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UniProtKB/Swiss-Prot entry P66005

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

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Entry information
Entry name DLDH_MYCBO
Primary accession number P66005
Secondary accession number O53747
Integrated into Swiss-Prot on October 11, 2004
Sequence was last modified on October 11, 2004 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 32)
Name and origin of the protein
Protein name Dihydrolipoyl dehydrogenase
Synonyms EC 1.8.1.4
Dihydrolipoamide dehydrogenase
E3 component of alpha keto acid dehydrogenase complexes
Gene name
Name: lpd
OrderedLocusNames: Mb0471
From
Mycobacterium bovis [TaxID: 1765] [HAMAP proteome]
Taxonomy Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; Corynebacterineae; Mycobacteriaceae; Mycobacterium; Mycobacterium tuberculosis complex.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-935 / AF2122/97;
DOI=10.1073/pnas.1130426100; PubMed=12788972 [NCBI, ExPASy, EBI, Israel, Japan]
Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M., Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B., Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J., Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
"The complete genome sequence of Mycobacterium bovis.";
Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
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
BX248335; CAD93334.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_854134.1; -.
3D structure databases
HSSP P11959; 1EBD. [HSSP ENTRY / PDB]
SMR P66005; 1-464.
ModBase P66005.
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 P66005.
Genome annotation databases
GeneID 1091506; -.
GenomeReviews BX248333_GR; Mb0471.
KEGG mbo:Mb0471; -.
Phylogenomic databases
HOGENOM P66005; -.
Genome annotation databases
CMR P66005; Mb0471.
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
CHAIN   1   464  464     Dihydrolipoyl dehydrogenase. PRO_0000068035
NP_BIND   33    41  9     FAD (By similarity). 
NP_BIND   178   182  5     NAD (By similarity). 
NP_BIND   266   269  4     NAD (By similarity). 
ACT_SITE   443   443        Proton acceptor (By similarity). 
BINDING   50    50        FAD (By similarity). 
BINDING   113   113        FAD; via amide nitrogen and carbonyl oxygen (By similarity). 
BINDING   201   201        NAD (By similarity). 
BINDING   309   309        FAD (By similarity). 
BINDING   317   317        FAD; via amide nitrogen (By similarity). 
DISULFID   41    46        Redox-active (By similarity). 
Sequence information
Length: 464 AA [This is the length of the unprocessed precursor] Molecular weight: 49239 Da [This is the MW of the unprocessed precursor] CRC64: DD93D95DC6F76B22 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MTHYDVVVLG AGPGGYVAAI RAAQLGLSTA IVEPKYWGGV CLNVGCIPSK ALLRNAELVH 

        70         80         90        100        110        120 
IFTKDAKAFG ISGEVTFDYG IAYDRSRKVA EGRVAGVHFL MKKNKITEIH GYGTFADANT 

       130        140        150        160        170        180 
LLVDLNDGGT ESVTFDNAII ATGSSTRLVP GTSLSANVVT YEEQILSREL PKSIIIAGAG 

       190        200        210        220        230        240 
AIGMEFGYVL KNYGVDVTIV EFLPRALPNE DADVSKEIEK QFKKLGVTIL TATKVESIAD 

       250        260        270        280        290        300 
GGSQVTVTVT KDGVAQELKA EKVLQAIGFA PNVEGYGLDK AGVALTDRKA IGVDDYMRTN 

       310        320        330        340        350        360 
VGHIYAIGDV NGLLQLAHVA EAQGVVAAET IAGAETLTLG DHRMLPRATF CQPNVASFGL 

       370        380        390        400        410        420 
TEQQARNEGY DVVVAKFPFT ANAKAHGVGD PSGFVKLVAD AKHGELLGGH LVGHDVAELL 

       430        440        450        460 
PELTLAQRWD LTASELARNV HTHPTMSEAL QECFHGLVGH MINF
P66005 in FASTA format

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