similarity
Binding sitei234 – 2341Glyceraldehyde 3-phosphateBy similarity
Binding sitei316 – 3161NADBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi13 – 142NADBy similarity

GO - Molecular functioni

GO - Biological processi

  • canonical glycolysis Source: PomBase
  • detection of oxidative stress Source: PomBase
  • gluconeogenesis Source: PomBase
  • positive regulation of phosphorelay signal transduction system involved in hydrogen peroxide mediated signaling pathway Source: PomBase
  • positive regulation of stress-activated MAPK cascade Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

NAD

Enzyme and pathway databases

ReactomeiR-SPO-70171. Glycolysis.
R-SPO-70263. Gluconeogenesis.
UniPathwayiUPA00109; UER00184.

Names & Taxonomyi

Protein namesi
Recommended name:
Glyceraldehyde-3-phosphate dehydrogenase 1 (EC:1.2.1.12)
Short name:
GAPDH 1
Gene namesi
Name:tdh1
Synonyms:gpd1
ORF Names:SPBC32F12.11
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC32F12.11.
PomBaseiSPBC32F12.11. tdh1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: PomBase
  • fungal-type cell wall Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 336336Glyceraldehyde-3-phosphate dehydrogenase 1PRO_0000145580Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei59 – 591Phosphoserine1 Publication
Modified residuei125 – 1251Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP78958.
PRIDEiP78958.

PTM databases

iPTMnetiP78958.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

BioGridi277074. 22 interactions.
IntActiP78958. 5 interactions.
MINTiMINT-1213925.

Structurei

3D structure databases

ProteinModelPortaliP78958.
SMRiP78958. Positions 5-335.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni151 – 1533Glyceraldehyde 3-phosphate bindingBy similarity
Regioni211 – 2122Glyceraldehyde 3-phosphate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000071678.
InParanoidiP78958.
KOiK00134.
OMAiMKAASSE.
OrthoDBiEOG70W3Q6.
PhylomeDBiP78958.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR020831. GlycerAld/Erythrose_P_DH.
IPR020830. GlycerAld_3-P_DH_AS.
IPR020829. GlycerAld_3-P_DH_cat.
IPR020828. GlycerAld_3-P_DH_NAD(P)-bd.
IPR006424. Glyceraldehyde-3-P_DH_1.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR10836. PTHR10836. 1 hit.
PfamiPF02800. Gp_dh_C. 1 hit.
PF00044. Gp_dh_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000149. GAP_DH. 1 hit.
PRINTSiPR00078. G3PDHDRGNASE.
SMARTiSM00846. Gp_dh_N. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01534. GAPDH-I. 1 hit.
PROSITEiPS00071. GAPDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P78958-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAIPKVGING FGRIGRIVLR NALVAKTIQV VAINDPFIDL EYMAYMFKYD
60 70 80 90 100
STHGRFDGSV EIKDGKLVID GNAIDVHNER DPADIKWSTS GADYVIESTG
110 120 130 140 150
VFTTQETASA HLKGGAKRVI ISAPSKDAPM YVVGVNEEKF NPSEKVISNA
160 170 180 190 200
SCTTNCLAPL AKVINDTFGI EEGLMTTVHA TTATQKTVDG PSKKDWRGGR
210 220 230 240 250
GASANIIPSS TGAAKAVGKV IPALNGKLTG MAFRVPTPDV SVVDLTVKLA
260 270 280 290 300
KPTNYEDIKA AIKAASEGPM KGVLGYTEDA VVSTDFCGDN HSSIFDASAG
310 320 330
IQLSPQFVKL VSWYDNEWGY SRRVVDLVAY TAAKDN
Length:336
Mass (Da):35,870
Last modified:May 1, 1997 - v1
Checksum:i38E58E194FF4747A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X85332 mRNA. Translation: CAA59681.1.
CU329671 Genomic DNA. Translation: CAA19372.1.
PIRiT40235.
RefSeqiNP_596154.1. NM_001022073.2.

Genome annotation databases

EnsemblFungiiSPBC32F12.11.1; SPBC32F12.11.1:pep; SPBC32F12.11.
GeneIDi2540547.
KEGGispo:SPBC32F12.11.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X85332 mRNA. Translation: CAA59681.1.
CU329671 Genomic DNA. Translation: CAA19372.1.
PIRiT40235.
RefSeqiNP_596154.1. NM_001022073.2.

3D structure databases

ProteinModelPortaliP78958.
SMRiP78958. Positions 5-335.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277074. 22 interactions.
IntActiP78958. 5 interactions.
MINTiMINT-1213925.

PTM databases

iPTMnetiP78958.

Proteomic databases

MaxQBiP78958.
PRIDEiP78958.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC32F12.11.1; SPBC32F12.11.1:pep; SPBC32F12.11.
GeneIDi2540547.
KEGGispo:SPBC32F12.11.

Organism-specific databases

EuPathDBiFungiDB:SPBC32F12.11.
PomBaseiSPBC32F12.11. tdh1.

Phylogenomic databases

HOGENOMiHOG000071678.
InParanoidiP78958.
KOiK00134.
OMAiMKAASSE.
OrthoDBiEOG70W3Q6.
PhylomeDBiP78958.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00184.
ReactomeiR-SPO-70171. Glycolysis.
R-SPO-70263. Gluconeogenesis.

Miscellaneous databases

NextBioi20801673.
PROiP78958.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR020831. GlycerAld/Erythrose_P_DH.
IPR020830. GlycerAld_3-P_DH_AS.
IPR020829. GlycerAld_3-P_DH_cat.
IPR020828. GlycerAld_3-P_DH_NAD(P)-bd.
IPR006424. Glyceraldehyde-3-P_DH_1.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR10836. PTHR10836. 1 hit.
PfamiPF02800. Gp_dh_C. 1 hit.
PF00044. Gp_dh_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000149. GAP_DH. 1 hit.
PRINTSiPR00078. G3PDHDRGNASE.
SMARTiSM00846. Gp_dh_N. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01534. GAPDH-I. 1 hit.
PROSITEiPS00071. GAPDH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Orlandi I., Popolo L., Cavadini P., Vai M.
    Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59 AND SER-125, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiG3P1_SCHPO
AccessioniPrimary (citable) accession number: P78958
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 1997
Last modified: May 11, 2016
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, 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

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 one 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.