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Database: UniProt
Entry: B8NT51_ASPFN
LinkDB: B8NT51_ASPFN
Original site: B8NT51_ASPFN 
ID   B8NT51_ASPFN            Unreviewed;       604 AA.
AC   B8NT51;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   SubName: Full=Acetolactate synthase, putative {ECO:0000313|EMBL:EED47279.1};
GN   ORFNames=AFLA_053340 {ECO:0000313|EMBL:EED47279.1}, G4B84_000110
GN   {ECO:0000313|EMBL:QMW24865.1};
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952 {ECO:0000313|EMBL:EED47279.1, ECO:0000313|Proteomes:UP000001875};
RN   [1] {ECO:0000313|EMBL:EED47279.1, ECO:0000313|Proteomes:UP000001875}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 /
RC   SRRC 167 {ECO:0000313|Proteomes:UP000001875}, and NRRL3357
RC   {ECO:0000313|EMBL:EED47279.1};
RX   PubMed=25883274; DOI=10.1128/genomeA.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
RN   [2] {ECO:0000313|EMBL:QMW24865.1, ECO:0000313|Proteomes:UP000515286}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL3357 {ECO:0000313|EMBL:QMW24865.1,
RC   ECO:0000313|Proteomes:UP000515286};
RA   Fountain J.C., Clevenger J.P., Nadon B., Youngblood R.C., Korani W.,
RA   Chang P.-K., Starr D., Wang H., Isett B., Johnston H.R., Wiggins R.,
RA   Chu Y., Agarwal G., Kemerait R.C., Pandey M.K., Bhatnagar D.,
RA   Ozias-Akins P., Varshney R.K., Scheffler B.E., Vaughn J.N., Guo B.;
RT   "Two New Chromosome-Level Aspergillus flavus Reference Genomes Reveal a
RT   Large Insertion Potentially Contributing to Isolate Stress Tolerance and
RT   Aflatoxin Production.";
RL   Submitted (JUL-2020) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; EQ963483; EED47279.1; -; Genomic_DNA.
DR   EMBL; CP059866; QMW24865.1; -; Genomic_DNA.
DR   RefSeq; XP_002383459.1; XM_002383418.1.
DR   AlphaFoldDB; B8NT51; -.
DR   SMR; B8NT51; -.
DR   STRING; 332952.B8NT51; -.
DR   EnsemblFungi; EED47279; EED47279; AFLA_053340.
DR   VEuPathDB; FungiDB:AFLA_011235; -.
DR   eggNOG; KOG1185; Eukaryota.
DR   HOGENOM; CLU_013748_4_0_1; -.
DR   OMA; VPWIPRR; -.
DR   OrthoDB; 1948175at2759; -.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
DR   Proteomes; UP000515286; Chromosome 1.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004737; F:pyruvate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   CDD; cd02002; TPP_BFDC; 1.
DR   CDD; cd07035; TPP_PYR_POX_like; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   InterPro; IPR045229; TPP_enz.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   PANTHER; PTHR18968:SF164; PYRUVATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   Pfam; PF00205; TPP_enzyme_M; 1.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE   3: Inferred from homology;
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          12..142
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          220..327
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          424..601
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   604 AA;  64906 MW;  36AA95E1C3044223 CRC64;
     MADESTVGSP IVADAFLEAL AEAGVDYLFT VLGSDHPSII EAYIRRQNDP TRQYPKMILF
     QHEFVAMSAA DGYARISHKP ACVIAHVDVG TAALGQGLHN ASSGRAPVVV FAGVAPSTLL
     GEAPGSRSEH VQWYQDIRDQ AALVAPYSRF SAEIKSPHNV GSLVHRAVLM ATTGSPGPVY
     LTATREILAT PIPSVEPRPK PVPSCHLGSL SPEAVEMIGN ALLEAKAPLV ITGYLGRSHR
     AVQQLITLAD TVQGLRVFDS ELREVCFPAT HPACLTRSTG AAPAIQSADV ILVLDADVPW
     IPRRVHPSPS AEIYHIDLDP RKERMNMFDI GASATFHADT TSALTQLNAY ITSSPRLPAL
     QEAWTSRGQD LLTAHKEGKA RIDSRATAPL STPNEPCTVD YLCSRIRASV PQDTIYITDS
     VTNQVPMTEQ LQLTRPGSHL TKGGSGLGWS GGAAIGASLA TARYDISDRP NLHLNETTKT
     PFICNIIGDG SFVFSVPTAV YWAAHRYQTP FLTVILNNGG WNATRQCLAD VHPSGVAAGL
     SNRDLGISLV EDGPDYGEVA KAAANGNLWT KRVRSVRELD VVLREGIRVV VEERKSVVLD
     VVIR
//
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