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UniProtKB/Swiss-Prot entry P43784

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

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Entry information
Entry name DLDH_HAEIN
Primary accession number P43784
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1995
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 72)
Name and origin of the protein
Protein name Dihydrolipoyl dehydrogenase
Synonyms EC 1.8.1.4
Dihydrolipoamide dehydrogenase
E3 component of pyruvate and 2-oxoglutarate dehydrogenases complexes
Gene name
Name: lpdA
OrderedLocusNames: HI1231
From
Haemophilus influenzae [TaxID: 727] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; Pasteurellaceae; Haemophilus.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
PubMed=7542800 [NCBI, ExPASy, EBI, Israel, Japan]
Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd.";
Science 269:496-512(1995).
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
L42023; AAC22884.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR H64111; H64111.
RefSeq NP_439387.1; -.
3D structure databases
HSSP Q51225; 1OJT. [HSSP ENTRY / PDB]
ModBase P43784.
Enzyme and pathway databases
BioCyc HINF71421:HI_1231-MON; -.
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: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: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.
ProtoNet P43784.
Genome annotation databases
GeneID 950173; -.
GenomeReviews L42023_GR; HI1231.
KEGG hin:HI1231; -.
NMPDR fig|71421.1.peg.1177; -.
TIGR HI1231; -.
Phylogenomic databases
HOGENOM P43784; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; FAD; Flavoprotein; Glycolysis; NAD; Oxidoreductase; Redox-active center.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   478  477     Dihydrolipoyl dehydrogenase. PRO_0000068030
NP_BIND   36    45  10     FAD (By similarity). 
NP_BIND   183   187  5     NAD (By similarity). 
NP_BIND   270   273  4     NAD (By similarity). 
ACT_SITE   445   445        Proton acceptor (By similarity). 
BINDING   54    54        FAD (By similarity). 
BINDING   117   117        FAD; via amide nitrogen and carbonyl oxygen (By similarity). 
BINDING   206   206        NAD (By similarity). 
BINDING   239   239        NAD; via amide nitrogen (By similarity). 
BINDING   313   313        FAD (By similarity). 
BINDING   321   321        FAD; via amide nitrogen (By similarity). 
DISULFID   45    50        Redox-active (By similarity). 
Sequence information
Length: 478 AA [This is the length of the unprocessed precursor] Molecular weight: 51154 Da [This is the MW of the unprocessed precursor] CRC64: E2554EE977AF749C [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MSKEIKTQVV VLGAGPAGYS AAFRCADLGL ETVIVERYST LGGVCLNVGC IPSKALLHVA 

        70         80         90        100        110        120 
KVIEEAKHAN KNGIYFSEPR IELDEVRAGK EAVVAKLTGG LAGMAKARKV TVVEGLATFT 

       130        140        150        160        170        180 
DSHTLVARDR DGNPTTVKFD NAIIAAGSRP VQLPFIPHED PRIWDSTDAL KLKEVPKKLL 

       190        200        210        220        230        240 
IMGGGIIGLE MGTVYNALGS EVEVVEMFDQ VIPAADKDVV GIYTKQVEKK FKLMLETKVT 

       250        260        270        280        290        300 
AVEAKDDGIY VSMEGKACND TKRYDAVLVA IGRVPNGKLI DAGKAGVEVD DRGFIHVDKQ 

       310        320        330        340        350        360 
MRTNVPHIYA IGDIVGQPML AHKGVHEGHV AAEVIAGQKH YFDPKVIPSI AYTEPEVAWV 

       370        380        390        400        410        420 
GKTEKECKQE GLNYEVAKFP WAASGRAIAS ECSEGMTKLI FDKDTHRVLG GAIVGSNGGE 

       430        440        450        460        470 
LLGEIGLAIE MGCDAEDIAL TIHAHPTLHE SVGLAAEVFE GSITDLPNAK AKEKIISI
P43784 in FASTA format

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