ID   ALDC_RAOTE              Reviewed;         259 AA.
AC   Q04518;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Alpha-acetolactate decarboxylase;
DE            EC=4.1.1.5;
GN   Name=budA;
OS   Raoultella terrigena (Klebsiella terrigena).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Raoultella.
OX   NCBI_TaxID=577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=VTT-E-74023;
RX   PubMed=8444801; DOI=10.1128/jb.175.5.1392-1404.1993;
RA   Blomqvist K., Nikkola M., Lehtovaara P., Suihko M.-L., Airaksinen U.,
RA   Straby K.B., Knowles J.K.C., Penttilae M.E.;
RT   "Characterization of the genes of the 2,3-butanediol operons from
RT   Klebsiella terrigena and Enterobacter aerogenes.";
RL   J. Bacteriol. 175:1392-1404(1993).
CC   -!- FUNCTION: Converts acetolactate into acetoin, which can be excreted by
CC       the cells. This may be a mechanism for controlling the internal pH of
CC       cells in the stationary stage.
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; L04507; AAA25054.1; -; Genomic_DNA.
DR   PIR; C47069; C47069.
DR   RefSeq; WP_041145972.1; NZ_VRKM01000010.1.
DR   AlphaFoldDB; Q04518; -.
DR   SMR; Q04518; -.
DR   GeneID; 57504478; -.
DR   UniPathway; UPA00626; UER00678.
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.
FT   CHAIN           1..259
FT                   /note="Alpha-acetolactate decarboxylase"
FT                   /id="PRO_0000218440"
SQ   SEQUENCE   259 AA;  29194 MW;  EC46F996CDE1CAE5 CRC64;
     MNHYPECTCQ ESLCETVRGF SAHHPDSVIY QTSLMSALLS GVYEGSTTIA DLLTHGDFGL
     GTFNELDGEL IAFSSEVYQL RADGSARKAR ADQKTPFAVM TWFRPQYRKT FDHPVSRQQL
     HDVIDQQIPS DNLFCALHID GHFRHAHTRT VPRQTPPYRA MTDVLDDQPV FRFNQRKGTL
     VGFRTPQHMQ GLNVAGYHEH FITDDRQGGG HLLDYQLDSG VLTFGEIHKL MIDLPADSAF
     LQADLHPDNL DAAIRAVEN