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UniProtKB/Swiss-Prot entry P0A0E6

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

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Entry information
Entry name DLDH_STAAM
Primary accession number P0A0E6
Secondary accession number Q59822
Integrated into Swiss-Prot on March 1, 2005
Sequence was last modified on March 1, 2005 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 31)
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: SAV1096
From
Staphylococcus aureus (strain Mu50 / ATCC 700699) [TaxID: 158878] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Staphylococcus.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1016/S0140-6736(00)04403-2; PubMed=11418146 [NCBI, ExPASy, EBI, Israel, Japan]
Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y., Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H., Hiramatsu K.;
"Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
Lancet 357:1225-1240(2001).
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
BA000017; BAB57258.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_371620.1; -.
3D structure databases
HSSP P11959; 1EBD. [HSSP ENTRY / PDB]
SMR P0A0E6; 8-461.
ModBase P0A0E6.
Enzyme and pathway databases
BioCyc SAUR158878:SAV1096-MON; -.
2D gel databases
World-2DPAGE 0002:P0A0E6; -.
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: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 1121073; -.
GenomeReviews BA000017_GR; SAV1096.
KEGG sav:SAV1096; -.
Phylogenomic databases
HOGENOM P0A0E6; -.
Genome annotation databases
CMR P0A0E6; SAV1096.
Other
ProtoNet P0A0E6.
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_0000068045
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
P0A0E6 in FASTA format

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