ID   ALDC_KLETE     STANDARD;      PRT;   259 AA.
AC   Q04518;
DT   01-OCT-1993 (Rel. 27, Created)
DT   01-OCT-1993 (Rel. 27, Last sequence update)
DT   01-FEB-2005 (Rel. 46, Last annotation update)
DE   Alpha-acetolactate decarboxylase (EC 4.1.1.5).
GN   Name=budA;
OS   Klebsiella terrigena.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Raoultella.
OX   NCBI_TaxID=577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=VTT-E-74023;
RX   MEDLINE=93186707; PubMed=8444801;
RA   Blomqvist K., Nikkola M., Lehtovaara P., Suihko M.-L., Airaksinen U.,
RA   Straby K.B., Knowles J.K.C., Penttilae M.E.;
RT   "Characterization of the genes of the 2,3-butanediol operons from
RT   Klebsiella terrigena and Enterobacter aerogenes.";
RL   J. Bacteriol. 175:1392-1404(1993).
CC   -!- FUNCTION: Converts acetolactate into acetoin, which can be
CC       excreted by the cells. This may be a mechanism for controlling the
CC       internal pH of cells in the stationary stage.
CC   -!- CATALYTIC ACTIVITY: (S)-2-hydroxy-2-methyl-3-oxobutanoate = (R)-2-
CC       acetoin + CO(2).
CC   -!- PATHWAY: Acetoin biosynthesis.
CC   -!- SIMILARITY: Belongs to the alpha-acetolactate decarboxylase
CC       family.
CC   --------------------------------------------------------------------------
CC   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; L04507; AAA25054.1; -.
DR   PIR; C47069; C47069.
DR   InterPro; IPR005128; Acetolac_decarb.
DR   Pfam; PF03306; AAL_decarboxy; 1.
DR   PIRSF; PIRSF001332; Acetolac_decarb; 1.
DR   ProDom; PD006931; Acetolac_decarb; 1.
DR   TIGRFAMs; TIGR01252; acetolac_decarb; 1.
KW   Acetoin biosynthesis; Decarboxylase; Lyase.
SQ   SEQUENCE   259 AA;  29194 MW;  EC46F996CDE1CAE5 CRC64;
     MNHYPECTCQ ESLCETVRGF SAHHPDSVIY QTSLMSALLS GVYEGSTTIA DLLTHGDFGL
     GTFNELDGEL IAFSSEVYQL RADGSARKAR ADQKTPFAVM TWFRPQYRKT FDHPVSRQQL
     HDVIDQQIPS DNLFCALHID GHFRHAHTRT VPRQTPPYRA MTDVLDDQPV FRFNQRKGTL
     VGFRTPQHMQ GLNVAGYHEH FITDDRQGGG HLLDYQLDSG VLTFGEIHKL MIDLPADSAF
     LQADLHPDNL DAAIRAVEN
//