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UniProtKB/Swiss-Prot entry Q8K9T7

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

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Entry information
Entry name DLDH_BUCAP
Primary accession number Q8K9T7
Secondary accession numbers None
Integrated into Swiss-Prot on November 15, 2002
Sequence was last modified on October 1, 2002 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 54)
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: BUsg_201
From
Buchnera aphidicola subsp. Schizaphis graminum [TaxID: 98794] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Buchnera.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1126/science.1071278; PubMed=12089438 [NCBI, ExPASy, EBI, Israel, Japan]
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
"50 million years of genomic stasis in endosymbiotic bacteria.";
Science 296:2376-2379(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
AE013218; AAM67765.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_660554.1; -.
3D structure databases
HSSP Q51225; 1OJT. [HSSP ENTRY / PDB]
ModBase Q8K9T7.
Enzyme and pathway databases
BioCyc BAPH198804:BUSG201-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 IPR000759; Adrndx_reductase.
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 PR00419; ADXRDTASE.
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 Q8K9T7.
Genome annotation databases
GeneID 1005398; -.
GenomeReviews AE013218_GR; BUsg_201.
KEGG bas:BUsg201; -.
Phylogenomic databases
HOGENOM Q8K9T7; -.
Genome annotation databases
CMR Q8K9T7; BUsg_201.
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   476  476     Dihydrolipoyl dehydrogenase. PRO_0000068020
NP_BIND   36    45  10     FAD (By similarity). 
NP_BIND   182   186  5     NAD (By similarity). 
NP_BIND   271   274  4     NAD (By similarity). 
ACT_SITE   446   446        Proton acceptor (By similarity). 
BINDING   54    54        FAD (By similarity). 
BINDING   117   117        FAD; via amide nitrogen and carbonyl oxygen (By similarity). 
BINDING   205   205        NAD (By similarity). 
BINDING   238   238        NAD; via amide nitrogen (By similarity). 
BINDING   314   314        FAD (By similarity). 
BINDING   322   322        FAD; via amide nitrogen (By similarity). 
DISULFID   45    50        Redox-active (By similarity). 
Sequence information
Length: 476 AA [This is the length of the unprocessed precursor] Molecular weight: 52187 Da [This is the MW of the unprocessed precursor] CRC64: 2BCD5F1ECB08BA58 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MHQEIQSEVV IIGSGPAGYS AAFRCADLGL ETVLIEHQER LGGVCLNVGC IPSKSLLHIA 

        70         80         90        100        110        120 
KIIKDASELS ESGVFFNKPI IDIKKINNWK EKIIKKLTTG LSNMGEKRKV RIVQGKALFN 

       130        140        150        160        170        180 
TDHSVLVKNK KNDFTIFFKH AIIATGSKPI KIPSLPNEDN RIWNSTDALS LKSIPNRFLI 

       190        200        210        220        230        240 
IGGGIIGLEM ATIYSALGSK VDIVDRFNAF LPSVDKDITD IYIKSIKKRF KLLLNTHVKS 

       250        260        270        280        290        300 
VEKSKDNDLI VKIAEENSDE NVCCYDNILV AIGRSPNVDF LGLEKIGLKL NESGFIEINQ 

       310        320        330        340        350        360 
QLKTNISHIY AIGDVTGFPM LAHKAVQQAH IAAEVISGKK HYFEPKVIPS VAYTDPEIAW 

       370        380        390        400        410        420 
VGLSEKEAEN NDIDYEVSLF PWSASGRAHA SNCTLGMTKL IFNKNTNKII GGSIIGTNAS 

       430        440        450        460        470 
ELISEIGLAI EMGSDAEDIS LTIHPHPTLS ESISLASEVF QGTITDLLNL KKSLLN
Q8K9T7 in FASTA format

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