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Database: UniProt
Entry: B8NL85_ASPFN
LinkDB: B8NL85_ASPFN
Original site: B8NL85_ASPFN 
ID   B8NL85_ASPFN            Unreviewed;       376 AA.
AC   B8NL85;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 82.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|RuleBase:RU364074};
DE            EC=1.2.4.1 {ECO:0000256|RuleBase:RU364074};
GN   ORFNames=AFLA_089210 {ECO:0000313|EMBL:EED48841.1}, G4B84_008251
GN   {ECO:0000313|EMBL:QMW32820.1};
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:EED48841.1, ECO:0000313|Proteomes:UP000001875};
RN   [1] {ECO:0000313|EMBL:EED48841.1, 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:EED48841.1};
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:QMW32820.1, ECO:0000313|Proteomes:UP000515286}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL3357 {ECO:0000313|EMBL:QMW32820.1,
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   -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC       conversion of pyruvate to acetyl-CoA and CO2.
CC       {ECO:0000256|RuleBase:RU364074}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC         acetyltransferase] + pyruvate = CO2 + N(6)-[(R)-S(8)-
CC         acetyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC         acetyltransferase]; Xref=Rhea:RHEA:19189, Rhea:RHEA-COMP:10480,
CC         Rhea:RHEA-COMP:10481, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:83099, ChEBI:CHEBI:83111; EC=1.2.4.1;
CC         Evidence={ECO:0000256|RuleBase:RU364074};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964,
CC         ECO:0000256|RuleBase:RU364074};
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DR   EMBL; EQ963480; EED48841.1; -; Genomic_DNA.
DR   EMBL; CP059870; QMW32820.1; -; Genomic_DNA.
DR   RefSeq; XP_002380742.1; XM_002380701.1.
DR   AlphaFoldDB; B8NL85; -.
DR   STRING; 332952.B8NL85; -.
DR   EnsemblFungi; EED48841; EED48841; AFLA_089210.
DR   VEuPathDB; FungiDB:AFLA_009132; -.
DR   eggNOG; KOG0524; Eukaryota.
DR   HOGENOM; CLU_012907_1_1_1; -.
DR   OMA; SRMRHHC; -.
DR   OrthoDB; 5473567at2759; -.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
DR   Proteomes; UP000515286; Chromosome 5.
DR   GO; GO:0042645; C:mitochondrial nucleoid; IEA:EnsemblFungi.
DR   GO; GO:0005967; C:mitochondrial pyruvate dehydrogenase complex; IEA:EnsemblFungi.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:EnsemblFungi.
DR   CDD; cd07036; TPP_PYR_E1-PDHc-beta_like; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR027110; PDHB.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR033248; Transketolase_C.
DR   PANTHER; PTHR11624; DEHYDROGENASE RELATED; 1.
DR   PANTHER; PTHR11624:SF96; PYRUVATE DEHYDROGENASE E1 COMPONENT SUBUNIT BETA, MITOCHONDRIAL; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|RuleBase:RU364074};
KW   Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000256|RuleBase:RU364074};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU364074}.
FT   DOMAIN          50..225
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   376 AA;  40403 MW;  1EDD3CF9D37EFD86 CRC64;
     MAAPRLFRPA ARLLSSRLSA PRRPAFPQSA CAPSILRSRG YATEGGAKEV TVRDALNEAL
     AEELETNPKT FILGEEVAQY NGAYKVTRGL LDRFGPKRVI DTPITEAGFC GLAVGAALAG
     LHPICEFMTF NFAMQAIDQI INSAAKTHYM SGGIQPCNVT FRGPNGFAAG VAAQHSQDYS
     AWYGSIPGLK VVSPWSSEDA KGLLKAAIRD PNPVVVLENE LLYGQAFPMS EAAQKDDFVL
     PIGKAKIERP GKDLTIVSLS RCVGLSLNAA AELKEKYGVD AEVINLRSVK PLDVETIVQS
     LKKTGRIMCV ESGFPMFGVS SEILALAMEY GFDYLTAPAV RVTGAEVPTP YAVGLEQMSF
     PQVDTILSQA TKLLRL
//
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