ALDC_BACLD
ID ALDC_BACLD Reviewed; 253 AA.
AC Q65E52; Q62PM2;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Alpha-acetolactate decarboxylase;
DE EC=4.1.1.5;
GN Name=alsD; OrderedLocusNames=BL02479, BLi03847;
OS Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=279010;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX PubMed=15383718; DOI=10.1159/000079829;
RA Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P.,
RA Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.;
RT "The complete genome sequence of Bacillus licheniformis DSM13, an organism
RT with great industrial potential.";
RL J. Mol. Microbiol. Biotechnol. 7:204-211(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A.,
RA Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT "Complete genome sequence of the industrial bacterium Bacillus
RT licheniformis and comparisons with closely related Bacillus species.";
RL Genome Biol. 5:R77.1-R77.12(2004).
CC -!- FUNCTION: Converts acetolactate into acetoin. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S)-2-acetolactate + H(+) = (R)-acetoin + CO2;
CC Xref=Rhea:RHEA:21580, ChEBI:CHEBI:15378, ChEBI:CHEBI:15686,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:58476; EC=4.1.1.5;
CC -!- PATHWAY: Polyol metabolism; (R,R)-butane-2,3-diol biosynthesis; (R,R)-
CC butane-2,3-diol from pyruvate: step 2/3.
CC -!- SIMILARITY: Belongs to the alpha-acetolactate decarboxylase family.
CC {ECO:0000305}.
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DR EMBL; CP000002; AAU25289.1; -; Genomic_DNA.
DR EMBL; AE017333; AAU42662.1; -; Genomic_DNA.
DR RefSeq; WP_003185849.1; NC_006322.1.
DR AlphaFoldDB; Q65E52; -.
DR SMR; Q65E52; -.
DR STRING; 279010.BL02479; -.
DR EnsemblBacteria; AAU25289; AAU25289; BL02479.
DR GeneID; 66214201; -.
DR KEGG; bld:BLi03847; -.
DR KEGG; bli:BL02479; -.
DR eggNOG; COG3527; Bacteria.
DR HOGENOM; CLU_072561_0_0_9; -.
DR OMA; YKPMLEA; -.
DR OrthoDB; 1445885at2; -.
DR BioCyc; BLIC279010:BLI_RS18915-MON; -.
DR UniPathway; UPA00626; UER00678.
DR Proteomes; UP000000606; Chromosome.
DR GO; GO:0047605; F:acetolactate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0045151; P:acetoin biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd17299; acetolactate_decarboxylase; 1.
DR InterPro; IPR005128; Acetolactate_a_deCO2ase.
DR PANTHER; PTHR35524; PTHR35524; 1.
DR Pfam; PF03306; AAL_decarboxy; 1.
DR PIRSF; PIRSF001332; Acetolac_decarb; 1.
DR TIGRFAMs; TIGR01252; acetolac_decarb; 1.
PE 3: Inferred from homology;
KW Acetoin biosynthesis; Decarboxylase; Lyase; Reference proteome.
FT CHAIN 1..253
FT /note="Alpha-acetolactate decarboxylase"
FT /id="PRO_0000403434"
SQ SEQUENCE 253 AA; 28864 MW; A2EE593B8C5237B8 CRC64;
MKSASKQKII QPVDKNLDQV YQVSTMVSLL DGIYDGDFYM SEAKEHGDFG IGTFNRLDGE
LIGFDGEFYR LRSDGKAYPV QGSDCSPFCS LAFFRPDIYH EIKQRMPLEA FEEEMKRIMP
SENLFYAIRM DGTFKKVKTR TVELQEKPYV PMVDAVKSQP IFDFNDITGT IVGFWTPQYA
NGIAVSGFHL HFIDEDRNVG GHVFDYEIEE CTVQISQKLN MNLRLPNTQD FFQADFNKHD
LAAGIEAAEG NPE
