ID B8N134_ASPFN Unreviewed; 476 AA.
AC B8N134;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 72.
DE RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN ORFNames=AFLA_028090 {ECO:0000313|EMBL:EED55537.1}, G4B84_003683
GN {ECO:0000313|EMBL:QMW28394.1};
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:EED55537.1, ECO:0000313|Proteomes:UP000001875};
RN [1] {ECO:0000313|EMBL:EED55537.1, 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:EED55537.1};
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:QMW28394.1, ECO:0000313|Proteomes:UP000515286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL3357 {ECO:0000313|EMBL:QMW28394.1,
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 -!- CATALYTIC ACTIVITY:
CC Reaction=2-methylpropanoyl-CoA + N(6)-[(R)-dihydrolipoyl]-L-lysyl-
CC [protein] = CoA + N(6)-[(R)-S(8)-2-methylpropanoyldihydrolipoyl]-L-
CC lysyl-[protein]; Xref=Rhea:RHEA:18865, Rhea:RHEA-COMP:10475,
CC Rhea:RHEA-COMP:10497, ChEBI:CHEBI:57287, ChEBI:CHEBI:57338,
CC ChEBI:CHEBI:83100, ChEBI:CHEBI:83142; EC=2.3.1.168;
CC Evidence={ECO:0000256|ARBA:ARBA00035973};
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|ARBA:ARBA00001938,
CC ECO:0000256|RuleBase:RU003423};
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU003423}.
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DR EMBL; EQ963473; EED55537.1; -; Genomic_DNA.
DR EMBL; CP059867; QMW28394.1; -; Genomic_DNA.
DR RefSeq; XP_002374319.1; XM_002374278.1.
DR AlphaFoldDB; B8N134; -.
DR STRING; 332952.B8N134; -.
DR EnsemblFungi; EED55537; EED55537; AFLA_028090.
DR VEuPathDB; FungiDB:AFLA_000660; -.
DR eggNOG; KOG0558; Eukaryota.
DR HOGENOM; CLU_016733_10_0_1; -.
DR OMA; PWVHRGE; -.
DR OrthoDB; 1399at2759; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
DR Proteomes; UP000515286; Chromosome 2.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR CDD; cd06849; lipoyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 4.10.320.10; E3-binding domain; 1.
DR InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR036625; E3-bd_dom_sf.
DR InterPro; IPR004167; PSBD.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR43178; DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR PANTHER; PTHR43178:SF5; LIPOAMIDE ACYLTRANSFERASE COMPONENT OF BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 1.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02817; E3_binding; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR SUPFAM; SSF47005; Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003423,
KW ECO:0000313|EMBL:EED55537.1}; Lipoyl {ECO:0000256|RuleBase:RU003423};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:EED55537.1}.
FT DOMAIN 47..123
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 180..217
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 126..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..147
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 476 AA; 51803 MW; CBCBC0DB5BFDEE81 CRC64;
MSILRCNGGL SWALRSCQSR RVLPITRSPS TISFPRRTFH AAPALWGVKS QILKDVGEGI
TEVQIIQWYV EEGAHIEEWK PLCQYQSDKA VDDITSRYEG IVKKLHFQAD DTVPTGRALC
DIEVEDGKYP EDNPPPEPAP APAQPSPAPA QAETKQPSVE VAATTQKPEA PKNGSRYATL
ATPAVRGMLK AHNVNILDIP GTGKDGRVLK EDVLRFVTVR DSAPTLQPTT PTIPTTPVSQ
QSDTAVNLTP IQSQMFKTMT RSLNIPHFLF ADELNINNIT ALRKKLANDP KDPRRITFLS
FVIKAVSLAL NEYPILNAKV DTSNPDKPQL IMRPRHNIGV AMDTPQGLIV PNVKDVANRS
IEDVAAEISR LSALGKEGKL TPADLSGGTI TVSNIGNIGG TYVAPVIVSN EVAILGVGKS
KTVPIFDEAG QVTKGELVNF SWSADHRVVD GATMARMANK VRECIESPEL MLLKLR
//