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Reviewed, UniProtKB/Swiss-Prot O13702 (GLD1_SCHPO)

Last modified January 19, 2010. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Glycerol dehydrogenase
      Short name=GLDH
      Short name=GDH
    EC=1.1.1.6
Gene names
Name: gld1
ORF Names: SPAC13F5.03c
OrganismSchizosaccharomyces pombe (Fission yeast) [Complete proteome]
Taxonomic identifier4896 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

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Protein attributes

Sequence length450 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

Glycerol + NAD+ = glycerone + NADH.

Cofactor

Binds 1 zinc ion per subunit.

Pathway

Polyol metabolism; glycerol fermentation; glycerone phosphate from glycerol (oxidative route): step 1/2.

Subcellular location

Mitochondrion Ref.2.

Sequence similarities

Belongs to the iron-containing alcohol dehydrogenase family.

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Ontologies

Keywords
   Biological processGlycerol metabolism
   Cellular componentMitochondrion
   LigandMetal-binding
NAD
Zinc
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processcellular response to stress

Inferred from expression pattern. Source: GeneDB_SPombe

glycerol metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrion Ref.2

Inferred from direct assay. Source: GeneDB_SPombe

   Molecular functionglycerol dehydrogenase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 450450Glycerol dehydrogenase
PRO_0000314770

Regions

Nucleotide binding155 – 1595NAD By similarity
Nucleotide binding177 – 1804NAD By similarity

Sites

Metal binding2321Zinc; catalytic
Metal binding3151Zinc; catalytic
Metal binding3331Zinc; catalytic
Binding site991NAD By similarity
Binding site1821Substrate By similarity
Binding site1861NAD By similarity
Binding site1881NAD; via carbonyl oxygen By similarity
Binding site1921NAD By similarity
Binding site2321Substrate By similarity
Binding site3151Substrate
Binding site3331Substrate

Secondary structure

1 ........................................................ 450
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
O13702-1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: E25248204A92E33A

FASTA45049,433
        10         20         30         40         50         60 
MIGPRLCAAT PRFPLVSLAH RNSKVFALAS SNAVAQRWGK RFYAPIETET PHKVGVEFEE 

        70         80         90        100        110        120 
SKDRIFTSPQ KYVQGRHAFT RSYMYVKKWA TKSAVVLADQ NVWNICANKI VDSLSQNGMT 

       130        140        150        160        170        180 
VTKLVFGGEA SLVELDKLRK QCPDDTQVII GVGGGKTMDS AKYIAHSMNL PSIICPTTAS 

       190        200        210        220        230        240 
SDAATSSLSV IYTPDGQFQK YSFYPLNPNL IFIDTDVIVR APVRFLISGI GDALSTWVET 

       250        260        270        280        290        300 
ESVIRSNSTS FAGGVASIAG RYIARACKDT LEKYALSAIL SNTRGVCTEA FENVVEANTL 

       310        320        330        340        350        360 
MSGLGFENGG LAAAHAIHNG MTAIHGPVHR LMHGEKVAYG TLVQVVLEDW PLEDFNNLAS 

       370        380        390        400        410        420 
FMAKCHLPIT LEELGIPNVT DEELLMVGRA TLRPDESIHN MSKKFNPSQI ADAIKAVDSY 

       430        440        450 
SQKWQEQTGW TERFRLPPSR HSPHLTDIHP

« Hide

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References

« Hide 'large scale' 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. 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: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 38366 / 972.
[2]"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
Nat. Biotechnol. 24:841-847(2006) [PubMed: 16823372] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[3]"Crystal structure of glycerol dehydrogenase from Schizosaccharomyces pombe."
Mulichak A.M.
Submitted (AUG-2005) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH ZINC AND SUBSTRATE.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU329670 Genomic DNA. Translation: CAB11766.1.
PIRT37628.
RefSeqNP_593651.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1TA9X-ray1.90A/B1-450[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGO13702.

Genome annotation databases

GeneID2542881.
GenomeReviewsGene locus gld1 in contig CU329670_GR.
KEGGspo:SPAC13F5.03c.
NMPDRfig|4896.1.peg.3621.

Organism-specific databases

GeneDB_SpombeSPAC13F5.03c.

Phylogenomic databases

eggNOGeuNOG17072.
HOGENOMHBG399530.
OMACERTLFA.
PhylomeDBO13702.

Enzyme and pathway databases

BRENDA1.1.1.6. 653.

Gene expression databases

ArrayExpressO13702.

Family and domain databases

InterProIPR001670. ADH_Fe.
IPR018211. ADH_Fe_CS.
[Graphical view]
PfamPF00465. Fe-ADH. 1 hit.
[Graphical view]
PROSITEPS00913. ADH_IRON_1. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameGLD1_SCHPO
AccessionPrimary (citable) accession number: O13702
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 1, 1998
Last modified: January 19, 2010
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents