Reviewed, UniProtKB/Swiss-Prot Q09845 (GPD2_SCHPO)

Names and origin

Protein names

Recommended name:
    Glycerol-3-phosphate dehydrogenase [NAD+] 2
    EC=1.1.1.8

Gene names

Name:	gpd2
ORF Names:	SPAC23D3.04c

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

General annotation (Comments)

Catalytic activity	sn-glycerol 3-phosphate + NAD(+) = glycerone phosphate + NADH.
Subcellular location	CytoplasmPotential.
Sequence similarities	Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	NAD
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro glycerol biosynthetic process Ref.1 Inferred from mutant phenotype. Source: GeneDB_SPombe glycerol-3-phosphate catabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	glycerol-3-phosphate dehydrogenase complex Inferred from electronic annotation. Source: InterPro
Molecular function	NAD binding Inferred from electronic annotation. Source: InterPro glycerol-3-phosphate dehydrogenase (NAD+) activity Ref.1 Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 373	373	Glycerol-3-phosphate dehydrogenase [NAD+] 2		PRO_0000138096
Regions
	Nucleotide binding	31 – 36	6	NAD By similarity
	Region	300 – 301	2	Substrate binding By similarity
Sites
	Active site	236	1	Proton acceptor By similarity
	Binding site	123	1	NAD By similarity
	Binding site	146	1	NAD; via amide nitrogen By similarity
	Binding site	146	1	Substrate By similarity
	Binding site	179	1	NAD; via amide nitrogen By similarity
	Binding site	300	1	NAD By similarity
	Binding site	329	1	NAD By similarity
Amino acid modifications
	Modified residue	15	1	Phosphoserine

Sequences

	Sequence		Length	Mass (Da)
	Q09845-1 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: 7C3AFBC3DFFB470E	FASTA	373	40,874
	10 20 30 40 50 60 MTVAALNKLS ALSGSIQKSF SPKLISVGII GSGNWGTAIA KICGENAKAH PDIFHPQVHM 70 80 90 100 110 120 WMYEEKIQHE GKECNLTEVF NTTHENVKYL KGIKCPSNVF ANPDIRDVGS RSDILVWVLP 130 140 150 160 170 180 HQFVVRICNQ LKGCLKKDAV AISCIKGVSV TKDRVRLFSD IIEENTGMYC GVLSGANIAS 190 200 210 220 230 240 EVAQEKFCET TIGYLPNSSV NPRYTPKTIQ ALFNRPYFRV NIVEDVPGVA LGGALKNIVA 250 260 270 280 290 300 VAAGIIDGLE LGDNTKSAVM RIGLLEMQKF GRMFFDCKPL TMSEESCGIA DLITTCLGGR 310 320 330 340 350 360 NHKCAVAFVK TGKPMHVVEQ ELLDGQKLQG AATAKEVYEF LDNQNKVSEF PLFTAVYRIV 370 YEGLPPNKLL EAI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Osmoregulation of fission yeast: cloning of two distinct genes encoding glycerol-3-phosphate dehydrogenase, one of which is responsible for osmotolerance for growth." Ohmiya R., Yamada H., Nakashima K., Aiba H., Mizuno T. Mol. Microbiol. 18:963-973(1995) [PubMed: 8825100] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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-15, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D50797 Genomic DNA. Translation: BAA09425.1. CU329670 Genomic DNA. Translation: CAA91239.1.
PIR	JC6053.
RefSeq	NP_594542.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2541502.
KEGG	spo:SPAC23D3.04c.
NMPDR	fig|4896.1.peg.4512.
Organism-specific databases
GeneDB_Spombe	SPAC23D3.04c.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-002639-MON.
Gene expression databases
ArrayExpress	Q09845.
Family and domain databases
InterPro	IPR013328. DHase_multihelical. IPR016040. NAD(P)-bd. IPR017751. NAD-dep_Gly3P_DH_euk. IPR006168. NAD-dep_Gly3P_DHase. IPR011128. NAD-dep_Gly3P_DHase_N. IPR006109. NAD_Gly3P_DHase_C. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. G3DSA:1.10.1040.10. Opine_DH. 1 hit.
PANTHER	PTHR11728. NAD_Gly3P_DH. 1 hit.
Pfam	PF07479. NAD_Gly3P_dh_C. 1 hit. PF01210. NAD_Gly3P_dh_N. 1 hit. [Graphical view]
PIRSF	PIRSF000114. Glycerol-3-P_dh. 1 hit.
PRINTS	PR00077. GPDHDRGNASE.
ProDom	PD001278. NAD_Gly3P_C. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00957. NAD_G3PDH. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GPD2_SCHPO

Accession

Primary (citable) accession number: Q09845

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	November 25, 2008
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)