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Database: UniProt/TrEMBL
Entry: B4FD17_MAIZE
LinkDB: B4FD17_MAIZE
Original site: B4FD17_MAIZE 
ID   B4FD17_MAIZE            Unreviewed;       457 AA.
AC   B4FD17;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   24-JAN-2024, entry version 79.
DE   RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE            EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN   Name=100192900 {ECO:0000313|EnsemblPlants:Zm00001eb138800_P001};
GN   ORFNames=ZEAMMB73_Zm00001d041839 {ECO:0000313|EMBL:ONM33805.1};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577 {ECO:0000313|EMBL:ACF80010.1};
RN   [1] {ECO:0000313|EMBL:ACF80010.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=B73 {ECO:0000313|EMBL:ACF80010.1};
RX   PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA   Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA   Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA   Walbot V., Yu Y.;
RT   "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL   PLoS Genet. 5:E1000740-E1000740(2009).
RN   [2] {ECO:0000313|EMBL:ONM33805.1, ECO:0000313|Proteomes:UP000007305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb138800_P001,
RC   ECO:0000313|Proteomes:UP000007305};
RC   TISSUE=Seedling {ECO:0000313|EMBL:ONM33805.1};
RG   Maize Genome Sequencing Project;
RA   Ware D.;
RT   "Update maize B73 reference genome by single molecule sequencing
RT   technologies.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblPlants:Zm00001eb138800_P001}
RP   IDENTIFICATION.
RC   STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb138800_P001};
RG   EnsemblPlants;
RL   Submitted (MAY-2021) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={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; BT035005; ACF80010.1; -; mRNA.
DR   EMBL; CM007649; ONM33805.1; -; Genomic_DNA.
DR   RefSeq; NP_001131559.1; NM_001138087.1.
DR   AlphaFoldDB; B4FD17; -.
DR   EnsemblPlants; Zm00001eb138800_T001; Zm00001eb138800_P001; Zm00001eb138800.
DR   EnsemblPlants; Zm00001eb138800_T002; Zm00001eb138800_P002; Zm00001eb138800.
DR   GeneID; 100192900; -.
DR   Gramene; Zm00001eb138800_T001; Zm00001eb138800_P001; Zm00001eb138800.
DR   Gramene; Zm00001eb138800_T002; Zm00001eb138800_P002; Zm00001eb138800.
DR   KEGG; zma:100192900; -.
DR   OrthoDB; 1399at2759; -.
DR   Proteomes; UP000007305; Chromosome 3.
DR   ExpressionAtlas; B4FD17; baseline and differential.
DR   GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:UniProt.
DR   GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
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; IPR045257; E2/Pdx1.
DR   InterPro; IPR036625; E3-bd_dom_sf.
DR   InterPro; IPR004167; PSBD.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR23151; DIHYDROLIPOAMIDE ACETYL/SUCCINYL-TRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR23151:SF75; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT 5 OF PYRUVATE DEHYDROGENASE COMPLEX, CHLOROPLASTIC; 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   1: Evidence at protein level;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003423};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:B4FD17};
KW   Pyruvate {ECO:0000313|EMBL:ONM33805.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007305};
KW   Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:ONM33805.1};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          40..115
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          124..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        124..146
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        147..168
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   457 AA;  47879 MW;  595DC014EF3DD2E1 CRC64;
     MAGLLHLQST LLPSASALRR RAGVPVPSSS RRRCRIEAKI REIFMPALSS TMTEGKIVSW
     TAAEGDRLAK GDPVVVVESD KADMDVETFY DGFLAAVLVP AGDSAPVGSA IALLAESEED
     IPVAQSQAAS FSSTSPLPSP PQETAAQEAS PSPPPPPPPG PVSVSAPTPP LPATQGERVV
     ASPYAKKLAK DLGVDLFSVT GSGPCGRIVA KDVEAALAAP KKAAPVTAPR PDVPLGSTVP
     FTTMQGAVSK NMVESLAIPT FRVGYTITTD ALDQLYKKIK SKGVTMTALL AKATAMALVQ
     HPVVNSSCRD GKSFTYSSSI NIAVAVAIDG GLITPVLQDA DKLDIYSLSR KWKELVDKAR
     AKQLQPHEYN SGTFTLSNLG MFGVDRFDAI LPPGTGAIMA VGASEPTIVG TKDGRIGIKN
     QMQVNVTADH RVIYGADLAA FLQTLAKIIE DPKDLTF
//
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