ID ALDC_BACSU Reviewed; 255 AA. AC Q04777; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 16-JUN-2009, entry version 70. DE RecName: Full=Alpha-acetolactate decarboxylase; DE EC=4.1.1.5; GN Name=alsD; OrderedLocusNames=BSU36000; OS Bacillus subtilis. OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1423; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=93286000; PubMed=7685336; RA Renna M.C., Najimudin N., Winik L.R., Zahler S.A.; RT "Regulation of the Bacillus subtilis alsS, alsD, and alsR genes RT involved in post-exponential-phase production of acetoin."; RL J. Bacteriol. 175:3863-3875(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=168; RX MEDLINE=98015417; PubMed=9353933; RA Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V., RA Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., RA Villani G., Kunst F., Danchin A., Glaser P.; RT "The Bacillus subtilis genome from gerBC (311 degrees) to licR (334 RT degrees)."; RL Microbiology 143:3313-3328(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=168; RX MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786; RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., RA Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., RA Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., RA Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., RA Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., RA Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., RA Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., RA Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., RA Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., RA Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., RA Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., RA Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., RA Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., RA Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., RA Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., RA Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., RA Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., RA Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., RA Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., RA Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., RA Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., RA Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., RA Yoshikawa H., Danchin A.; RT "The complete genome sequence of the Gram-positive bacterium Bacillus RT subtilis."; RL Nature 390:249-256(1997). RN [4] RP REGULATION. RX MEDLINE=20270134; PubMed=10809684; RX DOI=10.1128/JB.182.11.3072-3080.2000; RA Cruz Ramos H., Hoffmann T., Marino M., Nedjari H., Presecan-Siedel E., RA Dreesen O., Glaser P., Jahn D.; RT "Fermentative metabolism of Bacillus subtilis: physiology and RT regulation of gene expression."; RL J. Bacteriol. 182:3072-3080(2000). CC -!- FUNCTION: Converts acetolactate into acetoin, which can be CC excreted by the cells. This may be a mechanism for controlling the CC internal pH of cells in the stationary stage. CC -!- CATALYTIC ACTIVITY: (2S)-2-hydroxy-2-methyl-3-oxobutanoate = (3R)- CC 3-hydroxybutan-2-one + CO(2). CC -!- PATHWAY: Polyol metabolism; 2,3-butanediol biosynthesis; (R,R)- CC 2,3-butanediol from pyruvate: step 2/3. CC -!- INDUCTION: Strongly induced under anaerobic conditions. Activated CC by resDE, fnr and arfM. CC -!- SIMILARITY: Belongs to the alpha-acetolactate decarboxylase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L04470; AAA22223.1; -; Genomic_DNA. DR EMBL; Z93767; CAB07786.1; -; Genomic_DNA. DR EMBL; AL009126; CAB15617.1; -; Genomic_DNA. DR PIR; B47126; B47126. DR RefSeq; NP_391481.1; -. DR GeneID; 936857; -. DR GenomeReviews; AL009126_GR; BSU36000. DR KEGG; bsu:BSU36000; -. DR NMPDR; fig|224308.1.peg.3607; -. DR SubtiList; BG10472; alsD. DR HOGENOM; Q04777; -. DR OMA; Q04777; DGEMIAF. DR BioCyc; BSUB224308:BSU3598-MON; -. DR BRENDA; 4.1.1.5; 150. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:InterPro. DR GO; GO:0047605; F:acetolactate decarboxylase activity; IEA:EC. DR GO; GO:0045151; P:acetoin biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0019751; P:polyol metabolic process; IEA:InterPro. DR InterPro; IPR005128; Acetolactate_a_deCO2ase. DR Pfam; PF03306; AAL_decarboxy; 1. DR PIRSF; PIRSF001332; Acetolac_decarb; 1. DR ProDom; PD006931; Acetolac_decarb; 1. DR TIGRFAMs; TIGR01252; acetolac_decarb; 1. PE 2: Evidence at transcript level; KW Acetoin biosynthesis; Complete proteome; Decarboxylase; Lyase. FT CHAIN 1 255 Alpha-acetolactate decarboxylase. FT /FTId=PRO_0000218438. SQ SEQUENCE 255 AA; 28799 MW; 1B90C69424D39B10 CRC64; MKRESNIQVL SRGQKDQPVS QIYQVSTMTS LLDGVYDGDF ELSEIPKYGD FGIGTFNKLD GELIGFDGEF YRLRSDGTAT PVQNGDRSPF CSFTFFTPDM THKIDAKMTR EDFEKEINSM LPSRNLFYAI RIDGLFKKVQ TRTVELQEKP YVPMVEAVKT QPIFNFDNVR GTIVGFLTPA YANGIAVSGY HLHFIDEGRN SGGHVFDYVL EDCTVTISQK MNMNLRLPNT ADFFNANLDN PDFAKDIETT EGSPE //