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UniProtKB/Swiss-Prot entry Q8KCW2

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

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Entry information
Entry name DLDH_CHLTE
Primary accession number Q8KCW2
Secondary accession numbers None
Integrated into Swiss-Prot on November 25, 2002
Sequence was last modified on October 1, 2002 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 49)
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: lpd
Synonyms: lpd-1
OrderedLocusNames: CT1298
From
Chlorobium tepidum [TaxID: 1097] [HAMAP proteome]
Taxonomy Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 49652 / DSM 12025 / TLS;
DOI=10.1073/pnas.132181499; PubMed=12093901 [NCBI, ExPASy, EBI, Israel, Japan]
Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J., DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D., Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M., Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V., Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M., White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A., Fraser C.M.;
"The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic, anaerobic, green-sulfur bacterium.";
Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
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
AE006470; AAM72528.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_662186.1; -.
3D structure databases
HSSP P11959; 1EBD. [HSSP ENTRY / PDB]
ModBase Q8KCW2.
Enzyme and pathway databases
BioCyc CTEP194439:CT_1298-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: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.
Genome annotation databases
GeneID 1006658; -.
GenomeReviews AE006470_GR; CT1298.
KEGG cte:CT1298; -.
TIGR CT1298; -.
Phylogenomic databases
HOGENOM Q8KCW2; -.
Other
ProtoNet Q8KCW2.
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   469  469     Dihydrolipoyl dehydrogenase. PRO_0000068022
NP_BIND   40    48  9     FAD (By similarity). 
NP_BIND   186   190  5     NAD (By similarity). 
NP_BIND   275   278  4     NAD (By similarity). 
ACT_SITE   450   450        Proton acceptor (By similarity). 
BINDING   57    57        FAD (By similarity). 
BINDING   120   120        FAD; via amide nitrogen and carbonyl oxygen (By similarity). 
BINDING   209   209        NAD (By similarity). 
BINDING   317   317        FAD (By similarity). 
BINDING   325   325        FAD; via amide nitrogen (By similarity). 
DISULFID   48    53        Redox-active (By similarity). 
Sequence information
Length: 469 AA [This is the length of the unprocessed precursor] Molecular weight: 48007 Da [This is the MW of the unprocessed precursor] CRC64: CEEB79308FD4DC4E [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MQQADTLAAQ FDVAVIGSGP GGYEAAIHAA RYGLKTCIVE KAVLGGVCVN WGCIPTKALL 

        70         80         90        100        110        120 
RSAEVFDLAK NPETFGVNVG NVSFDLAQAV KRSRNVALKS SKGVAYLLKK AAVEVLAGEA 

       130        140        150        160        170        180 
VLTGGAGVMV TMPDGSVRML GAKNIIVATG STPRVIPGLE PDGKKIITSR EALILKEVPK 

       190        200        210        220        230        240 
SMIVVGGGAI GVEMAWFYAK AGSKVTIVEL MPRMLPAEEA EVSEALKRSF EKAGITVHCG 

       250        260        270        280        290        300 
AKLDNVAVSE SGVSAELVVE GSAPQTLNAS CLLVAVGVTG AIDGLGLDAV GVETERGFIR 

       310        320        330        340        350        360 
TDGQCRTSAP GIYAIGDVRG GMLLAHKASA EAAIAVEAIA GKSPEPLSEP LIPRCVYAQP 

       370        380        390        400        410        420 
SVASVGLTEE AAVNAGYQVA VGRSQFAASG KANAYGQLEG FVKLVFDAAT GKMLGGHLIG 

       430        440        450        460 
HDAVELIGEL GLACRYGVTA GGLVNTVHAH PTLSETVREA AFDALQSMG
Q8KCW2 in FASTA format

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