ID A0A1E5SL94_9BACT Unreviewed; 251 AA.
AC A0A1E5SL94;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Alpha-acetolactate decarboxylase {ECO:0000256|ARBA:ARBA00020164};
DE EC=4.1.1.5 {ECO:0000256|ARBA:ARBA00013204};
GN ORFNames=BFP71_10120 {ECO:0000313|EMBL:OEJ99894.1};
OS Roseivirga misakiensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Roseivirgaceae;
OC Roseivirga.
OX NCBI_TaxID=1563681 {ECO:0000313|EMBL:OEJ99894.1, ECO:0000313|Proteomes:UP000095552};
RN [1] {ECO:0000313|EMBL:OEJ99894.1, ECO:0000313|Proteomes:UP000095552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK-8 {ECO:0000313|EMBL:OEJ99894.1,
RC ECO:0000313|Proteomes:UP000095552};
RA Wong S.-K., Hamasaki K., Yoshizawa S.;
RT "Draft genome of Fabibacter sp. strain SK-8.";
RL Submitted (AUG-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 -!- 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}.
CC -!- SIMILARITY: Belongs to the alpha-acetolactate decarboxylase family.
CC {ECO:0000256|ARBA:ARBA00007106}.
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:OEJ99894.1}.
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DR EMBL; MDGQ01000005; OEJ99894.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E5SL94; -.
DR STRING; 1563681.BFP71_10120; -.
DR UniPathway; UPA00626; UER00678.
DR Proteomes; UP000095552; Unassembled WGS sequence.
DR GO; GO:0047605; F:acetolactate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0045151; P:acetoin biosynthetic process; IEA:UniProtKB-KW.
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 SUPFAM; SSF117856; AF0104/ALDC/Ptd012-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Acetoin biosynthesis {ECO:0000256|ARBA:ARBA00023061};
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Reference proteome {ECO:0000313|Proteomes:UP000095552};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..251
FT /note="Alpha-acetolactate decarboxylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009185126"
SQ SEQUENCE 251 AA; 28017 MW; ACCE92F1E79F8F99 CRC64;
MVRACSAKTK AYVVFFSLLA TALTSCQVTQ EQKDTRETET YADVQIVGAM RNVMWNGELN
GNINLDTISN KTGLFGLGPV SYLQGELLIN NGKSYVSTVT SDSTMIVEST FNTSAPFLVY
TNVNEWDEIA LPNGIKSIQA LETFIDKNTA DYKRPFAFKV SGRVSSAKIH IQNLPEGTKV
SSPAEAHQGQ TNYHIENKEV EIIGFFSTDH KGVFTHHDTF LHMHLITKEE DKMGHLDELE
IGEMKLYLPK K
//