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Q04777 (ALDC_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Alpha-acetolactate decarboxylase
EC=4.1.1.5
Gene names
Name:alsD
Ordered Locus Names:BSU36000
OrganismBacillus subtilis
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length255 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Converts acetolactate into acetoin, which can be excreted by the cells. This may be a mechanism for controlling the internal pH of cells in the stationary stage.

Catalytic activity

(2S)-2-hydroxy-2-methyl-3-oxobutanoate = (3R)-3-hydroxybutan-2-one + CO2.

Pathway

Polyol metabolism; (R,R)-butane-2,3-diol biosynthesis; (R,R)-butane-2,3-diol from pyruvate: step 2/3.

Induction

Strongly induced under anaerobic conditions. Activated by ResDE, Fnr and ArfM. Ref.4

Sequence similarities

Belongs to the alpha-acetolactate decarboxylase family.

Ontologies

Keywords
   Biological processAcetoin biosynthesis
   Molecular functionDecarboxylase
Lyase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processacetoin biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

polyol metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentendoplasmic reticulum membrane

Inferred from electronic annotation. Source: InterPro

   Molecular functionacetolactate decarboxylase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 255255Alpha-acetolactate decarboxylase
PRO_0000218438

Sequences

Sequence LengthMass (Da)Tools
Q04777 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 1B90C69424D39B10

FASTA25528,799
        10         20         30         40         50         60 
MKRESNIQVL SRGQKDQPVS QIYQVSTMTS LLDGVYDGDF ELSEIPKYGD FGIGTFNKLD 

        70         80         90        100        110        120 
GELIGFDGEF YRLRSDGTAT PVQNGDRSPF CSFTFFTPDM THKIDAKMTR EDFEKEINSM 

       130        140        150        160        170        180 
LPSRNLFYAI RIDGLFKKVQ TRTVELQEKP YVPMVEAVKT QPIFNFDNVR GTIVGFLTPA 

       190        200        210        220        230        240 
YANGIAVSGY HLHFIDEGRN SGGHVFDYVL EDCTVTISQK MNMNLRLPNT ADFFNANLDN 

       250 
PDFAKDIETT EGSPE

« Hide

References

« Hide 'large scale' references
[1]"Regulation of the Bacillus subtilis alsS, alsD, and alsR genes involved in post-exponential-phase production of acetoin."
Renna M.C., Najimudin N., Winik L.R., Zahler S.A.
J. Bacteriol. 175:3863-3875(1993) [PubMed: 7685336] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The Bacillus subtilis genome from gerBC (311 degrees) to licR (334 degrees)."
Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V., Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G., Kunst F., Danchin A., Glaser P.
Microbiology 143:3313-3328(1997) [PubMed: 9353933] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[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: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[4]"Fermentative metabolism of Bacillus subtilis: physiology and regulation of gene expression."
Cruz Ramos H., Hoffmann T., Marino M., Nedjari H., Presecan-Siedel E., Dreesen O., Glaser P., Jahn D.
J. Bacteriol. 182:3072-3080(2000) [PubMed: 10809684] [Abstract]
Cited for: REGULATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L04470 Genomic DNA. Translation: AAA22223.1.
Z93767 Genomic DNA. Translation: CAB07786.1.
AL009126 Genomic DNA. Translation: CAB15617.1.
PIRB47126.
RefSeqNP_391481.1. NC_000964.3.

3D structure databases

ProteinModelPortalQ04777.
SMRQ04777. Positions 19-251.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000003668; EBBACP00000003668; EBBACG00000003661.
GeneID936857.
GenomeReviewsGene locus BSU36000 in contig AL009126_GR.
KEGGbsu:BSU36000.
NMPDRfig|224308.1.peg.3607.
PATRIC18979220. VBIBacSub10457_3772.

Organism-specific databases

GenoListBSU36000. [Micado]

Phylogenomic databases

GeneTreeEBGT00050000002881.
HOGENOMHBG364469.
OMAEMSYTVE.
PhylomeDBQ04777.
ProtClustDBCLSK887995.

Enzyme and pathway databases

BioCycBSUB:BSU36000-MONOMER.

Family and domain databases

InterProIPR005128. Acetolactate_a_deCO2ase.
[Graphical view]
KOK01575.
PfamPF03306. AAL_decarboxy. 1 hit.
[Graphical view]
PIRSFPIRSF001332. Acetolac_decarb. 1 hit.
TIGRFAMsTIGR01252. Acetolac_decarb. 1 hit.
ProtoNetSearch...

Entry information

Entry nameALDC_BACSU
AccessionPrimary (citable) accession number: Q04777
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: January 25, 2012
This is version 90 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