ID Q98UJ6_CHICK Unreviewed; 493 AA.
AC Q98UJ6;
DT 01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2001, sequence version 1.
DT 27-MAR-2024, entry version 141.
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|Ensembl:ENSGALP00010035287.1};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031 {ECO:0000313|EMBL:BAB32667.1};
RN [1] {ECO:0000313|EMBL:BAB32667.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Liver {ECO:0000313|EMBL:BAB32667.1};
RX PubMed=11168412; DOI=10.1046/j.1432-1327.2001.01925.x;
RA Ono K., Hakozaki M., Suzuki T., Mori T., Hata H., Kochi H.;
RT "cDNA cloning of the chicken branched-chain alpha-keto acid dehydrogenase
RT complex. Chicken-specific residues of the acyltransferase affect the
RT overall activity and the interaction with the dehydrogenase.";
RL Eur. J. Biochem. 268:727-736(2001).
RN [2] {ECO:0000313|Ensembl:ENSGALP00010035287.1}
RP IDENTIFICATION.
RC STRAIN=broiler {ECO:0000313|Ensembl:ENSGALP00010035287.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB035085; BAB32667.1; -; mRNA.
DR RefSeq; NP_989987.1; NM_204656.1.
DR Ensembl; ENSGALT00010058117.1; ENSGALP00010035287.1; ENSGALG00010023826.1.
DR GeneID; 395374; -.
DR KEGG; gga:395374; -.
DR CTD; 1629; -.
DR VEuPathDB; HostDB:geneid_395374; -.
DR GeneTree; ENSGT00940000156750; -.
DR OMA; MPFCIKA; -.
DR OrthoDB; 1399at2759; -.
DR PhylomeDB; Q98UJ6; -.
DR BRENDA; 2.3.1.168; 1306.
DR Proteomes; UP000000539; Chromosome 8.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW Acyltransferase {ECO:0000256|RuleBase:RU003423,
KW ECO:0000313|EMBL:BAB32667.1};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Proteomics identification {ECO:0007829|PeptideAtlas:Q98UJ6};
KW Reference proteome {ECO:0000313|Proteomes:UP000000539};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:BAB32667.1};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 64..139
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 174..211
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
SQ SEQUENCE 493 AA; 53998 MW; 196C1B38EA476F1F CRC64;
MAAVTTLRSS CRTAGRLVCV HHIRSCSSIR FIKSKYACVF DKSAFNFSHQ QRLFRTSAVS
HGQIVQFKLS DIGEGITEVT VKEWYIKEGD SVSQFDSICE VQSDKASVTI TSRYDGIIRK
LHYNLDEIAY VGKPLVDIEI DASKGVAPEE DVVETPAMSH EEHTHQEIKG HKTLATPAVR
RLAMENNIKL SEVIGTGKDN RILKEDILSF LAKQTGAILP PSPKAEIIAP LSKSETVPTA
PKDKARKIPI PISRPVVFSG KDKTEPITGF HKAMVKTMSA ALKIPHFGYC DEIDLTHLVQ
LREELKPLAQ SRGVKLSFMP FFIKAASLGL LQYPILNASL DEGCQNVTYK ASHNIGVAMD
TEQGLIVPNV KNVQVSSIFE IASELNRLQA LGSASQLGTN DLTGGTFTLS NIGTIGGTYA
KAVILPPEVA IGALGKIQVL PRFNGKGEVF KAQIMNVSWS ADHRIIDGAT MARFSNLWKS
YLENPALMLL DLK
//
