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UniProtKB/Swiss-Prot entry P35484

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

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Entry information
Entry name DLDH_ACHLA
Primary accession number P35484
Secondary accession numbers None
Integrated into Swiss-Prot on June 1, 1994
Sequence was last modified on June 1, 1994 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 67)
Name and origin of the protein
Protein name Dihydrolipoyl dehydrogenase [Fragment]
Synonyms EC 1.8.1.4
Dihydrolipoamide dehydrogenase
E3 component of pyruvate complex
Gene name
Name: pdhD
From
Acholeplasma laidlawii [TaxID: 2148] 
Taxonomy Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae; Acholeplasma.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1735725 [NCBI, ExPASy, EBI, Israel, Japan]
Wallbrandt P., Tegman V., Jonsson B.-H., Wieslander A.;
"Identification and analysis of the genes coding for the putative pyruvate dehydrogenase enzyme complex in Acholeplasma laidlawii.";
J. Bacteriol. 174:1388-1396(1992).
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
M81753; AAA21910.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR D42653; D42653.
3D structure databases
HSSP P11959; 1EBD. [HSSP ENTRY / PDB]
ModBase P35484.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0004148; Molecular function: dihydrolipoyl dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050660; Molecular function: FAD binding (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.
IPR012999; Pyr_OxRdtase_I_AS.
IPR001327; Pyr_OxRdtase_NAD_bd.
Graphical view of domain structure.
PANTHER PTHR22912:SF20; Lipoamide_DH; 1.
Pfam PF00070; Pyr_redox; 1.
PF07992; Pyr_redox_2; 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]
PROSITE PS00076; PYRIDINE_REDOX_1; 1.
ProtoNet P35484.
Other
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   >336  >336     Dihydrolipoyl dehydrogenase. PRO_0000068012
NP_BIND   34     42  9     FAD (By similarity). 
NP_BIND   180    184  5     NAD (By similarity). 
NP_BIND   264    267  4     NAD (By similarity). 
BINDING   51     51        FAD (By similarity). 
BINDING   115    115        FAD; via amide nitrogen and carbonyl oxygen (By similarity). 
BINDING   203    203        NAD (By similarity). 
BINDING   237    237        NAD; via amide nitrogen (By similarity). 
BINDING   304    304        FAD (By similarity). 
BINDING   312    312        FAD; via amide nitrogen (By similarity). 
DISULFID   42     47        Redox-active (By similarity). 
NON_TER   336    336         
Sequence information
Length: 336 AA [This is the length of the partial sequence of the unprocessed precursor] Molecular weight: 35996 Da [This is the MW of the partial sequence of the unprocessed precursor] CRC64: 4405B1097279B36C [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MSKEYEIIIV GGGPGGYVAA IKAAQYGAKV ALVEKEVVGG ICLNHGCIPT KTFLKSAKVF 

        70         80         90        100        110        120 
NTVKKSMDFG VSTSGEVGFD WSKIVSRKDG VVKQLTNGVA FLLKKNGVDV YNGFGDIKSA 

       130        140        150        160        170        180 
NEVVVNGESL KTKNVIIATG SSAVVPPIPG VKEAYEKGIV VTSRELLNVK NYPKSIVIVG 

       190        200        210        220        230        240 
GGVIGVEFAT VFNSFGSKVT IIEMMDGILP TMDDDIRVAY AKTLKRDGIE ILTKAEVKKV 

       250        260        270        280        290        300 
DDHKVTYSLD GKETTIEGDL ILMSVGTRAN SKGLEHLGLE MDRANIKTNE YLQTNVPGVY 

       310        320        330 
AIGDVNGKFM LAHVAEHEGI TAVQHILKIG HAKMNY
P35484 in FASTA format

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