ID   ALDC_STRTR              Reviewed;         239 AA.
AC   Q8L208;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=Alpha-acetolactate decarboxylase;
DE            EC=4.1.1.5;
GN   Name=aldC;
OS   Streptococcus thermophilus.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP   REGULATION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=CNRZ 385;
RX   PubMed=12753249; DOI=10.1046/j.1472-765x.2003.01326.x;
RA   Monnet C., Nardi M., Hols P., Gulea M., Corrieu G., Monnet V.;
RT   "Regulation of branched-chain amino acid biosynthesis by alpha-acetolactate
RT   decarboxylase in Streptococcus thermophilus.";
RL   Lett. Appl. Microbiol. 36:399-405(2003).
CC   -!- FUNCTION: Converts acetolactate into acetoin. Regulates leucine and
CC       valine biosynthesis by diverting the flux of alpha-acetolactate towards
CC       acetoin when the branched-chain amino acids are present in high
CC       concentration. {ECO:0000269|PubMed:12753249}.
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         Evidence={ECO:0000269|PubMed:12753249};
CC   -!- ACTIVITY REGULATION: The enzyme is active only in the presence of
CC       branched-chain amino acids. Valine results in much higher activation
CC       than leucine or isoleucine. {ECO:0000269|PubMed:12753249}.
CC   -!- PATHWAY: Polyol metabolism; (R,R)-butane-2,3-diol biosynthesis; (R,R)-
CC       butane-2,3-diol from pyruvate: step 2/3.
CC   -!- DISRUPTION PHENOTYPE: Slower growth in media containing valine, leucine
CC       plus isoleucine, or leucine plus valine. {ECO:0000269|PubMed:12753249}.
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; AY072795; AAL68399.1; -; Genomic_DNA.
DR   RefSeq; WP_011227170.1; NZ_WMLD01000014.1.
DR   AlphaFoldDB; Q8L208; -.
DR   SMR; Q8L208; -.
DR   STRING; 322159.STER_0941; -.
DR   GeneID; 66898792; -.
DR   eggNOG; COG3527; Bacteria.
DR   OMA; YKPMLEA; -.
DR   BRENDA; 4.1.1.5; 5956.
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   1: Evidence at protein level;
KW   Acetoin biosynthesis; Decarboxylase; Lyase.
FT   CHAIN           1..239
FT                   /note="Alpha-acetolactate decarboxylase"
FT                   /id="PRO_0000403437"
SQ   SEQUENCE   239 AA;  26843 MW;  23235EC9402DBE3C CRC64;
     MSEAIKLFQY NTLGALMAGL YGGTLTVGEL LEHGDLGLGT LDSIDGELIV LDGKAYQAKG
     SEGKVEVVEV SPDEKVPYAA VVPHQAEVIF RQRYEMTDKE LEDRIESYYD GVNLFRSIKI
     KGHFKHMHVR MIPKSNADIK FADVATRQPE YEVDDISGTI VGIWTPEMFH GVSVAGYHLH
     FISDDLTFGG HVMDFVIENG IIEVGPVDQL DQRFPVQDRQ YLFAKFNVDE MRKDITKAE