ID A0A224X813_9LACT Unreviewed; 236 AA.
AC A0A224X813;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=RsY01_1070 {ECO:0000313|EMBL:GAX47470.1};
OS Lactococcus reticulitermitis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=2025039 {ECO:0000313|EMBL:GAX47470.1, ECO:0000313|Proteomes:UP000218689};
RN [1] {ECO:0000313|Proteomes:UP000218689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rs-Y01 {ECO:0000313|Proteomes:UP000218689};
RA Ohkuma M., Yuki M.;
RT "Draft genome sequence of Lactococcus sp. strain Rs-Y01, isolated from the
RT gut of the lower termite Reticulitermes speratus.";
RL Submitted (AUG-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAX47470.1}.
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DR EMBL; BEDT01000002; GAX47470.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A224X813; -.
DR OrthoDB; 8612680at2; -.
DR UniPathway; UPA00626; UER00678.
DR Proteomes; UP000218689; 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 NCBIfam; TIGR01252; acetolac_decarb; 1.
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:UP000218689}.
SQ SEQUENCE 236 AA; 26539 MW; 86A8626A8E6E0CC2 CRC64;
MSEPIKLFQY NTLSALMSGL FEGSLTIGEL LEQGDLGIGT LDEIDGELIV LDGKAYQARG
DKTITEVSPE VKVPYAAVVF HHAEVIFKQR FEVTNDELQT RIETYYDGAN LFRSIKIHGT
FSKMHVRMIP KAKEGARFAD VATRQSEYTV DNVTGTIVGI WTPEMFHGVS VAGYHLHFIT
DDHTFGGHVM DYVMSEGIVE VGAVDQLDQR FPVQDRKYLF AKLNLDELKE DIEKSE
//
