ID   ALDC_VIBCH              Reviewed;         261 AA.
AC   Q9KRP7;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Alpha-acetolactate decarboxylase;
DE            EC=4.1.1.5;
GN   OrderedLocusNames=VC_1589;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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; AE003852; AAF94743.1; -; Genomic_DNA.
DR   PIR; H82180; H82180.
DR   RefSeq; NP_231229.1; NC_002505.1.
DR   RefSeq; WP_001068896.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9KRP7; -.
DR   SMR; Q9KRP7; -.
DR   STRING; 243277.VC_1589; -.
DR   DNASU; 2613843; -.
DR   EnsemblBacteria; AAF94743; AAF94743; VC_1589.
DR   GeneID; 57740243; -.
DR   GeneID; 66939445; -.
DR   KEGG; vch:VC_1589; -.
DR   PATRIC; fig|243277.26.peg.1515; -.
DR   eggNOG; COG3527; Bacteria.
DR   HOGENOM; CLU_072561_0_0_6; -.
DR   OMA; YKPMLEA; -.
DR   BioCyc; VCHO:VC1589-MON; -.
DR   UniPathway; UPA00626; UER00678.
DR   Proteomes; UP000000584; Chromosome 1.
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..261
FT                   /note="Alpha-acetolactate decarboxylase"
FT                   /id="PRO_0000403438"
SQ   SEQUENCE   261 AA;  29340 MW;  97FEBA9EBBDA721A CRC64;
     MNPLLSAHCS CSQEIAQQFA HYQHISGEGE IYQTSLMSAL IAGVYEGATT IAQLLEHGDF
     GLGTFNELDG ELIAFDRQVF QLRADGSAQP AHPEQQTPFA VFTFFKADIE LPITERMTRE
     QVHQLIDRLV PSDNLFCAIR IDGTFPSVQT RTVPKQQRPY RPMLEVVKQQ PVFRFQQQHG
     VIAGFRSPQY TTGINVPGYH EHFITQQRTG GGHIQDYIIR SGFLQIGRVS RLVVDTPVSR
     DFLEANLTPN NIRTAIEAAE K