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P54533 (DLDH2_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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 branched-chain alpha-keto acid dehydrogenase complex
LPD-Val
Gene names
Name:bfmBC
Synonyms:yqiV
Ordered Locus Names:BSU24060
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›

Protein attributes

Sequence length474 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO2. It contains multiple copies of 3 enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).

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 By similarity.

Subcellular location

Cytoplasm By similarity.

Miscellaneous

The active site is a redox-active disulfide bond By similarity.

Sequence similarities

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

Sequence caution

The sequence M97391 differs from that shown. Reason: Frameshift at position 426.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   DomainRedox-active center
   LigandFAD
Flavoprotein
NAD
   Molecular functionOxidoreductase
   PTMDisulfide bond
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell 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 – 474474Dihydrolipoyl dehydrogenase
PRO_0000068017

Regions

Nucleotide binding34 – 429FAD By similarity
Nucleotide binding188 – 1925NAD By similarity
Nucleotide binding278 – 2814NAD By similarity

Sites

Active site4531Proton acceptor By similarity
Binding site511FAD By similarity
Binding site1141FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site2111NAD By similarity
Binding site2451NAD; via amide nitrogen By similarity
Binding site3201FAD By similarity
Binding site3281FAD; via amide nitrogen By similarity

Amino acid modifications

Disulfide bond42 ↔ 47Redox-active By similarity

Experimental info

Sequence conflict451 – 47323HPHPT…GKAIH → SPASNA in BAA12597. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P54533 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 38F5F8AFCF80D53F

FASTA47450,436
        10         20         30         40         50         60 
MATEYDVVIL GGGTGGYVAA IRAAQLGLKT AVVEKEKLGG TCLHKGCIPS KALLRSAEVY 

        70         80         90        100        110        120 
RTAREADQFG VETAGVSLNF EKVQQRKQAV VDKLAAGVNH LMKKGKIDVY TGYGRILGPS 

       130        140        150        160        170        180 
IFSPLPGTIS VERGNGEEND MLIPKQVIIA TGSRPRMLPG LEVDGKSVLT SDEALQMEEL 

       190        200        210        220        230        240 
PQSIIIVGGG VIGIEWASML HDFGVKVTVI EYADRILPTE DLEISKEMES LLKKKGIQFI 

       250        260        270        280        290        300 
TGAKVLPDTM TKTSDDISIQ AEKDGETVTY SAEKMLVSIG RQANIEGIGL ENTDIVTENG 

       310        320        330        340        350        360 
MISVNESCQT KESHIYAIGD VIGGLQLAHV ASHEGIIAVE HFAGLNPHPL DPTLVPKCIY 

       370        380        390        400        410        420 
SSPEAASVGL TEDEAKANGH NVKIGKFPFM AIGKALVYGE SDGFVKIVAD RDTDDILGVH 

       430        440        450        460        470 
MIGPHVTDMI SEAGLAKVLD ATPWEVGQTI HPHPTLSEAI GEAALAADGK AIHF

« Hide

References

« Hide 'large scale' references
[1]"Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the Bacillus subtilis genome containing the skin element and many sporulation genes."
Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M., Kobayashi Y.
Microbiology 142:3103-3111(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168 / JH642.
[2]"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.
[3]"From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION TO C-TERMINUS.
[4]"The primary structure of branched-chain alpha-oxo acid dehydrogenase from Bacillus subtilis and its similarity to other alpha-oxo acid dehydrogenases."
Wang G.-F., Kuriki T., Roy K.L., Kaneda T.
Eur. J. Biochem. 213:1091-1099(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 412-474.
Strain: 168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D84432 Genomic DNA. Translation: BAA12597.1.
AL009126 Genomic DNA. Translation: CAB14337.2.
M97391 Genomic DNA. No translation available.
PIRD69962.
RefSeqNP_390286.2. NC_000964.3.

3D structure databases

ProteinModelPortalP54533.
SMRP54533. Positions 5-474.
ModBaseSearch...

Protein-protein interaction databases

STRING224308.BSU24060.

Proteomic databases

PaxDbP54533.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB14337; CAB14337; BSU24060.
GeneID938669.
KEGGbsu:BSU24060.
PATRIC18976640. VBIBacSub10457_2510.

Organism-specific databases

GenoListBSU24060. [Micado]

Phylogenomic databases

eggNOGCOG1249.
HOGENOMHOG000276708.
KOK00382.
ProtClustDBPRK05976.

Enzyme and pathway databases

BioCycBSUB:BSU24060-MONOMER.

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 nameDLDH2_BACSU
AccessionPrimary (citable) accession number: P54533
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 1, 2013
This is version 112 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

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