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Database: UniProt
Entry: A0A2H3IEV8_9EURO
LinkDB: A0A2H3IEV8_9EURO
Original site: A0A2H3IEV8_9EURO 
ID   A0A2H3IEV8_9EURO        Unreviewed;       239 AA.
AC   A0A2H3IEV8;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   RecName: Full=Alpha-acetolactate decarboxylase {ECO:0000256|ARBA:ARBA00020164};
DE            EC=4.1.1.5 {ECO:0000256|ARBA:ARBA00013204};
GN   ORFNames=PENO1_043350 {ECO:0000313|EMBL:PCH01412.1};
OS   Penicillium occitanis (nom. inval.).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=290292 {ECO:0000313|EMBL:PCH01412.1, ECO:0000313|Proteomes:UP000218381};
RN   [1] {ECO:0000313|EMBL:PCH01412.1, ECO:0000313|Proteomes:UP000218381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CL100 {ECO:0000313|EMBL:PCH01412.1,
RC   ECO:0000313|Proteomes:UP000218381};
RX   PubMed=28951729; DOI=10.3389/fmicb.2017.01627;
RA   Bravo-Ruiz G., Sassi A.H., Marcet-Houben M., Di Pietro A., Gargouri A.,
RA   Gabaldon T., Roncero M.I.G.;
RT   "Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium
RT   occitanis and Functional Analysis of a Candidate Gene in the Plant Pathogen
RT   Fusarium oxysporum.";
RL   Front. Microbiol. 8:1627-1627(2017).
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:PCH01412.1}.
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DR   EMBL; NPFK01000101; PCH01412.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H3IEV8; -.
DR   STRING; 290292.A0A2H3IEV8; -.
DR   OrthoDB; 2583430at2759; -.
DR   UniPathway; UPA00626; UER00678.
DR   Proteomes; UP000218381; 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   CDD; cd17299; acetolactate_decarboxylase; 1.
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   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   Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218381}.
SQ   SEQUENCE   239 AA;  26239 MW;  6C6B76DD2A482DE6 CRC64;
     MADRLYQYST ASALMAGVAS TGIPLSNLLK HGTHGLGTMS SINGEVVILD STTYHLQSSG
     AVRVVEAHEQ LPFAMVTSFN ACKTRTQSTF SDLPSKQSIL QYLQTLFHGI NNRFAFFLIP
     RIHLETITAR VVRGQQYPRQ PLSELGEAQK VNTYESVTGS IVGFWSPAYM DGVSVSGLHM
     HFLSEDRSYG GHVLEMRSAS KFELQAALLN EFDLELADNE EFGDAELGMG GEALRRVEG
//
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