ID A0A2I0MDV3_COLLI Unreviewed; 520 AA.
AC A0A2I0MDV3;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=DBT {ECO:0000313|EMBL:PKK27859.1};
GN ORFNames=A306_00005757 {ECO:0000313|EMBL:PKK27859.1};
OS Columba livia (Rock dove).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
OX NCBI_TaxID=8932 {ECO:0000313|EMBL:PKK27859.1, ECO:0000313|Proteomes:UP000053872};
RN [1] {ECO:0000313|EMBL:PKK27859.1, ECO:0000313|Proteomes:UP000053872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Blood {ECO:0000313|EMBL:PKK27859.1};
RX PubMed=23371554; DOI=10.1126/science.1230422;
RA Shapiro M.D., Kronenberg Z., Li C., Domyan E.T., Pan H., Campbell M.,
RA Tan H., Huff C.D., Hu H., Vickrey A.I., Nielsen S.C., Stringham S.A.,
RA Hu H., Willerslev E., Gilbert M.T., Yandell M., Zhang G., Wang J.;
RT "Genomic diversity and evolution of the head crest in the rock pigeon.";
RL Science 339:1063-1067(2013).
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|ARBA:ARBA00001938,
CC 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PKK27859.1}.
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DR EMBL; AKCR02000018; PKK27859.1; -; Genomic_DNA.
DR RefSeq; XP_005499046.1; XM_005498989.1.
DR AlphaFoldDB; A0A2I0MDV3; -.
DR STRING; 8932.A0A2I0MDV3; -.
DR InParanoid; A0A2I0MDV3; -.
DR Proteomes; UP000053872; Unassembled WGS sequence.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0043754; F:dihydrolipoyllysine-residue (2-methylpropanoyl)transferase activity; IEA:RHEA.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
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:UP000053872};
KW Transferase {ECO:0000256|RuleBase:RU003423};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 93..168
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 203..240
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 175..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 520 AA; 57229 MW; 690A17FA8AFB57F6 CRC64;
MPLAGVSTVA CFHKNLYKLE TVASEILNEL YVPQSIILTL ETFLSQVCIH RVRSCSSIRF
IKSKYVCVFD KSTLKFSHQQ RLFRTSAVSC GQIVQFKLAD IGEGITEVTV KEWYVKEGDS
VSQFDSICEV QSDKASVTIT SRYDGIIRKL HYNVDETAYV GKPLVDIETD ASKDVAPEED
VVETPPMSHE EHTHQEIKGH KTLATPAVRR LAMENNIKLS EVIGTGKDNR ILKEDILNYL
AKQTGAILPP SPKAEIIPPL PKSETVPAAP KDKAHKIPVS RPIVFSGKDK TEPITGFQKA
MVKTMSAALK IPHFGYCDEI DLTQLVQLRE ELKPLAQLRG VKLSFMPFFI KAASLGLLQY
PILNASLDES CQNVTYKASH NIGVAMDTEQ GLIVPNVKNV QVCSVFEIAS ELNRLQSLGS
AGQLGTNDLT GGTFTLSNIG TIGGTYAKPV ILPPEVAIGA LGKIQLLPRF NGKGEVFKAQ
IMNVSWSADH RIIDGATMAR FSNLWKSYLE NPASMLLDLK
//
