Reviewed, UniProtKB/Swiss-Prot P78958 (G3P1_SCHPO)

Names and origin

Protein names

Recommended name:
    Glyceraldehyde-3-phosphate dehydrogenase 1
      Short name=GAPDH 1
    EC=1.2.1.12

Gene names

Name:	tdh1
Synonyms:	gpd1
ORF Names:	SPBC32F12.11

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	336 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH.
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5.
Subunit structure	Homotetramer By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm
Ligand	NAD
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cellular response to hydrogen peroxide Inferred from mutant phenotype. Source: GeneDB_SPombe gluconeogenesis Inferred by curator. Source: GeneDB_SPombe glycolysis Inferred by curator. Source: GeneDB_SPombe oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW regulation of stress-activated protein kinase signaling pathway Inferred from mutant phenotype. Source: GeneDB_SPombe regulation of two-component signal transduction Inferred from physical interaction. Source: GeneDB_SPombe stress-activated protein kinase signaling pathway Inferred from mutant phenotype. Source: GeneDB_SPombe
Cellular component	cytosol Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	NAD or NADH binding Inferred from electronic annotation. Source: InterPro glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity Non-traceable author statement. Source: GeneDB_SPombe protein binding Inferred from physical interaction. Source: GeneDB_SPombe
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 336	336	Glyceraldehyde-3-phosphate dehydrogenase 1		PRO_0000145580
Regions
	Nucleotide binding	13 – 14	2	NAD By similarity
	Region	151 – 153	3	Glyceraldehyde 3-phosphate binding By similarity
	Region	211 – 212	2	Glyceraldehyde 3-phosphate binding By similarity
Sites
	Active site	152	1	Nucleophile By similarity
	Binding site	35	1	NAD By similarity
	Binding site	80	1	NAD; via carbonyl oxygen By similarity
	Binding site	182	1	Glyceraldehyde 3-phosphate By similarity
	Binding site	234	1	Glyceraldehyde 3-phosphate By similarity
	Binding site	316	1	NAD By similarity
	Site	179	1	Activates thiol group during catalysis By similarity
Amino acid modifications
	Modified residue	59	1	Phosphoserine Ref.3
	Modified residue	125	1	Phosphoserine Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P78958-1 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: 38E58E194FF4747A	FASTA	336	35,870
	10 20 30 40 50 60 MAIPKVGING FGRIGRIVLR NALVAKTIQV VAINDPFIDL EYMAYMFKYD STHGRFDGSV 70 80 90 100 110 120 EIKDGKLVID GNAIDVHNER DPADIKWSTS GADYVIESTG VFTTQETASA HLKGGAKRVI 130 140 150 160 170 180 ISAPSKDAPM YVVGVNEEKF NPSEKVISNA SCTTNCLAPL AKVINDTFGI EEGLMTTVHA 190 200 210 220 230 240 TTATQKTVDG PSKKDWRGGR GASANIIPSS TGAAKAVGKV IPALNGKLTG MAFRVPTPDV 250 260 270 280 290 300 SVVDLTVKLA KPTNYEDIKA AIKAASEGPM KGVLGYTEDA VVSTDFCGDN HSSIFDASAG 310 320 330 IQLSPQFVKL VSWYDNEWGY SRRVVDLVAY TAAKDN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.
[3]	"Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59 AND SER-125, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X85332 mRNA. Translation: CAA59681.1. CU329671 Genomic DNA. Translation: CAA19372.1.
PIR	T40235.
RefSeq	NP_596154.1.
3D structure databases
HSSP	HSSP built from PDB template 1DSS based on UniProtKB P56649.
SMR	P78958. Positions 5-335.
ModBase	Search...
Protein-protein interaction databases
IntAct	P78958. 2 interactions.
Genome annotation databases
GeneID	2540547.
KEGG	spo:SPBC32F12.11.
NMPDR	fig|4896.1.peg.2020.
Organism-specific databases
GeneDB_Spombe	SPBC32F12.11.
Phylogenomic databases
OMA	P78958. RLELECH.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-004190-MON.
BRENDA	1.2.1.12. 653.
Gene expression databases
ArrayExpress	P78958.
Family and domain databases
InterPro	IPR000173. GlycerAld_3-P_DH. IPR006424. Glyceraldehyde-3-P_DH_1. [Graphical view]
PANTHER	PTHR10836. GAP_DH. 1 hit.
Pfam	PF02800. Gp_dh_C. 1 hit. PF00044. Gp_dh_N. 1 hit. [Graphical view]
PIRSF	PIRSF000149. GAP_DH. 1 hit.
PRINTS	PR00078. G3PDHDRGNASE.
TIGRFAMs	TIGR01534. GAPDH-I. 1 hit.
PROSITE	PS00071. GAPDH. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

G3P1_SCHPO

Accession

Primary (citable) accession number: P78958

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	May 1, 1997
Last modified:	June 16, 2009
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)