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P21696 (GPD1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length385 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 385385Glycerol-3-phosphate dehydrogenase [NAD(+)] 1
PRO_0000138095

Regions

Nucleotide binding29 – 346NAD By similarity
Region296 – 2972Substrate binding By similarity

Sites

Active site2321Proton acceptor By similarity
Binding site1211NAD By similarity
Binding site1441NAD; via amide nitrogen By similarity
Binding site1441Substrate By similarity
Binding site1771NAD; via amide nitrogen By similarity
Binding site2961NAD By similarity
Binding site3251NAD By similarity

Amino acid modifications

Modified residue3761Phosphoserine Ref.4
Modified residue3821Phosphothreonine Ref.4

Experimental info

Sequence conflict54 – 563SKV → GKG in CAA39630. Ref.1
Sequence conflict126 – 1272CD → WH in CAA39630. Ref.1
Sequence conflict1531Missing in CAA39630. Ref.1
Sequence conflict1541R → S in CAA39630. Ref.1
Sequence conflict2091F → S in CAA39630. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P21696 [UniParc].

Last modified January 11, 2001. Version 2.
Checksum: 8061C294196516E1

FASTA38541,995
        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 

« Hide

References

« Hide '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] [Europe PMC] [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. expand/collapse author list , 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]"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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-376 AND THR-382, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X56162 Genomic DNA. Translation: CAA39630.1.
CU329671 Genomic DNA. Translation: CAA22119.1.
D50796 Genomic DNA. Translation: BAA09424.1.
PIRT39895.
RefSeqNP_596682.1. NM_001022605.2.

3D structure databases

ProteinModelPortalP21696.
SMRP21696. Positions 24-371.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid276983. 45 interactions.
MINTMINT-4687624.
STRING4896.SPBC215.05-1.

Proteomic databases

PaxDbP21696.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC215.05.1; SPBC215.05.1:pep; SPBC215.05.
GeneID2540455.
KEGGspo:SPBC215.05.

Organism-specific databases

PomBaseSPBC215.05.

Phylogenomic databases

eggNOGCOG0240.
HOGENOMHOG000246855.
KOK00006.
OMAPKNVVAV.
OrthoDBEOG7V76H7.
PhylomeDBP21696.

Family and domain databases

Gene3D1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
InterProIPR008927. 6-PGluconate_DH_C-like.
IPR013328. DH_multihelical.
IPR006168. G3P_DH_NAD-dep.
IPR006109. G3P_DH_NAD-dep_C.
IPR017751. G3P_DH_NAD-dep_euk.
IPR011128. G3P_DH_NAD-dep_N.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR11728. PTHR11728. 1 hit.
PfamPF07479. NAD_Gly3P_dh_C. 1 hit.
PF01210. NAD_Gly3P_dh_N. 1 hit.
[Graphical view]
PIRSFPIRSF000114. Glycerol-3-P_dh. 1 hit.
PRINTSPR00077. GPDHDRGNASE.
SUPFAMSSF48179. SSF48179. 1 hit.
TIGRFAMsTIGR03376. glycerol3P_DH. 1 hit.
PROSITEPS00957. NAD_G3PDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20801582.

Entry information

Entry nameGPD1_SCHPO
AccessionPrimary (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: April 16, 2014
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names