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Database: UniProt
Entry: A0A1H7T3Y8_9FIRM
LinkDB: A0A1H7T3Y8_9FIRM
Original site: A0A1H7T3Y8_9FIRM 
ID   A0A1H7T3Y8_9FIRM        Unreviewed;       237 AA.
AC   A0A1H7T3Y8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Alpha-acetolactate decarboxylase {ECO:0000256|ARBA:ARBA00020164, ECO:0000256|PIRNR:PIRNR001332};
DE            EC=4.1.1.5 {ECO:0000256|ARBA:ARBA00013204, ECO:0000256|PIRNR:PIRNR001332};
GN   ORFNames=SAMN04487770_11790 {ECO:0000313|EMBL:SEL79448.1};
OS   Butyrivibrio sp. ob235.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Butyrivibrio.
OX   NCBI_TaxID=1761780 {ECO:0000313|EMBL:SEL79448.1, ECO:0000313|Proteomes:UP000199418};
RN   [1] {ECO:0000313|EMBL:SEL79448.1, ECO:0000313|Proteomes:UP000199418}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OB235 {ECO:0000313|EMBL:SEL79448.1,
RC   ECO:0000313|Proteomes:UP000199418};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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         Evidence={ECO:0000256|ARBA:ARBA00001784,
CC         ECO:0000256|PIRNR:PIRNR001332};
CC   -!- PATHWAY: Polyol metabolism; (R,R)-butane-2,3-diol biosynthesis; (R,R)-
CC       butane-2,3-diol from pyruvate: step 2/3.
CC       {ECO:0000256|ARBA:ARBA00005170, ECO:0000256|PIRNR:PIRNR001332}.
CC   -!- SIMILARITY: Belongs to the alpha-acetolactate decarboxylase family.
CC       {ECO:0000256|ARBA:ARBA00007106, ECO:0000256|PIRNR:PIRNR001332}.
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DR   EMBL; FOBE01000017; SEL79448.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H7T3Y8; -.
DR   OrthoDB; 8612680at2; -.
DR   UniPathway; UPA00626; UER00678.
DR   Proteomes; UP000199418; Unassembled WGS sequence.
DR   GO; GO:0047605; F:acetolactate decarboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0045151; P:acetoin biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd17299; acetolactate_decarboxylase; 1.
DR   InterPro; IPR005128; Acetolactate_a_deCO2ase.
DR   PANTHER; PTHR35524; ALPHA-ACETOLACTATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR35524:SF1; ALPHA-ACETOLACTATE DECARBOXYLASE; 1.
DR   Pfam; PF03306; AAL_decarboxy; 1.
DR   PIRSF; PIRSF001332; Acetolac_decarb; 1.
DR   SUPFAM; SSF117856; AF0104/ALDC/Ptd012-like; 1.
PE   3: Inferred from homology;
KW   Acetoin biosynthesis {ECO:0000256|ARBA:ARBA00023061,
KW   ECO:0000256|PIRNR:PIRNR001332};
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793,
KW   ECO:0000256|PIRNR:PIRNR001332};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001332};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199418}.
SQ   SEQUENCE   237 AA;  26747 MW;  0088E05C0BA22798 CRC64;
     MENTMYQVST LQALILGYSR TVINVDELIQ HGDTGLGTFE DVNGEMIVMD GHCYRSDQFG
     NVTEVDPSTG IPFAAVARLY GNQQFQLNDM PNFASIQTEL TRKIEEVFGL NSMHIVRIDG
     EFGKIDARSE GPYRSHHIRL KEILLHTQQS FLFENIRGSL VGVYFPDYMD GINMPGWHLH
     FLSEDRTKGG HVFDASIIKG AARVDKITSI HINLPKEASF DTYSLKEDLE SEIKSVE
//
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