ID M2SX30_COCSN Unreviewed; 503 AA.
AC M2SX30;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=COCSADRAFT_95933 {ECO:0000313|EMBL:EMD61392.1};
OS Cochliobolus sativus (strain ND90Pr / ATCC 201652) (Common root rot and
OS spot blotch fungus) (Bipolaris sorokiniana).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=665912 {ECO:0000313|EMBL:EMD61392.1, ECO:0000313|Proteomes:UP000016934};
RN [1] {ECO:0000313|EMBL:EMD61392.1, ECO:0000313|Proteomes:UP000016934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ND90Pr / ATCC 201652 {ECO:0000313|Proteomes:UP000016934};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
RN [2] {ECO:0000313|Proteomes:UP000016934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ND90Pr / ATCC 201652 {ECO:0000313|Proteomes:UP000016934};
RX PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite, and effector coding
RT capacity across Cochliobolus pathogens.";
RL PLoS Genet. 9:E1003233-E1003233(2013).
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; KB445648; EMD61392.1; -; Genomic_DNA.
DR RefSeq; XP_007702753.1; XM_007704563.1.
DR AlphaFoldDB; M2SX30; -.
DR STRING; 665912.M2SX30; -.
DR GeneID; 19141646; -.
DR KEGG; bsc:COCSADRAFT_95933; -.
DR eggNOG; KOG0558; Eukaryota.
DR HOGENOM; CLU_016733_10_0_1; -.
DR OMA; TIPHFTY; -.
DR OrthoDB; 1399at2759; -.
DR Proteomes; UP000016934; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0043754; F:dihydrolipoyllysine-residue (2-methylpropanoyl)transferase activity; IEA:RHEA.
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; IPR003016; 2-oxoA_DH_lipoyl-BS.
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; PS00189; LIPOYL; 1.
DR PROSITE; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003423};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Reference proteome {ECO:0000313|Proteomes:UP000016934};
KW Transferase {ECO:0000256|RuleBase:RU003423};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 49..125
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 206..243
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 138..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 245..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 503 AA; 54438 MW; 207C3E4CB4D186F3 CRC64;
MKSFASREAS RLFSRSNLAQ RASIAGRRSA NIRVHEQRRG FRETRGLLVV KPYLLADIGE
GITECQVIQW FVKPGARVEQ FDPICEVQSD KASVEITSRF DGVIKKLYYE PDDMAKVGKP
LVDIDIQSEI SAADEALLNG GSGERPKDEP SRATEAQEQG IEVDRNDTKA ATGHIPKSDQ
SAALAPGSSQ AAALPTPRQP GKYASLATPA VRHMIKEHKL TIEDIQGTGK EGRVLKEDVQ
RHIESAKQTA SAPRATTTPT PVPTQQLEDQ IKPLTPVQSG MFKQMTKSLS IPHFLYTDSV
DFSSLTSLRK KYNAGREKAD RITPLPVIIK AVSLAFQQFP LLNSHLDTSA NPDKPQMILK
GSHNIGVAVD SPSGLLVPVI KNVQNHSIAS LAQEIQRLSS LARSGKLTSA DLTGATFTVS
NIGSIGGGTV APVIVGPQVG ILGIGKARVV PAFGENGELM KREECVFSWS ADHRVVDGAY
VARAAEEVRK CIEGVESMLV RMK
//
