Reviewed, UniProtKB/Swiss-Prot O43026 (G3P2_SCHPO)

Names and origin

Protein names

Recommended name:
    Glyceraldehyde-3-phosphate dehydrogenase 2
      Short name=GAPDH 2
    EC=1.2.1.12

Gene names

Name:	gpd3
ORF Names:	SPBC354.12

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	335 AA.
Sequence status	Complete.
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	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
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 Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 335	335	Glyceraldehyde-3-phosphate dehydrogenase 2		PRO_0000145581
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	125	1	Phosphoserine Ref.2
	Modified residue	151	1	Phosphoserine Ref.2
	Modified residue	153	1	Phosphothreonine Ref.2
	Modified residue	154	1	Phosphothreonine Ref.2
	Modified residue	182	1	Phosphothreonine Ref.2
	Modified residue	184	1	Phosphothreonine Ref.2
	Modified residue	192	1	Phosphoserine Ref.2
	Modified residue	203	1	Phosphoserine Ref.2
	Modified residue	209	1	Phosphoserine Ref.2
	Modified residue	211	1	Phosphothreonine Ref.2
	Modified residue	237	1	Phosphothreonine Ref.2
	Modified residue	241	1	Phosphoserine Ref.2

Sequences

	Sequence		Length	Mass (Da)
	O43026-1 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: F0A0FB6AED5EB625	FASTA	335	35,675
	10 20 30 40 50 60 MAIPKVGING FGRIGRIVLR NAILTGKIQV VAVNDPFIDL DYMAYMFKYD STHGRFEGSV 70 80 90 100 110 120 ETKGGKLVID GHSIDVHNER DPANIKWSAS GAEYVIESTG VFTTKETASA HLKGGAKRVI 130 140 150 160 170 180 ISAPSKDAPM FVVGVNLEKF 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 KGVLGYTEDS VVSTDFCGDN HSSIFDASAG 310 320 330 IQLSPQFVKL VSWYDNEWGY SHRVVDLVAY TASKD

References

[1]

"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.

[2]

"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-125; SER-151; THR-153; THR-154; THR-182; THR-184; SER-192; SER-203; SER-209; THR-211; THR-237 AND SER-241, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329671 Genomic DNA. Translation: CAA17812.1.
PIR	T40292.
RefSeq	NP_595236.1.
3D structure databases
SMR	O43026. Positions 5-335.
ModBase	Search...
Protein-protein interaction databases
IntAct	O43026. 1 interaction.
STRING	O43026.
Genome annotation databases
GeneID	2540975.
GenomeReviews	Gene locus gpd3 in contig CU329671_GR.
KEGG	spo:SPBC354.12.
NMPDR	fig|4896.1.peg.1102.
Organism-specific databases
GeneDB_Spombe	SPBC354.12.
Phylogenomic databases
eggNOG	fuNOG04196.
HOGENOM	HBG571736.
OMA	KETASAH.
OrthoDB	EOG90S1Z3.
PhylomeDB	O43026.
Enzyme and pathway databases
BRENDA	1.2.1.12. 653.
Gene expression databases
ArrayExpress	O43026.
Family and domain databases
InterPro	IPR020830. GlycerAld_3-P_DH_AS. IPR020829. GlycerAld_3-P_DH_cat. IPR020832. GlycerAld_3-P_DH_cat_sub. IPR020831. GlycerAld_3-P_DH_family. IPR020828. GlycerAld_3-P_DH_NAD(P)_bd. IPR000173. GlycerAld_3-P_DH_subfam. IPR006424. Glyceraldehyde-3-P_DH_1. IPR016040. NAD(P)-bd_dom. [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.
SMART	SM00846. Gp_dh_N. 1 hit. [Graphical view]
TIGRFAMs	TIGR01534. GAPDH-I. 1 hit.
PROSITE	PS00071. GAPDH. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

G3P2_SCHPO

Accession

Primary (citable) accession number: O43026

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	June 1, 1998
Last modified:	February 9, 2010
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)