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O34324 (DLDH3_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dihydrolipoyl dehydrogenase
EC=1.8.1.4
Alternative name(s):
Dihydrolipoamide dehydrogenase
E3 component of acetoin cleaving system
Gene names
Name:acoL
Synonyms:yfjH
Ordered Locus Names:BSU08090
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›

Protein attributes

Sequence length458 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 1 FAD per subunit By similarity.

Pathway

Ketone degradation; acetoin degradation.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm Potential.

Miscellaneous

The active site is a redox-active disulfide bond.

Sequence similarities

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

Ontologies

Keywords
   Biological processAcetoin catabolism
Glycolysis
   Cellular componentCytoplasm
   DomainRedox-active center
   LigandFAD
Flavoprotein
NAD
   Molecular functionOxidoreductase
   PTMDisulfide bond
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processacetoin catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

cell redox homeostasis

Inferred from electronic annotation. Source: InterPro

glycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functiondihydrolipoyl dehydrogenase activity

Inferred from electronic annotation. Source: EC

flavin adenine dinucleotide binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 458458Dihydrolipoyl dehydrogenase
PRO_0000068018

Regions

Nucleotide binding30 – 389FAD By similarity
Nucleotide binding177 – 1815NAD By similarity
Nucleotide binding263 – 2664NAD By similarity

Sites

Active site4371Proton acceptor By similarity
Binding site471FAD By similarity
Binding site1121FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site2001NAD By similarity
Binding site3051FAD By similarity
Binding site3131FAD; via amide nitrogen By similarity

Amino acid modifications

Disulfide bond38 ↔ 43Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
O34324 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 2496832534945183

FASTA45848,853
        10         20         30         40         50         60 
MTLAIIGGGP AGYAAAVSAA QQGRNVLLID KGKLGGTCLN EGCIPTKSLL ESANVLDKIK 

        70         80         90        100        110        120 
HADSFGIELP AGAISVDWSK MQSRKQQVVS QLVQGVQYLM KKNQIQVVKG TASFLSERKL 

       130        140        150        160        170        180 
LIEGENGKEI READQVLIAS GSEPIELPFA PFDGEWILDS KDALSLSEIP SSLVIVGGGV 

       190        200        210        220        230        240 
IGCEYAGLFA RLGSQVTIIE TADRLIPAED EDIARLFQEK LEEDGVEVHT SSRLGRVDQT 

       250        260        270        280        290        300 
AKTAIWKSGQ REFKTKADYV LVAIGRKPRL DGLQLEQAGV DFSPKGIPVN GHMQTNVPHI 

       310        320        330        340        350        360 
YACGDAIGGI QLAHAAFHEG IIAASHASGR DVKINEKHVP RCIYTSPEIA CIGMTERQAR 

       370        380        390        400        410        420 
SIYGDVKIGE FSFSANGKAL IKQQAEGKVK IMAEPEFGEI VGVSMIGPDV TELIGQAAAI 

       430        440        450 
MNGEMTADMA EHFIAAHPTL SETLHEALLS TIGLAVHA

« Hide

References

« Hide 'large scale' references
[1]"Biochemical and molecular characterization of the Bacillus subtilis acetoin catabolic pathway."
Huang M., Oppermann-Sanio F.B., Steinbuechel A.
J. Bacteriol. 181:3837-3841(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168 / ATCC 33234 / DSM 402 / NCIMB 10106.
[2]"Cloning and sequencing of a 40.6 kb segment in the 73 degrees-76 degrees region of the Bacillus subtilis chromosome containing genes for trehalose metabolism and acetoin utilization."
Yamamoto H., Uchiyama S., Sekiguchi J.
Microbiology 142:3057-3065(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168 / AC327.
[3]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF006075 Genomic DNA. Translation: AAC05585.1.
D78509 Genomic DNA. Translation: BAA24293.1.
AL009126 Genomic DNA. Translation: CAB12638.1.
PIRG69581.
RefSeqNP_388690.1. NC_000964.3.

3D structure databases

ProteinModelPortalO34324.
SMRO34324. Positions 1-458.
ModBaseSearch...

Protein-protein interaction databases

STRING224308.BSU08090.

Proteomic databases

PaxDbO34324.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB12638; CAB12638; BSU08090.
GeneID939702.
KEGGbsu:BSU08090.
PATRIC18973268. VBIBacSub10457_0848.

Organism-specific databases

GenoListBSU08090. [Micado]

Phylogenomic databases

eggNOGCOG1249.
HOGENOMHOG000276708.
KOK00382.
OMANSSHAMS.
ProtClustDBPRK06912.

Enzyme and pathway databases

BioCycBSUB:BSU08090-MONOMER.
UniPathwayUPA00040.

Family and domain databases

Gene3D3.30.390.30. 1 hit.
InterProIPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR006258. Lipoamide_DH.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
[Graphical view]
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
SUPFAMSSF55424. FAD/NAD-linked_reductase_dimer. 1 hit.
TIGRFAMsTIGR01350. lipoamide_DH. 1 hit.
PROSITEPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDLDH3_BACSU
AccessionPrimary (citable) accession number: O34324
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: May 1, 2013
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents