ID   ALDC_KLEAE              Reviewed;         260 AA.
AC   P05361; Q59340;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Alpha-acetolactate decarboxylase;
DE            EC=4.1.1.5;
GN   Name=budA; Synonyms=aldC;
OS   Klebsiella aerogenes (Enterobacter aerogenes).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=548;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3278689; DOI=10.1128/aem.54.1.38-42.1988;
RA   Sone H., Fujii T., Kondo K., Shimizu F., Tanaka J., Inoue T.;
RT   "Nucleotide sequence and expression of the Enterobacter aerogenes alpha-
RT   acetolactate decarboxylase gene in brewer's yeast.";
RL   Appl. Environ. Microbiol. 54:38-42(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8444801; DOI=10.1128/jb.175.5.1392-1404.1993;
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 excreted by
CC       the cells. This may be a mechanism for controlling the internal pH of
CC       cells in the stationary stage.
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; J03433; AAA24794.1; -; Genomic_DNA.
DR   EMBL; L04506; AAA56801.1; -; Genomic_DNA.
DR   PIR; A32515; A32515.
DR   PDB; 5YHO; X-ray; 2.40 A; A/B=23-260.
DR   PDB; 6J92; X-ray; 2.42 A; A/B=23-260.
DR   PDBsum; 5YHO; -.
DR   PDBsum; 6J92; -.
DR   AlphaFoldDB; P05361; -.
DR   SMR; P05361; -.
DR   STRING; 548.EAG7_01916; -.
DR   BioCyc; MetaCyc:MON-17721; -.
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   3D-structure; Acetoin biosynthesis; Decarboxylase; Lyase.
FT   CHAIN           1..260
FT                   /note="Alpha-acetolactate decarboxylase"
FT                   /id="PRO_0000218439"
FT   CONFLICT        24
FT                   /note="K -> Q (in Ref. 2; AAA56801)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        45..47
FT                   /note="EGD -> VGE (in Ref. 2; AAA56801)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        113..114
FT                   /note="DA -> NG (in Ref. 2; AAA56801)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        137..138
FT                   /note="AL -> V (in Ref. 2; AAA56801)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        257
FT                   /note="S -> A (in Ref. 2; AAA56801)"
FT                   /evidence="ECO:0000305"
FT   STRAND          30..34
FT                   /evidence="ECO:0007829|PDB:5YHO"
FT   HELIX           36..41
FT                   /evidence="ECO:0007829|PDB:5YHO"
FT   HELIX           50..54
FT                   /evidence="ECO:0007829|PDB:5YHO"
FT   STRAND          58..63
FT                   /evidence="ECO:0007829|PDB:5YHO"
FT   HELIX           65..67
FT                   /evidence="ECO:0007829|PDB:5YHO"
FT   STRAND          69..74
FT                   /evidence="ECO:0007829|PDB:5YHO"
FT   STRAND          77..81
FT                   /evidence="ECO:0007829|PDB:5YHO"
FT   STRAND          83..85
FT                   /evidence="ECO:0007829|PDB:5YHO"
FT   STRAND          87..89
FT                   /evidence="ECO:0007829|PDB:6J92"
FT   STRAND          95..101
FT                   /evidence="ECO:0007829|PDB:5YHO"
FT   STRAND          107..114
FT                   /evidence="ECO:0007829|PDB:5YHO"
FT   HELIX           118..128
FT                   /evidence="ECO:0007829|PDB:5YHO"
FT   STRAND          134..149
FT                   /evidence="ECO:0007829|PDB:5YHO"
FT   HELIX           162..164
FT                   /evidence="ECO:0007829|PDB:6J92"
FT   STRAND          172..186
FT                   /evidence="ECO:0007829|PDB:5YHO"
FT   HELIX           188..190
FT                   /evidence="ECO:0007829|PDB:5YHO"
FT   TURN            191..193
FT                   /evidence="ECO:0007829|PDB:6J92"
FT   STRAND          197..204
FT                   /evidence="ECO:0007829|PDB:5YHO"
FT   STRAND          210..228
FT                   /evidence="ECO:0007829|PDB:5YHO"
FT   STRAND          230..234
FT                   /evidence="ECO:0007829|PDB:5YHO"
FT   HELIX           239..242
FT                   /evidence="ECO:0007829|PDB:5YHO"
FT   HELIX           251..259
FT                   /evidence="ECO:0007829|PDB:5YHO"
SQ   SEQUENCE   260 AA;  29032 MW;  BDDC14B941E012F3 CRC64;
     MMMHSSACDC EASLCETLRG FSAKHPDSVI YQTSLMSALL SGVYEGDTTI ADLLAHGDFG
     LGTFNELDGE MIAFSSQVYQ LRADGSARAA KPEQKTPFAV MTWFQPQYRK TFDAPVSRQQ
     IHDVIDQQIP SDNLFCALRI DGNFRHAHTR TVPRQTPPYR AMTDVLDDQP VFRFNQREGV
     LVGFRTPQHM QGINVAGYHE HFITDDRQGG GHLLDYQLES GVLTFGEIHK LMIDLPADSA
     FLQANLHPSN LDAAIRSVEN