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Reviewed, UniProtKB/Swiss-Prot O34788 (BDHA_BACSU)

Last modified November 24, 2009. Version 64. 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:
    (R,R)-butanediol dehydrogenase
    EC=1.1.1.4
Alternative name(s):
    Acetoin reductase/2,3-butanediol dehydrogenase
      Short name=AR/BDH
Gene names
Name: bdhA
Synonyms: ydjL
Ordered Locus Names: BSU06240
OrganismBacillus subtilis [Complete proteome] [HAMAP]
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

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Protein attributes

Sequence length346 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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General annotation (Comments)

Catalytic activity

(R,R)-butane-2,3-diol + NAD+ = (R)-acetoin + NADH.

Cofactor

Zinc Potential.

Disruption phenotype

Cells lacking this gene have no acetoin reductase/2,3-butanediol dehydrogenase activity. Ref.3

Sequence similarities

Belongs to the zinc-containing alcohol dehydrogenase family.

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Ontologies

Keywords
   LigandMetal-binding
NAD
Zinc
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular function(R,R)-butanediol dehydrogenase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 346346(R,R)-butanediol dehydrogenase
PRO_0000378092

Sites

Metal binding371Zinc Potential
Metal binding701Zinc Potential
Metal binding1521Zinc Potential

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Sequences

Sequence LengthMass (Da)Tools
O34788-1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 5E327192D678F8A2

FASTA34637,341
        10         20         30         40         50         60 
MKAARWHNQK DIRIEHIEEP KTEPGKVKIK VKWCGICGSD LHEYLGGPIF IPVDKPHPLT 

        70         80         90        100        110        120 
NETAPVTMGH EFSGEVVEVG EGVENYKVGD RVVVEPIFAT HGHQGAYNLD EQMGFLGLAG 

       130        140        150        160        170        180 
GGGGFSEYVS VDEELLFKLP DELSYEQGAL VEPSAVALYA VRSSKLKAGD KAAVFGCGPI 

       190        200        210        220        230        240 
GLLVIEALKA AGATDIYAVE LSPERQQKAE ELGAIIVDPS KTDDVVAEIA ERTGGGVDVA 

       250        260        270        280        290        300 
FEVTGVPVVL RQAIQSTTIA GETVIVSIWE KGAEIHPNDI VIKERTVKGI IGYRDIFPAV 

       310        320        330        340 
LSLMKEGYFS ADKLVTKKIV LDDLIEEGFG ALIKEKSQVK ILVRPN

« Hide

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References

« Hide 'large scale' references
[1]"Sequence analysis of the groESL-cotA region of the Bacillus subtilis genome, containing the restriction/modification system genes."
Kasahara Y., Nakai S., Ogasawara N., Yata K., Sadaie Y.
DNA Res. 4:335-339(1997) [PubMed: 9455482] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168 / Marburg.
[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: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[3]"The Bacillus subtilis ydjL (bdhA) gene encodes acetoin reductase/2,3-butanediol dehydrogenase."
Nicholson W.L.
Appl. Environ. Microbiol. 74:6832-6838(2008) [PubMed: 18820069] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
Strain: 168.

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Cross-references

Sequence databases

AB007638 Genomic DNA. Translation: BAA22767.1.
AL009126 Genomic DNA. Translation: CAB12443.1.
PIRH69789.
RefSeqNP_388505.1.

3D structure databases

HSSPHSSP built from PDB template 1RJW based on UniProtKB P42328.
ModBaseSearch...

Genome annotation databases

GeneID939490.
GenomeReviewsGene locus BSU06240 in contig AL009126_GR.
KEGGbsu:BSU06240.
NMPDRfig|224308.1.peg.624.

Organism-specific databases

SubtiListBG12803. bdhA. [Micado]
CMRSearch...

Phylogenomic databases

HOGENOMO34788.
OMAIVIKERT

Enzyme and pathway databases

BioCycSUBTI:BSU06240-MON.

Family and domain databases

InterProIPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn.
IPR013149. ADH_Zn-bd.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR11695. ADH_Sf_Zn. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
PROSITEPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameBDHA_BACSU
AccessionPrimary (citable) accession number: O34788
Secondary accession number(s): Q797C2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 16, 2009
Last sequence update: January 1, 1998
Last modified: November 24, 2009
This is version 64 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