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UniProtKB/Swiss-Prot entry O18480

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

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Entry information
Entry name DLDH_MANSE
Primary accession number O18480
Secondary accession numbers None
Integrated into Swiss-Prot on July 15, 1999
Sequence was last modified on January 1, 1998 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 63)
Name and origin of the protein
Protein name Dihydrolipoyl dehydrogenase
Synonyms EC 1.8.1.4
Dihydrolipoamide dehydrogenase
E3
Gene name None
From
Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm) [TaxID: 7130] 
Taxonomy Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea; Sphingidae; Sphinginae; Sphingini; Manduca.
Protein existence 2: Evidence at transcript level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1016/S0378-1119(97)00413-7; PubMed=9373151 [NCBI, ExPASy, EBI, Israel, Japan]
Pullikuth A.K., Gill S.S.;
"Primary structure of an invertebrate dihydrolipoamide dehydrogenase with phylogenetic relationship to vertebrate and bacterial disulfide oxidoreductases.";
Gene 200:163-172(1997).
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
AF008586; AAB88282.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
HSSP P31023; 1DXL. [HSSP ENTRY / PDB]
ModBase O18480.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0004148; Molecular function: dihydrolipoyl dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0050660; Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0045454; Biological process: cell redox homeostasis (inferred from electronic annotation from InterPro).
GO:0006096; Biological process: glycolysis (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 IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR000815; Hg_reductase.
IPR006258; Lipoamide_DHase.
IPR001100; Pyr_nuc-diS_OxRdtase.
IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
IPR012999; Pyr_OxRdtase_I_AS.
IPR001327; Pyr_OxRdtase_NAD_bd.
Graphical view of domain structure.
Gene3D G3DSA:3.30.390.30; Pyr_redox_dim; 1.
PANTHER PTHR22912:SF20; Lipoamide_DH; 1.
Pfam PF00070; Pyr_redox; 1.
PF07992; Pyr_redox_2; 1.
PF02852; Pyr_redox_dim; 1.
Pfam graphical view of domain structure.
PRINTS PR00368; FADPNR.
PR00945; HGRDTASE.
PR00411; PNDRDTASEI.
ProDom PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01350; lipoamide_DH; 1.
PROSITE PS00076; PYRIDINE_REDOX_1; 1.
Other
ProtoNet O18480.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cytoplasm; FAD; Flavoprotein; Glycolysis; NAD; Oxidoreductase; Redox-active center.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   497  497     Dihydrolipoyl dehydrogenase. PRO_0000068007
NP_BIND   60    69  10     FAD (By similarity). 
NP_BIND   170   172  3     FAD (By similarity). 
NP_BIND   207   214  8     NAD (By similarity). 
NP_BIND   349   352  4     FAD (By similarity). 
ACT_SITE   475   475        Proton acceptor (By similarity). 
BINDING   78    78        FAD (By similarity). 
BINDING   142   142        FAD; via amide nitrogen and carbonyl oxygen (By similarity). 
BINDING   230   230        NAD (By similarity). 
BINDING   264   264        NAD; via amide nitrogen and carbonyl oxygen (By similarity). 
BINDING   302   302        NAD; via amide nitrogen (By similarity). 
BINDING   343   343        FAD (By similarity). 
DISULFID   69    74        Redox-active (By similarity). 
Sequence information
Length: 497 AA [This is the length of the unprocessed precursor] Molecular weight: 53083 Da [This is the MW of the unprocessed precursor] CRC64: 1689E564E165137A [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MGYKFLKLAS ASFRNGGVRI VSRQYSTTHD ADLVVIGAGP GGYVAAIKAA QLGMKVVSVE 

        70         80         90        100        110        120 
KEPSLGGTCL NVGCIPSKAL LHNTHLYHMA KHDFKHRGIE TGEVKFNFKA MMDYKVNAVK 

       130        140        150        160        170        180 
ALTGGIAMLF QKNKVKLVRG AGTIVAPNKV EVKGEKGVET VNTKNILIAT GSEVTPFPGV 

       190        200        210        220        230        240 
TFDEKQIITS TGALSLESVP KKMLVIGAGV IGLELGSVYQ RLGADVTAIE FLGSIGGIGI 

       250        260        270        280        290        300 
DMEVSKDYRI LAKQGMKFKL ETKVLGVKKE GSTVKVEDVS IEGAKGGNKE TMDCDVVLIS 

       310        320        330        340        350        360 
IGRRPYTKDL GLDKVGIALD DRGRVPVNNK FQTTVPGIYA IGDVIHGPML AHKAEDEGIV 

       370        380        390        400        410        420 
CVEGIKGMPV HFNYDAIPSV IYTSPEVGWV RKTEEDLKKE GKAYKVRKFP FLANSRAKTN 

       430        440        450        460        470        480 
GEPDGFVKVL SDKATDVILG THIIGPGGGE LINEAVLAQE YGAAAEDVAR VCHAHPTCAE 

       490 
ALREANLAAY CGKPINF
O18480 in FASTA format

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