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UniProtKB/Swiss-Prot entry Q5HGY8

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

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Entry information
Entry name DLDH_STAAC
Primary accession number Q5HGY8
Secondary accession numbers None
Integrated into Swiss-Prot on July 19, 2005
Sequence was last modified on February 15, 2005 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 33)
Name and origin of the protein
Protein name Dihydrolipoyl dehydrogenase
Synonyms EC 1.8.1.4
Dihydrolipoamide dehydrogenase
E3 component of pyruvate complex
Membrane-bound ribosome protein complex 50 kDa subunit
Gene name
Name: pdhD
OrderedLocusNames: SACOL1105
From
Staphylococcus aureus (strain COL) [TaxID: 93062] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Staphylococcus.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1128/JB.187.7.2426-2438.2005; PubMed=15774886 [NCBI, ExPASy, EBI, Israel, Japan]
Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., Fraser C.M.;
"Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain.";
J. Bacteriol. 187:2426-2438(2005).
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
CP000046; AAW37985.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_185969.1; -.
3D structure databases
SMR Q5HGY8; 8-461.
ModBase Q5HGY8.
Enzyme and pathway databases
BioCyc SAUR93062:SACOL1105-MON; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0016020; Cellular component: membrane (inferred from electronic annotation from UniProtKB-KW).
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 Q5HGY8.
Genome annotation databases
GeneID 3237345; -.
GenomeReviews CP000046_GR; SACOL1105.
KEGG sac:SACOL1105; -.
TIGR SACOL1105; -.
Phylogenomic databases
HOGENOM Q5HGY8; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; FAD; Flavoprotein; Glycolysis; Membrane; NAD; Oxidoreductase; Redox-active center.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   468  468     Dihydrolipoyl dehydrogenase. PRO_0000068044
NP_BIND   39    47  9     FAD (By similarity). 
NP_BIND   183   187  5     NAD (By similarity). 
NP_BIND   271   274  4     NAD (By similarity). 
ACT_SITE   446   446        Proton acceptor (By similarity). 
BINDING   56    56        FAD (By similarity). 
BINDING   119   119        FAD; via amide nitrogen and carbonyl oxygen (By similarity). 
BINDING   206   206        NAD (By similarity). 
BINDING   314   314        FAD (By similarity). 
BINDING   322   322        FAD; via amide nitrogen (By similarity). 
DISULFID   47    52        Redox-active (By similarity). 
Sequence information
Length: 468 AA [This is the length of the unprocessed precursor] Molecular weight: 49451 Da [This is the MW of the unprocessed precursor] CRC64: 7B061FE2C39ED2D9 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MVVGDFPIET DTIVIGAGPG GYVAAIRAAQ LGQKVTIVEK GNLGGVCLNV GCIPSKALLH 

        70         80         90        100        110        120 
ASHRFVEAQH SENLGVIAES VSLNFQKVQE FKSSVVNKLT GGVEGLLKGN KVNIVKGEAY 

       130        140        150        160        170        180 
FVDNNSLRVM DEKSAQTYNF KNAIIATGSR PIEIPNFKFG KRVIDSTGAL NLQEVPGKLV 

       190        200        210        220        230        240 
VVGGGYIGSE LGTAFANFGS EVTILEGAKD ILGGFEKQMT QPVKKGMKEK GVEIVTEAMA 

       250        260        270        280        290        300 
KSAEETDNGV KVTYEAKGEE KTIEADYVLV TVGRRPNTDE LGLEELGVKF ADRGLLEVDK 

       310        320        330        340        350        360 
QSRTSISNIY AIGDIVPGLP LAHKASYEAK VAAEAIDGQA AEVDYIGMPA VCFTEPELAT 

       370        380        390        400        410        420 
VGYSEAQAKE EGLAIKASKF PYAANGRALS LDDTNGFVKL ITLKEDDTLI GAQVVGTGAS 

       430        440        450        460 
DIISELGLAI EAGMNAEDIA LTIHAHPTLG EMTMEAAEKA IGYPIHTM
Q5HGY8 in FASTA format

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