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Reviewed, UniProtKB/Swiss-Prot P21880 (DLDH1_BACSU)

Last modified June 16, 2009. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Dihydrolipoyl dehydrogenase
    EC=1.8.1.4
Alternative name(s):
    Dihydrolipoamide dehydrogenase
    E3 component of pyruvate complex
    S complex, 50 kDa subunit
Gene names
Name: pdhD
Synonyms: aceD, citL
Ordered Locus Names: BSU14610
OrganismBacillus subtilis [Complete proteome] [HAMAP]
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

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Protein attributes

Sequence length470 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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General annotation (Comments)

Function

Catalyzes the oxidation of dihydrolipoamide to lipoamide.

Catalytic activity

Protein N(6)-(dihydrolipoyl)lysine + NAD+ = protein N(6)-(lipoyl)lysine + NADH.

Cofactor

Binds 1 FAD per subunit By similarity.

Subunit structure

Homodimer. Component of two multienzyme complexes: pyruvate dehydrogenase complex and oxoglutarate dehydrogenase complex.

Subcellular location

Cytoplasm.

Miscellaneous

The active site is a redox-active disulfide bond.

Sequence similarities

Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

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Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   DomainRedox-active center
   LigandFAD
Flavoprotein
NAD
   Molecular functionOxidoreductase
   PTMDisulfide bond
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcell redox homeostasis

Inferred from electronic annotation. Source: InterPro

glycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionFAD binding

Inferred from electronic annotation. Source: InterPro

dihydrolipoyl dehydrogenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 470470Dihydrolipoyl dehydrogenase
PRO_0000068016

Regions

Nucleotide binding39 – 479FAD By similarity
Nucleotide binding183 – 1875NAD By similarity
Nucleotide binding272 – 2754NAD By similarity

Sites

Active site4471Proton acceptor By similarity
Binding site561FAD By similarity
Binding site1191FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site2061NAD By similarity
Binding site3151FAD By similarity
Binding site3231FAD; via amide nitrogen By similarity

Amino acid modifications

Disulfide bond47 ↔ 52Redox-active By similarity

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Sequences

Sequence LengthMass (Da)Tools
P21880-1 [UniParc].

Last modified May 1, 1991. Version 1.
Checksum: 874CA310F3B48A5F

FASTA47049,733
        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

« Hide

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References

« Hide 'large scale' references
[1]"Secretory S complex of Bacillus subtilis: sequence analysis and identity to pyruvate dehydrogenase."
Hemilae H.O., Palva A., Paulin L., Arvidson S., Palva I.
J. Bacteriol. 172:5052-5063(1990) [PubMed: 1697575] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"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."
Winters P., Caldwell R.M., Enfield L., Ferrari E.
Microbiology 142:3033-3037(1996) [PubMed: 8969500] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[3]"Sequence analysis of the mobA-ampS region of the Bacillus subtilis chromosome."
Caldwell R.M., Ferrari E.
Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[4]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
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. expand/collapse author list , 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.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[5]"Sequence of a PAL-related lipoprotein from Bacillus subtilis."
Hemilae H.O.
FEMS Microbiol. Lett. 66:37-41(1991) [PubMed: 1936936] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 461-470.

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Cross-references

Sequence databases

M57435 Genomic DNA. Translation: AAA62684.1.
AF012285 Genomic DNA. Translation: AAC24935.1.
AL009126 Genomic DNA. Translation: CAB13334.1.
PIRE36718.
RefSeqNP_389344.1.

3D structure databases

HSSPHSSP built from PDB template 1EBD based on UniProtKB P11959.
SMRP21880. Positions 8-462.
ModBaseSearch...

Genome annotation databases

GeneID939492.
GenomeReviewsGene locus BSU14610 in contig AL009126_GR.
KEGGbsu:BSU14610.
NMPDRfig|224308.1.peg.1463.

Organism-specific databases

SubtiListBG10210. pdhD. [Micado]
CMRSearch...

Phylogenomic databases

HOGENOMP21880.
OMAP21880. ASICGPE.

Enzyme and pathway databases

BioCycBSUB224308:BSU1463-MON.
MetaCyc:MON-11687.
BRENDA1.8.1.4. 150.

Family and domain databases

InterProIPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR000815. Hg_reductase.
IPR006258. Lipoamide_DH.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD_bd.
[Graphical view]
Gene3DG3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.
PANTHERPTHR22912:SF20. Lipoamide_DH. 1 hit.
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
PR00945. HGRDTASE.
ProDomPD000139. FAD_pyr_redox. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01350. lipoamide_DH. 1 hit.
PROSITEPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameDLDH1_BACSU
AccessionPrimary (citable) accession number: P21880
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: June 16, 2009
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents