Reviewed, UniProtKB/Swiss-Prot P21696 (GPD1_SCHPO)

Names and origin

Protein names

Recommended name:
    Glycerol-3-phosphate dehydrogenase [NAD+] 1
    EC=1.1.1.8
Alternative name(s):
    GPDH-C
      Short name=GPD-C

Gene names

Name:	gpd1
ORF Names:	SPBC215.05

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	385 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	Cytoplasm.
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	cellular response to stress Inferred from expression pattern. Source: GeneDB_SPombe cellular water homeostasis Ref.3 Inferred from expression pattern. Source: GeneDB_SPombe glycerol-3-phosphate catabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to osmotic stress Ref.3 Inferred from expression pattern. Source: GeneDB_SPombe
Cellular component	cytosol Inferred from direct assay. Source: GeneDB_SPombe glycerol-3-phosphate dehydrogenase complex Inferred from electronic annotation. Source: InterPro nucleus Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	NAD or NADH binding Inferred from electronic annotation. Source: InterPro glycerol-3-phosphate dehydrogenase (NAD+) activity Inferred from electronic annotation. Source: EC protein homodimerization activity 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 – 385	385	Glycerol-3-phosphate dehydrogenase [NAD+] 1		PRO_0000138095
Regions
	Nucleotide binding	29 – 34	6	NAD By similarity
	Region	296 – 297	2	Substrate binding By similarity
Sites
	Active site	232	1	Proton acceptor By similarity
	Binding site	121	1	NAD By similarity
	Binding site	144	1	NAD; via amide nitrogen By similarity
	Binding site	144	1	Substrate By similarity
	Binding site	177	1	NAD; via amide nitrogen By similarity
	Binding site	296	1	NAD By similarity
	Binding site	325	1	NAD By similarity
Amino acid modifications
	Modified residue	376	1	Phosphoserine Ref.4
	Modified residue	382	1	Phosphothreonine Ref.4
Experimental info
	Sequence conflict	54 – 56	3	SKV → GKG in CAA39630. Ref.1
	Sequence conflict	126 – 127	2	CD → WH in CAA39630. Ref.1
	Sequence conflict	153	1	Missing Ref.1
	Sequence conflict	209	1	F → S in CAA39630. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P21696-1 [UniParc]. Last modified January 11, 2001. Version 2. Checksum: 8061C294196516E1	FASTA	385	41,995
	10 20 30 40 50 60 MSGYGQQGVS AANIDSIRPK KRLSIGVVGS GNWGTAIAKI CGENARAHGH HFRSKVRMWV 70 80 90 100 110 120 FEEEIEYKGE KRKLTEVFNE AHENVKYLPG IECPPNVIAV PDVREVARRA DILVFVVPHQ 130 140 150 160 170 180 FIERVCDQMV GLIRPGAVGI SCIKGVAVSK EGVRLYSEVI SEKLGIYCGV LSGANVANEV 190 200 210 220 230 240 AREQFCETTI GFNPPNEVDI PREQIAAVFD RPYFSVVSVD DVAGVALGGA LKNVVAMAVG 250 260 270 280 290 300 FADGLEWGGN TKAAIMRRGL LEMQKFATTF FDSDPRTMVE QSCGIADLVT SCLGGRNNRC 310 320 330 340 350 360 AEAFVKTGKS LETLEKELLG GQLLQGAATS KDVHEFLLTK DMVKDFPLFT AVYNISYEDM 370 380 DPKDLIIVLQ PLKEDSENEG GTETE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Glycerol-3-phosphate dehydrogenase homologue from Schizosaccharomyces pombe." Pidoux A.L., Fawell E.H., Armstrong J. Nucleic Acids Res. 18:7145-7145(1990) [PubMed: 2263480] [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]	"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] OF 1-77.
[4]	"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-376 AND THR-382, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X56162 Genomic DNA. Translation: CAA39630.1. CU329671 Genomic DNA. Translation: CAA22119.1. D50796 Genomic DNA. Translation: BAA09424.1.
PIR	T39895.
RefSeq	NP_596682.1.
3D structure databases
HSSP	HSSP built from PDB template 1EVY based on UniProtKB P90551.
ModBase	Search...
Protein-protein interaction databases
STRING	P21696.
Genome annotation databases
GeneID	2540455.
GenomeReviews	Gene locus gpd1 in contig CU329671_GR.
KEGG	spo:SPBC215.05.
NMPDR	fig|4896.1.peg.2548.
Organism-specific databases
GeneDB_Spombe	SPBC215.05.
Phylogenomic databases
OMA	ATIGCKS.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-004669-MON.
BRENDA	1.1.1.8. 653.
Gene expression databases
ArrayExpress	P21696.
Family and domain databases
InterPro	IPR013328. DH_multihelical. IPR016040. NAD(P)-bd_dom. IPR006168. NAD-dep_Gly3P_DH. IPR017751. NAD-dep_Gly3P_DH_euk. IPR011128. NAD-dep_Gly3P_DH_N. IPR006109. NAD_Gly3P_DH_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]
TIGRFAMs	TIGR03376. glycerol3P_DH. 1 hit.
PROSITE	PS00957. NAD_G3PDH. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GPD1_SCHPO

Accession

Primary (citable) accession number: P21696
Secondary accession number(s): O94310, P78927

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	January 11, 2001
Last modified:	November 3, 2009
This is version 84 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)