ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry O13702


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name GLD1_SCHPO
Primary accession number O13702
Secondary accession numbers None
Integrated into Swiss-Prot on January 15, 2008
Sequence was last modified on January 1, 1998 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 43)
Name and origin of the protein
Protein name Glycerol dehydrogenase
Synonyms GLDH
GDH
EC 1.1.1.6
Gene name
Name: gld1
ORFNames: SPAC13F5.03c
From
Schizosaccharomyces pombe (Fission yeast) [TaxID: 4896] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; Schizosaccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 38366 / 972;
DOI=10.1038/nature724; PubMed=11859360 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
[2]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
DOI=10.1038/nbt1222; PubMed=16823372 [NCBI, ExPASy, EBI, Israel, Japan]
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.;
"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe.";
Nat. Biotechnol. 24:841-847(2006).
[3]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH ZINC AND SUBSTRATE.
Mulichak A.M.;
"Crystal structure of glycerol dehydrogenase from Schizosaccharomyces pombe.";
Submitted (AUG-2005) to the PDB data bank.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
CU329670; CAB11766.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T37628; T37628.
RefSeq NP_593651.1; -.
3D structure databases
PDB
1TA9; X-ray; 1.90 A; A/B=1-450.[ExPASy / RCSB / EBI]
PDBsum 1TA9; -.
ModBase O13702.
Organism-specific databases
GeneDB_Spombe SPAC13F5.03c; -.
Gene expression databases
ArrayExpress O13702; -.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (inferred from electronic annotation from UniProtKB-KW).
GO:0008888; Molecular function: glycerol dehydrogenase activity (inferred from electronic annotation from EC).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0033554; Biological process: cellular response to stress (inferred from expression pattern from GeneDB_SPombe).
GO:0006071; Biological process: glycerol metabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR001670; Fe_AlcDHase.
Graphical view of domain structure.
Pfam PF00465; Fe-ADH; 1.
Pfam graphical view of domain structure.
PROSITE PS00913; ADH_IRON_1; 1.
Genome annotation databases
GeneID 2542881; -.
KEGG spo:SPAC13F5.03c; -.
NMPDR fig|4896.1.peg.3621; -.
Other
ProtoNet O13702.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Glycerol metabolism; Metal-binding; Mitochondrion; NAD; Oxidoreductase; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   450  450     Glycerol dehydrogenase. PRO_0000314770
NP_BIND   155   159  5     NAD (By similarity). 
NP_BIND   177   180  4     NAD (By similarity). 
METAL   232   232        Zinc; catalytic. 
METAL   315   315        Zinc; catalytic. 
METAL   333   333        Zinc; catalytic. 
BINDING   99    99        NAD (By similarity). 
BINDING   182   182        Substrate (By similarity). 
BINDING   186   186        NAD (By similarity). 
BINDING   188   188        NAD; via carbonyl oxygen (By similarity). 
BINDING   192   192        NAD (By similarity). 
BINDING   232   232        Substrate (By similarity). 
BINDING   315   315        Substrate. 
BINDING   333   333        Substrate. 
STRAND   62    67  6      
STRAND   70    75  6      
HELIX   78    81  4      
HELIX   82    86  5      
TURN   87    89  3      
STRAND   91    99  9      
HELIX   100   105  6      
HELIX   107   116  10      
STRAND   120   126  7      
HELIX   132   139  8      
STRAND   148   154  7      
HELIX   155   167  13      
STRAND   172   178  7      
STRAND   187   191  5      
STRAND   200   203  4      
STRAND   209   214  6      
HELIX   215   220  6      
HELIX   223   245  23      
STRAND   253   255  3      
HELIX   258   284  27      
HELIX   289   307  19      
HELIX   313   321  9      
HELIX   322   324  3      
HELIX   326   330  5      
HELIX   333   347  15      
HELIX   352   364  13      
HELIX   371   374  4      
HELIX   381   391  11      
HELIX   397   400  4      
STRAND   401   403  3      
HELIX   407   428  22      
Sequence information
Length: 450 AA [This is the length of the unprocessed precursor] Molecular weight: 49433 Da [This is the MW of the unprocessed precursor] CRC64: E25248204A92E33A [This is a checksum on the sequence]
        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 

O13702 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by kr flag YPRC Korea Mirror sites: Australia  Brazil  Canada  China  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!