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UniProtKB/Swiss-Prot entry Q02912


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

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Entry information
Entry name DHSO_BOMMO
Primary accession number Q02912
Secondary accession numbers None
Integrated into Swiss-Prot on July 1, 1993
Sequence was last modified on July 1, 1993 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 57)
Name and origin of the protein
Protein name Sorbitol dehydrogenase
Synonyms EC 1.1.1.14
L-iditol 2-dehydrogenase
Gene name
Name: SDH
From
Bombyx mori (Silk moth) [TaxID: 7091] 
Taxonomy Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea; Bombycidae; Bombycinae; Bombyx.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8504807 [NCBI, ExPASy, EBI, Israel, Japan]
Niimi T., Yamashita O., Yaginuma T.;
"A cold-inducible Bombyx gene encoding a protein similar to mammalian sorbitol dehydrogenase. Yolk nuclei-dependent gene expression in diapause eggs.";
Eur. J. Biochem. 213:1125-1131(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Tokai X Asahi;
TISSUE=Fat body;
PubMed=8933178 [NCBI, ExPASy, EBI, Israel, Japan]
Niimi T., Yamashita O., Yaginuma T.;
"Structure of the Bombyx sorbitol dehydrogenase gene: a possible alternative use of the promoter.";
Insect Mol. Biol. 5:269-280(1996).
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
D13371; BAA02634.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D66906; BAA11030.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S32484; S32484.
RefSeq NP_001037311.1; -.
UniGene Bmo.3
3D structure databases
HSSP O96496; 1E3J. [HSSP ENTRY / PDB]
ModBase Q02912.
Ontologies
GO
GO:0003939; Molecular function: L-iditol 2-dehydrogenase activity (inferred from electronic annotation from EC).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006950; Biological process: response to stress (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR013154; AlcDHase_GroES-like.
IPR002085; AlcDHase_SF_Zn.
IPR013149; AlcDHase_Zn-bd.
IPR002328; AlcDHase_Zn_CS.
IPR001100; Pyr_nuc-diS_OxRdtase.
Graphical view of domain structure.
PANTHER PTHR11695; ADH_Sf_Zn; 1.
Pfam PF08240; ADH_N; 1.
PF00107; ADH_zinc_N; 1.
Pfam graphical view of domain structure.
PRINTS PR00411; PNDRDTASEI.
ProDom PD040557; GroES_related; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00059; ADH_ZINC; 1.
BLOCKS Q02912.
ProtoNet Q02912.
Genome annotation databases
GeneID 692742; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Metal-binding; NAD; Oxidoreductase; Stress response; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom  To Length Description FTId
CHAIN   1   348  348     Sorbitol dehydrogenase. PRO_0000160820
METAL   40    40        Zinc; catalytic (By similarity). 
METAL   65    65        Zinc; catalytic (By similarity). 
METAL   66    66        Zinc; catalytic (By similarity). 
Sequence information
Length: 348 AA [This is the length of the unprocessed precursor] Molecular weight: 37158 Da [This is the MW of the unprocessed precursor] CRC64: 2985304E9ADE6FF0 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTENYAAVLH GANDVRIEKI PVPEINDDEV LIKIDCVGIC GSDVKLYSTG TCGADVIDKP 

        70         80         90        100        110        120 
IVIGHEGAGT VVKVGDKVSS LRVGDRVAIE PTQPCRSCEL CKRGKYNLCV EPRYCSSMGA 

       130        140        150        160        170        180 
PGNLCRYYKH VADFCHKLPD NLTMEEGAAV QPLAIVIHAC NRAKITLGSK IVILGAGPIG 

       190        200        210        220        230        240 
ILCAMSAKAM GASKIILTDV VQSRLDAALE LGADNVLLVR REYTDEEVVE KIVKLLGDRP 

       250        260        270        280        290        300 
DVSIDACGYG SAQRVALLVT KTAGLVLVVG IADKTVELPL SQALLREVDV VGSFRIMNTY 

       310        320        330        340 
QPALAAVSSG AIPLDKFITH RFPLNKTKEA LDLAKSGAAM KILIHVQN 

Q02912 in FASTA format

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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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