ID   ALDC_METCA              Reviewed;         260 AA.
AC   Q607C3;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Alpha-acetolactate decarboxylase;
DE            EC=4.1.1.5;
GN   Name=budA; OrderedLocusNames=MCA1838;
OS   Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales;
OC   Methylococcaceae; Methylococcus.
OX   NCBI_TaxID=243233;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33009 / NCIMB 11132 / Bath;
RX   PubMed=15383840; DOI=10.1371/journal.pbio.0020303;
RA   Ward N.L., Larsen O., Sakwa J., Bruseth L., Khouri H.M., Durkin A.S.,
RA   Dimitrov G., Jiang L., Scanlan D., Kang K.H., Lewis M.R., Nelson K.E.,
RA   Methe B.A., Wu M., Heidelberg J.F., Paulsen I.T., Fouts D.E., Ravel J.,
RA   Tettelin H., Ren Q., Read T.D., DeBoy R.T., Seshadri R., Salzberg S.L.,
RA   Jensen H.B., Birkeland N.K., Nelson W.C., Dodson R.J., Grindhaug S.H.,
RA   Holt I.E., Eidhammer I., Jonasen I., Vanaken S., Utterback T.R.,
RA   Feldblyum T.V., Fraser C.M., Lillehaug J.R., Eisen J.A.;
RT   "Genomic insights into methanotrophy: the complete genome sequence of
RT   Methylococcus capsulatus (Bath).";
RL   PLoS Biol. 2:1616-1628(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; AE017282; AAU91940.1; -; Genomic_DNA.
DR   RefSeq; WP_010961090.1; NC_002977.6.
DR   AlphaFoldDB; Q607C3; -.
DR   SMR; Q607C3; -.
DR   STRING; 243233.MCA1838; -.
DR   EnsemblBacteria; AAU91940; AAU91940; MCA1838.
DR   KEGG; mca:MCA1838; -.
DR   eggNOG; COG3527; Bacteria.
DR   HOGENOM; CLU_072561_0_0_6; -.
DR   OMA; YKPMLEA; -.
DR   OrthoDB; 1445885at2; -.
DR   UniPathway; UPA00626; UER00678.
DR   Proteomes; UP000006821; 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..260
FT                   /note="Alpha-acetolactate decarboxylase"
FT                   /id="PRO_0000403435"
SQ   SEQUENCE   260 AA;  29184 MW;  EA3460282205D7D0 CRC64;
     MAIDDIFIQA FRTHQQKGDL FHPLGHEDHE VFQSSTIGAL MEGVYDGDTT YGELARHGDF
     GLGTFNALDG EMIALGGRFF QIKSDGKAYP VPPTAKTPFA VVTLFDPTVQ VVWPDPIDWK
     QFQAAVDKAV PSKNVFYAIR VRACFDHIRV RTVPRQRKPY PPLVEVARRQ PEFEYGHLEG
     TLVGFRFPDY TQGVNVAGYH VHFLDKAETL GGHVLDFSMR NAVVDIDVTS QFRMEVPECG
     AFLDADLARN QDEAIHEAEN