ID   ALDC_LACLM              Reviewed;         236 AA.
AC   P77880; A2RKQ4;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Alpha-acetolactate decarboxylase;
DE            EC=4.1.1.5;
GN   Name=aldB; OrderedLocusNames=llmg_1275;
OS   Lactococcus lactis subsp. cremoris (strain MG1363).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus; Lactococcus cremoris subsp. cremoris.
OX   NCBI_TaxID=416870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8779601; DOI=10.1128/aem.62.7.2641-2643.1996;
RA   Swindell S.R., Benson K.H., Griffin H.G., Renault P., Ehrlich S.D.,
RA   Gasson M.J.;
RT   "Genetic manipulation of the pathway for diacetyl metabolism in Lactococcus
RT   lactis.";
RL   Appl. Environ. Microbiol. 62:2641-2643(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MG1363;
RX   PubMed=17307855; DOI=10.1128/jb.01768-06;
RA   Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA   Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA   van Sinderen D., Kok J.;
RT   "The complete genome sequence of the lactic acid bacterial paradigm
RT   Lactococcus lactis subsp. cremoris MG1363.";
RL   J. Bacteriol. 189:3256-3270(2007).
CC   -!- FUNCTION: Converts acetolactate into acetoin.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X82620; CAA57941.1; -; Genomic_DNA.
DR   EMBL; AM406671; CAL97868.1; -; Genomic_DNA.
DR   RefSeq; WP_011835154.1; NZ_WJVF01000013.1.
DR   AlphaFoldDB; P77880; -.
DR   SMR; P77880; -.
DR   STRING; 416870.llmg_1275; -.
DR   PRIDE; P77880; -.
DR   EnsemblBacteria; CAL97868; CAL97868; llmg_1275.
DR   KEGG; llm:llmg_1275; -.
DR   eggNOG; COG3527; Bacteria.
DR   HOGENOM; CLU_072561_0_0_9; -.
DR   OMA; YKPMLEA; -.
DR   PhylomeDB; P77880; -.
DR   BioCyc; LLAC416870:LLMG_RS06465-MON; -.
DR   UniPathway; UPA00626; UER00678.
DR   Proteomes; UP000000364; 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.
FT   CHAIN           1..236
FT                   /note="Alpha-acetolactate decarboxylase"
FT                   /id="PRO_0000218442"
SQ   SEQUENCE   236 AA;  26366 MW;  32269A9E8CC871A5 CRC64;
     MSEITQLFQY NTLGALMAGL YEGTMTIGEL LKHGDLGIGT LDSIDGELIV LDGKAYQAKG
     DKTIVELTDD IKVPYAAVVP HQAEVVFKQK FTVSDKELED RIESYFDGQN LFRSIKITGK
     FPKMHVRMIP RAKSGTKFVE VSQNQPEYTE ENIKGTIVGI WTPEMFHGVS VAGYHLHFIS
     EDFTFGGHVL DFIIDNGTVE IGAIDQLNQS FPVQDRKFLF ADLDIEALKK DIDVAE