ID A0A178B6Q9_9PLEO Unreviewed; 212 AA.
AC A0A178B6Q9;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Alpha-acetolactate decarboxylase {ECO:0000256|ARBA:ARBA00020164};
DE EC=4.1.1.5 {ECO:0000256|ARBA:ARBA00013204};
GN ORFNames=IQ06DRAFT_290583 {ECO:0000313|EMBL:OAL04488.1};
OS Stagonospora sp. SRC1lsM3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX NCBI_TaxID=765868 {ECO:0000313|EMBL:OAL04488.1, ECO:0000313|Proteomes:UP000077206};
RN [1] {ECO:0000313|EMBL:OAL04488.1, ECO:0000313|Proteomes:UP000077206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAL04488.1,
RC ECO:0000313|Proteomes:UP000077206};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-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}.
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DR EMBL; KV441707; OAL04488.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178B6Q9; -.
DR STRING; 765868.A0A178B6Q9; -.
DR InParanoid; A0A178B6Q9; -.
DR OrthoDB; 1922432at2759; -.
DR UniPathway; UPA00626; UER00678.
DR Proteomes; UP000077206; 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; 2.
DR SUPFAM; SSF117856; AF0104/ALDC/Ptd012-like; 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:UP000077206}.
SQ SEQUENCE 212 AA; 23321 MW; CD9F3FC9A33A716B CRC64;
MVGSIPNDIF QFSTFAAHTA GFNTGQPRTA DLTGHGTDGI GIYEDGSLMI LLDRSAYSIR
KDGTIVPAPM NDRLPFAMVT IYQPTYRIKL PSLDFDGLEE LISSSELGPA KGINTLMPFK
ITATFAAVSL EQGGDYANIE GTIFGYVVPK WMREISGPRI HAHFLDEEEQ NGGKVEGFEI
EQDVTLGFAK CGRFHLGFPQ VPEWEDVRLS KN
//
