ID A0A2K5LZJ3_CERAT Unreviewed; 482 AA.
AC A0A2K5LZJ3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
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:ENSCATP00000018367.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000018367.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000018367.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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}.
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DR RefSeq; XP_011924778.1; XM_012069388.1.
DR RefSeq; XP_011924779.1; XM_012069389.1.
DR RefSeq; XP_011924780.1; XM_012069390.1.
DR AlphaFoldDB; A0A2K5LZJ3; -.
DR SMR; A0A2K5LZJ3; -.
DR STRING; 9531.ENSCATP00000018367; -.
DR Ensembl; ENSCATT00000042542.1; ENSCATP00000018367.1; ENSCATG00000032994.1.
DR GeneID; 105590148; -.
DR KEGG; caty:105590148; -.
DR CTD; 1629; -.
DR GeneTree; ENSGT00940000156750; -.
DR OrthoDB; 1399at2759; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000032994; Expressed in liver and 12 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0015630; C:microtubule cytoskeleton; IEA:Ensembl.
DR GO; GO:0005947; C:mitochondrial alpha-ketoglutarate dehydrogenase complex; IEA:Ensembl.
DR GO; GO:0042645; C:mitochondrial nucleoid; IEA:Ensembl.
DR GO; GO:0043754; F:dihydrolipoyllysine-residue (2-methylpropanoyl)transferase activity; IEA:RHEA.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0009083; P:branched-chain amino acid catabolic process; IEA:Ensembl.
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:UP000233060};
KW Transferase {ECO:0000256|RuleBase:RU003423};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 64..139
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 172..209
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 147..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 482 AA; 53467 MW; F67DC827469FCF73 CRC64;
MAAVRMLRTW SRNAGKLICV RYFQTCGNVH VLKPNYVCFF GYPSFKYSHP HHFLKTTAAL
RGQVVQFKLS DIGEGIREVT VKEWYVKEGD TVSQFDSICE VQSDKASVTI TSRYDGVIKK
LYYNLDDIAY VGKPLVDIET EALKDSEEDV VETPAVSHDE HTHQEIKGRK TLATPAVRRL
AMENNIKLSE VVGSGKDGRI LKEDILNYLE KQTGAILPPS PKAEIMPPPP KPKDMTIPIP
VSKPPVFTGK DKTEPIKGFQ KAMVKTMSAA LKIPHFGYCD EVDLTELVKL REELKPIAFA
RGIKLSFMPF FLKAVSLGLL QFPILNASVD ENCQNITYKA SHNIGIAMDT EQGLIVPNVK
NVQICSIFDI ATELNRLQKL GSVGQLSTTD LTGGTFTLSN IGSIGGTYTK PVILPPEVAI
GALGSIKAIP RFNQKGEVYK AQIVNVSWSA DHRVIDGATM SRFSNLWKSY LENPAFMLLD
LK
//
