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Database: UniProt
Entry: A0A1E5SL94_9BACT
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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
//
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