ID A0A2K9PUM2_9FLAO Unreviewed; 275 AA.
AC A0A2K9PUM2;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
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 Name=budA {ECO:0000313|EMBL:AUP80498.1};
GN ORFNames=C1H87_17980 {ECO:0000313|EMBL:AUP80498.1};
OS Flavivirga eckloniae.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavivirga.
OX NCBI_TaxID=1803846 {ECO:0000313|EMBL:AUP80498.1, ECO:0000313|Proteomes:UP000235826};
RN [1] {ECO:0000313|EMBL:AUP80498.1, ECO:0000313|Proteomes:UP000235826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ECD14 {ECO:0000313|EMBL:AUP80498.1,
RC ECO:0000313|Proteomes:UP000235826};
RA Lee J.H., Baik K.S., Seong C.N.;
RT "Complete genome sequence of Flavivirga eckloniae ECD14 isolated from
RT seaweed Ecklonia cava.";
RL Submitted (JAN-2018) 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; CP025791; AUP80498.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K9PUM2; -.
DR KEGG; fek:C1H87_17980; -.
DR OrthoDB; 8612680at2; -.
DR UniPathway; UPA00626; UER00678.
DR Proteomes; UP000235826; Chromosome.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000235826};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..275
FT /note="Alpha-acetolactate decarboxylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014947162"
SQ SEQUENCE 275 AA; 31183 MW; 7B09CF0CC35D2C22 CRC64;
MIPKKIPFLF TACALLMLFL SSACKQEQDV NVTSEPVVTE KPVVERDLFY HYSIWYAFVN
KVFEGDLTVS KLKTKGDIGL GSYTKLDGEL IMLDGVPYRA TEDGVVSIAD DADKIVYVNA
TFFDEDISFK VTDSINYDAL RGEINKHLPT KNMFYGFKIH GTFKNIKCGG LNKQEPPFKE
GLDVLIPNRP IFKAENIEGT MVGFYCPQFI GDINVAGYHL HFISDDKKFG GHVMAFNAVS
LDVSIDEMYE YQFVLPNTDA YRKVGFDKQF QYKKN
//
