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UniProtKB/Swiss-Prot entry P21880


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

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Entry information
Entry name DLDH1_BACSU
Primary accession number P21880
Secondary accession numbers None
Integrated into Swiss-Prot on May 1, 1991
Sequence was last modified on May 1, 1991 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 82)
Name and origin of the protein
Protein name Dihydrolipoyl dehydrogenase
Synonyms EC 1.8.1.4
Dihydrolipoamide dehydrogenase
E3 component of pyruvate complex
S complex, 50 kDa subunit
Gene name
Name: pdhD
Synonyms: aceD, citL
OrderedLocusNames: BSU14610
From
Bacillus subtilis [TaxID: 1423] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
PubMed=1697575 [NCBI, ExPASy, EBI, Israel, Japan]
Hemilae H.O., Palva A., Paulin L., Arvidson S., Palva I.;
"Secretory S complex of Bacillus subtilis: sequence analysis and identity to pyruvate dehydrogenase.";
J. Bacteriol. 172:5052-5063(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
PubMed=8969500 [NCBI, ExPASy, EBI, Israel, Japan]
Winters P., Caldwell R.M., Enfield L., Ferrari E.;
"The ampS-nprE (124 degrees-127 degrees) region of the Bacillus subtilis 168 chromosome: sequencing of a 27 kb segment and identification of several genes in the area.";
Microbiology 142:3033-3037(1996).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
Caldwell R.M., Ferrari E.;
"Sequence analysis of the mobA-ampS region of the Bacillus subtilis chromosome.";
Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
DOI=10.1038/36786; PubMed=9384377 [NCBI, ExPASy, EBI, Israel, Japan]
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis.";
Nature 390:249-256(1997).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 461-470.
DOI=10.1016/0378-1097(91)90417-9; PubMed=1936936 [NCBI, ExPASy, EBI, Israel, Japan]
Hemilae H.O.;
"Sequence of a PAL-related lipoprotein from Bacillus subtilis.";
FEMS Microbiol. Lett. 66:37-41(1991).
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
M57435; AAA62684.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF012285; AAC24935.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99111; CAB13334.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR E36718; E36718.
RefSeq NP_389344.1; -.
3D structure databases
HSSP P11959; 1EBD. [HSSP ENTRY / PDB]
SMR P21880; 8-462.
ModBase P21880.
Enzyme and pathway databases
BioCyc BSUB224308:BSU1463-MON; -.
MetaCyc:MON-11687; -.
Organism-specific databases
SubtiList BG10210; pdhD. [Micado]
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 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 P21880.
Genome annotation databases
GeneID 939492; -.
GenomeReviews AL009126_GR; BSU14610.
KEGG bsu:BSU14610; -.
NMPDR fig|224308.1.peg.1463; -.
Phylogenomic databases
HOGENOM P21880; -.
Genome annotation databases
CMR P21880; BSU14610.
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   470  470     Dihydrolipoyl dehydrogenase. PRO_0000068016
NP_BIND   39    47  9     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   56    56        FAD (By similarity). 
BINDING   119   119        FAD; via amide nitrogen and carbonyl oxygen (By similarity). 
BINDING   206   206        NAD (By similarity). 
BINDING   315   315        FAD (By similarity). 
BINDING   323   323        FAD; via amide nitrogen (By similarity). 
DISULFID   47    52        Redox-active (By similarity). 
Sequence information
Length: 470 AA [This is the length of the unprocessed precursor] Molecular weight: 49733 Da [This is the MW of the unprocessed precursor] CRC64: 874CA310F3B48A5F [This is a checksum on the sequence]
        10         20         30         40         50         60 
MVVGDFPIET DTLVIGAGPG GYVAAIRAAQ LGQKVTVVEK ATLGGVCLNV GCIPSKALIN 

        70         80         90        100        110        120 
AGHRYENAKH SDDMGITAEN VTVDFTKVQE WKASVVNKLT GGVAGLLKGN KVDVVKGEAY 

       130        140        150        160        170        180 
FVDSNSVRVM DENSAQTYTF KNAIIATGSR PIELPNFKYS ERVLNSTGAL ALKEIPKKLV 

       190        200        210        220        230        240 
VIGGGYIGTE LGTAYANFGT ELVILEGGDE ILPGFEKQMS SLVTRRLKKK GNVEIHTNAM 

       250        260        270        280        290        300 
AKGVEERPDG VTVTFEVKGE EKTVDADYVL ITVGRRPNTD ELGLEQVGIE MTDRGIVKTD 

       310        320        330        340        350        360 
KQCRTNVPNI YAIGDIIEGP PLAHKASYEG KIAAEAIAGE PAEIDYLGIP AVVFSEPELA 

       370        380        390        400        410        420 
SVGYTEAQAK EEGLDIVAAK FPFAANGRAL SLNETDGFMK LITRKEDGLV IGAQIAGASA 

       430        440        450        460        470 
SDMISELSLA IEGGMTAEDI AMTIHAHPTL GEITMEAAEV AIGSPIHIVK 

P21880 in FASTA format

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View entry in raw text format (no links)
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