ID A0A384A1R0_BALAS Unreviewed; 480 AA.
AC A0A384A1R0;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 03-MAY-2023, entry version 21.
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=PDHX {ECO:0000313|RefSeq:XP_007181124.1};
OS Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS (Balaenoptera davidsoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC Balaenopteridae; Balaenoptera.
OX NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_007181124.1};
RN [1] {ECO:0000313|RefSeq:XP_007181124.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_007181124.1};
RG RefSeq;
RL Submitted (JAN-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|RuleBase:RU003423};
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000256|ARBA:ARBA00004305}.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU003423}.
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DR RefSeq; XP_007181124.1; XM_007181062.2.
DR AlphaFoldDB; A0A384A1R0; -.
DR GeneID; 103012403; -.
DR CTD; 8050; -.
DR OrthoDB; 5483022at2759; -.
DR Proteomes; UP000261681; Unplaced.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
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:SF9; PYRUVATE DEHYDROGENASE PROTEIN X COMPONENT, 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 Pyruvate {ECO:0000313|RefSeq:XP_007181124.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000261681};
KW Transferase {ECO:0000256|RuleBase:RU003423};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 54..130
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 181..218
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 143..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 480 AA; 51909 MW; 2137DE50D1158699 CRC64;
MAASWRLGCD PRLLRCLLGF SRSPGLVKGA AGRSVGRGAS WRWFHSTKWL RADPITILMP
SLSPTMEEGN IVKWLKKEGE AVSTGDALCE IETDKAVVTL DASDDGILAK IVVAEGSKNI
RLGALIGLLV EEGEDWKHVE IPKDIGPSSP ASKPSVPCPS PEPQISTPVK KEHIPGKLQF
RLSPAARNIL EKHGLDANQG TATGPRGIFT KEDALKLVQL KQMSKITESR PTPALPTIPT
ASLPPQATAR PSYPRPMIPP VSTPGQPNVA GTFTEVPTSN IRRVIAKRLT ESKRTVPHAY
ATTDCDLGAV LKVRQNLVRD DIKVSVNDFI IKAAAVTLKQ MPSVNVSWDG ESPKQLPFID
ISVAVATDRG LITPVIKDAA AKGLPEIADS VKALSKKARD GKLLPEEYQG GSFSLVQDLQ
VSASCSCSRD PSSFHLVAPP SSKSLESSPY SRWIRKESKD LRMHGPHQTS WEGVNPERRT
//
