Reviewed, UniProtKB/Swiss-Prot Q04777 (ALDC_BACSU)

Names and origin

Protein names

Recommended name:
    Alpha-acetolactate decarboxylase
    EC=4.1.1.5

Gene names

Name:	alsD
Ordered Locus Names:	BSU36000

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	255 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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; 2,3-butanediol biosynthesis; (R,R)-2,3-butanediol from pyruvate: step 2/3.
Induction	Strongly induced under anaerobic conditions. Activated by resDE, fnr and arfM.
Sequence similarities	Belongs to the alpha-acetolactate decarboxylase family.

Ontologies

Keywords
Biological process	Acetoin biosynthesis
Molecular function	Decarboxylase Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	acetoin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW polyol metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: InterPro
Molecular function	acetolactate decarboxylase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 255	255	Alpha-acetolactate decarboxylase		PRO_0000218438

Sequences

	Sequence		Length	Mass (Da)
	Q04777-1 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: 1B90C69424D39B10	FASTA	255	28,799
	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

References

	« Hide 'large scale' referencesShow '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. , 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
EMBLGenBankDDBJ	L04470 Genomic DNA. Translation: AAA22223.1. Z93767 Genomic DNA. Translation: CAB07786.1. AL009126 Genomic DNA. Translation: CAB15617.1.
PIR	B47126.
RefSeq	NP_391481.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	936857.
GenomeReviews	Gene locus BSU36000 in contig AL009126_GR.
KEGG	bsu:BSU36000.
NMPDR	fig|224308.1.peg.3607.
Organism-specific databases
SubtiList	BG10472. alsD. [Micado]
CMR	Search...
Phylogenomic databases
HOGENOM	Q04777.
OMA	Q04777. DGEMIAF.
Enzyme and pathway databases
BioCyc	BSUB224308:BSU3598-MON.
BRENDA	4.1.1.5. 150.
Family and domain databases
InterPro	IPR005128. Acetolactate_a_deCO2ase. [Graphical view]
Pfam	PF03306. AAL_decarboxy. 1 hit. [Graphical view]
PIRSF	PIRSF001332. Acetolac_decarb. 1 hit.
ProDom	PD006931. Acetolac_decarb. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01252. acetolac_decarb. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ALDC_BACSU

Accession

Primary (citable) accession number: Q04777

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	June 16, 2009
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)