ID H3AQ82_LATCH Unreviewed; 534 AA.
AC H3AQ82;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 65.
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|Ensembl:ENSLACP00000011803.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000011803.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000011803.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 EMBL; AFYH01125721; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01125722; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01125723; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01125724; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01125725; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01125726; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01125727; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01125728; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01125729; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01125730; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_014347495.1; XM_014492009.1.
DR RefSeq; XP_014347496.1; XM_014492010.1.
DR AlphaFoldDB; H3AQ82; -.
DR STRING; 7897.ENSLACP00000011803; -.
DR Ensembl; ENSLACT00000011893.1; ENSLACP00000011803.1; ENSLACG00000010390.1.
DR GeneID; 102348671; -.
DR KEGG; lcm:102348671; -.
DR CTD; 8050; -.
DR eggNOG; KOG0557; Eukaryota.
DR GeneTree; ENSGT00940000156046; -.
DR HOGENOM; CLU_016733_10_2_1; -.
DR InParanoid; H3AQ82; -.
DR OMA; TIKQKPW; -.
DR OrthoDB; 5483022at2759; -.
DR TreeFam; TF332256; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000010390; Expressed in muscle tissue and 6 other cell types or tissues.
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 Reference proteome {ECO:0000313|Proteomes:UP000008672};
KW Transferase {ECO:0000256|RuleBase:RU003423};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 82..158
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 211..248
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 173..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..288
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 534 AA; 56639 MW; 5199FA1981FBEF4D CRC64;
MAAAVVVRRF GSSGGTGIIR AFSHHRTGTL RTLSQPGPGS GALRAGTENA CPRARLSPRW
TGTETGHRFL AGSGRLQLGV PPVKVLMPAL SPTMEEGNIV KWYKKEGEVV TAGDALCEIE
TDKAVVTMDS NDDGILAKIM LEEGSKNVRL GTLIALLVEE GQDWKQVEIP ADTDAPTTAS
APPLSMPSPP VGAKVSVSNK PAYQAGNLQI RLSPAARYIL ETHGLDPSQI TPSGPRGIIT
KEDALKAMKA GVSVSSLTKV APVHTTMPRP PAAPAAPPAA PTPQTYPRPT TPAVSILGQP
AAPGTFTEIP ASNIRRVIAK RLTESKTTIP HAYATIDCDL DKVLQMRKEL AKDEVKVSVN
DFIIKAAAMT LKQMPDVNVT WNGEGPRQLS SIDIAIAVAT DRGLITPIIR DAVAKGIQEI
AASAKVLAKK ARDGKLLPEE YQGGSFSISN LGMFGISGFS AVINPPQACI LAVGQTRPEL
TVVEDPAGET SIRQRQLLTV TLSSDGRMVD DELASRFLEN FKANIENPIQ FSLF
//
