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UniProtKB/Swiss-Prot entry Q89AQ8

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

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Entry information
Entry name DLDH_BUCBP
Primary accession number Q89AQ8
Secondary accession numbers None
Integrated into Swiss-Prot on November 14, 2003
Sequence was last modified on June 1, 2003 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 48)
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: bbp_191
From
Buchnera aphidicola subsp. Baizongia pistaciae [TaxID: 135842] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Buchnera.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1073/pnas.0235981100; PubMed=12522265 [NCBI, ExPASy, EBI, Israel, Japan]
van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
"Reductive genome evolution in Buchnera aphidicola.";
Proc. Natl. Acad. Sci. U.S.A. 100:581-586(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
AE016826; AAO26923.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_777818.1; -.
3D structure databases
HSSP Q51225; 1OJT. [HSSP ENTRY / PDB]
ModBase Q89AQ8.
Enzyme and pathway databases
BioCyc BAPH224915:BBP_191-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.
BLOCKS Q89AQ8.
ProtoNet Q89AQ8.
Genome annotation databases
GeneID 1058236; -.
GenomeReviews AE016826_GR; bbp_191.
KEGG bab:bbp191; -.
Phylogenomic databases
HOGENOM Q89AQ8; -.
Genome annotation databases
CMR Q89AQ8; bbp_191.
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   475  475     Dihydrolipoyl dehydrogenase. PRO_0000068021
NP_BIND   37    46  10     FAD (By similarity). 
NP_BIND   183   187  5     NAD (By similarity). 
NP_BIND   272   275  4     NAD (By similarity). 
ACT_SITE   447   447        Proton acceptor (By similarity). 
BINDING   55    55        FAD (By similarity). 
BINDING   118   118        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   315   315        FAD (By similarity). 
BINDING   323   323        FAD; via amide nitrogen (By similarity). 
DISULFID   46    51        Redox-active (By similarity). 
Sequence information
Length: 475 AA [This is the length of the unprocessed precursor] Molecular weight: 52409 Da [This is the MW of the unprocessed precursor] CRC64: A29761D2D44C9BC7 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MISKKVDTQV VIIGSGPSGY SAAFRCSDLG LNVVLIEQYY SLGGVCLNVG CIPSKYLLHI 

        70         80         90        100        110        120 
AKVIKDVKKL SRIGISFEKL DINLKEIQCN QKKIIESFSS GISNLARKRN VRIIFGYAKF 

       130        140        150        160        170        180 
LDANSIFVQG EHDSYVVSFN KIVIATGSLS KKLSYIPYDD IRIWNSSFAV SIPSIPKKLL 

       190        200        210        220        230        240 
IIGGGIIGLE MATIYSALGS NVDIIDNSHD ILPHLDRDVI DIFKRSVNHD YNIFFNSNVI 

       250        260        270        280        290        300 
KIVQEKNGLL VHIAENDNKN KRFELYDIIL VAIGRVPNTD MLDISKVGLK TDNNGFIKVN 

       310        320        330        340        350        360 
EQFCTNIPNI YAIGDVIGQP MLAHKGTHEG HIVAEVISGK KHYFNPFVIP CVSYTEPEIA 

       370        380        390        400        410        420 
WVGITENEAR KNNINYEVSS VLWNTLGRAV SSQCSEGVTK LIFDKKTNKI IGGCIVGSNA 

       430        440        450        460        470 
GELLGEISLA IEMGCDAEDL ALTIHAHPTL YESINLSAQI FQGTITDLIN KKIKK
Q89AQ8 in FASTA format

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