ID   ALDC_METMA              Reviewed;         288 AA.
AC   Q8PZ55;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=Alpha-acetolactate decarboxylase;
DE            EC=4.1.1.5;
DE   Flags: Precursor;
GN   OrderedLocusNames=MM_0639;
OS   Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS   11833 / OCM 88) (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=192952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX   PubMed=12125824;
RA   Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA   Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA   Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA   Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA   Fritz H.-J., Gottschalk G.;
RT   "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT   between Bacteria and Archaea.";
RL   J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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; AE008384; AAM30335.1; -; Genomic_DNA.
DR   RefSeq; WP_011032590.1; NC_003901.1.
DR   AlphaFoldDB; Q8PZ55; -.
DR   SMR; Q8PZ55; -.
DR   STRING; 192952.MM_0639; -.
DR   PRIDE; Q8PZ55; -.
DR   EnsemblBacteria; AAM30335; AAM30335; MM_0639.
DR   GeneID; 24876925; -.
DR   KEGG; mma:MM_0639; -.
DR   PATRIC; fig|192952.21.peg.757; -.
DR   eggNOG; arCOG03340; Archaea.
DR   HOGENOM; CLU_072561_0_0_2; -.
DR   OMA; YKPMLEA; -.
DR   UniPathway; UPA00626; UER00678.
DR   Proteomes; UP000000595; 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; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..288
FT                   /note="Alpha-acetolactate decarboxylase"
FT                   /id="PRO_0000403436"
SQ   SEQUENCE   288 AA;  31604 MW;  CA61B52D5FF1DB41 CRC64;
     MNIKYFLIFL ILLAVTSFTL FSGCTGFAGN TPETSGKNSN VESIENLVPD ISNNASDVLY
     QVSTIDALLL GVYDGVLPVS DLKTHGDFGI GTFDGLEGEM LALDGNYYQI KTDGIAYPVS
     GEITTPFATV TYFEADETFR LEKSANLSEL EDFLDLNLPS ENLFYAVKVD GNFSYVKARS
     VPRQEKPYLQ LADAVSSQSV FEFENVSGTL VGFRTPEYVK GVNVPGYHLH FITENRSAGG
     HVLDLEMEKG DAALDITSIF LMELPASGDF YNAELGQNLQ EDLEKVEK