ID   ALDC_BREBE              Reviewed;         285 AA.
AC   P23616;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Alpha-acetolactate decarboxylase;
DE            Short=ALDC;
DE            EC=4.1.1.5;
DE   Flags: Precursor;
GN   Name=aldB;
OS   Brevibacillus brevis (Bacillus brevis).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX   NCBI_TaxID=1393;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=ATCC 11031 / LMG 17054 / NRS 799;
RX   PubMed=2198252; DOI=10.1128/jb.172.8.4315-4321.1990;
RA   Diderichsen B., Wedsted U., Hedegaard L., Jensen B.R., Sjoeholm C.;
RT   "Cloning of aldB, which encodes alpha-acetolactate decarboxylase, an
RT   exoenzyme from Bacillus brevis.";
RL   J. Bacteriol. 172:4315-4321(1990).
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   PIR; A37757; A37757.
DR   RefSeq; WP_064202791.1; NZ_LVYG01000024.1.
DR   PDB; 4BT2; X-ray; 1.10 A; A=29-285.
DR   PDB; 4BT3; X-ray; 1.10 A; A=29-285.
DR   PDB; 4BT4; X-ray; 1.60 A; A=29-285.
DR   PDB; 4BT5; X-ray; 1.10 A; A=29-285.
DR   PDB; 4BT6; X-ray; 1.60 A; A=29-285.
DR   PDB; 4BT7; X-ray; 1.10 A; A=29-285.
DR   PDBsum; 4BT2; -.
DR   PDBsum; 4BT3; -.
DR   PDBsum; 4BT4; -.
DR   PDBsum; 4BT5; -.
DR   PDBsum; 4BT6; -.
DR   PDBsum; 4BT7; -.
DR   AlphaFoldDB; P23616; -.
DR   SMR; P23616; -.
DR   BRENDA; 4.1.1.5; 638.
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;
KW   Direct protein sequencing; Lyase; Signal.
FT   SIGNAL          1..25
FT   CHAIN           26..285
FT                   /note="Alpha-acetolactate decarboxylase"
FT                   /id="PRO_0000001109"
FT   VARIANT         26..28
FT                   /note="Missing (in some forms)"
FT   STRAND          53..57
FT                   /evidence="ECO:0007829|PDB:4BT2"
FT   HELIX           59..63
FT                   /evidence="ECO:0007829|PDB:4BT2"
FT   HELIX           73..76
FT                   /evidence="ECO:0007829|PDB:4BT2"
FT   HELIX           77..79
FT                   /evidence="ECO:0007829|PDB:4BT2"
FT   STRAND          81..85
FT                   /evidence="ECO:0007829|PDB:4BT2"
FT   HELIX           88..90
FT                   /evidence="ECO:0007829|PDB:4BT2"
FT   STRAND          92..97
FT                   /evidence="ECO:0007829|PDB:4BT2"
FT   STRAND          100..104
FT                   /evidence="ECO:0007829|PDB:4BT2"
FT   STRAND          110..112
FT                   /evidence="ECO:0007829|PDB:4BT2"
FT   STRAND          118..124
FT                   /evidence="ECO:0007829|PDB:4BT2"
FT   STRAND          130..138
FT                   /evidence="ECO:0007829|PDB:4BT2"
FT   HELIX           141..152
FT                   /evidence="ECO:0007829|PDB:4BT2"
FT   STRAND          157..174
FT                   /evidence="ECO:0007829|PDB:4BT2"
FT   HELIX           185..189
FT                   /evidence="ECO:0007829|PDB:4BT2"
FT   STRAND          193..209
FT                   /evidence="ECO:0007829|PDB:4BT2"
FT   HELIX           211..213
FT                   /evidence="ECO:0007829|PDB:4BT2"
FT   TURN            214..216
FT                   /evidence="ECO:0007829|PDB:4BT2"
FT   STRAND          219..227
FT                   /evidence="ECO:0007829|PDB:4BT2"
FT   STRAND          233..251
FT                   /evidence="ECO:0007829|PDB:4BT2"
FT   STRAND          254..257
FT                   /evidence="ECO:0007829|PDB:4BT2"
FT   HELIX           262..266
FT                   /evidence="ECO:0007829|PDB:4BT2"
FT   HELIX           269..271
FT                   /evidence="ECO:0007829|PDB:4BT3"
FT   HELIX           274..281
FT                   /evidence="ECO:0007829|PDB:4BT2"
SQ   SEQUENCE   285 AA;  31586 MW;  50151D9B909C0400 CRC64;
     MKKNIITSIT SLALVAGLSL TAFAATTATV PAPPAKQESK PAVAANPAPK NVLFQYSTIN
     ALMLGQFEGD LTLKDLKLRG DMGLGTINDL DGEMIQMGTK FYQIDSTGKL SELPESVKTP
     FAVTTHFEPK EKTTLTNVQD YNQLTKMLEE KFENKNVFYA VKLTGTFKMV KARTVPKQTR
     PYPQLTEVTK KQSEFEFKNV KGTLIGFYTP NYAAALNVPG FHLHFITEDK TSGGHVLNLQ
     FDNANLEISP IHEFDVQLPH TDDFAHSDLT QVTTSQVHQA ESERK