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Database: UniProt
Entry: A0A3Q1D146_AMPOC
LinkDB: A0A3Q1D146_AMPOC
Original site: A0A3Q1D146_AMPOC 
ID   A0A3Q1D146_AMPOC        Unreviewed;       497 AA.
AC   A0A3Q1D146;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE            EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
OS   Amphiprion ocellaris (Clown anemonefish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Amphiprion.
OX   NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000031694.1, ECO:0000313|Proteomes:UP000257160};
RN   [1] {ECO:0000313|Ensembl:ENSAOCP00000031694.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|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   AlphaFoldDB; A0A3Q1D146; -.
DR   STRING; 80972.ENSAOCP00000031694; -.
DR   Ensembl; ENSAOCT00000027908.1; ENSAOCP00000031694.1; ENSAOCG00000023544.1.
DR   GeneTree; ENSGT00940000156750; -.
DR   OMA; TIPHFTY; -.
DR   OrthoDB; 1399at2759; -.
DR   Proteomes; UP000257160; Unplaced.
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:UP000257160};
KW   Transferase {ECO:0000256|RuleBase:RU003423};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          65..140
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          175..212
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
SQ   SEQUENCE   497 AA;  54531 MW;  158FEF1F162E62C4 CRC64;
     MAAVTRGSFS VFRRLVSQQY RRRCFRLQTF RSVRTLQPLS STWDRKLQMF SSRTLHTTMV
     NQGPIVQFKL SDIGEGIMEV TVKEWYVKEG DKVSQFDSIC EVQSDKASVT ITSRYDGVIR
     KLYYDVDATA LVGKPLVDIE TESSSEVIQE EDVVETPAMA REEHTHQEIK GHKTQATPAV
     RRLAMENNIK LSEVVGTGKD GRILKEDILN FLAKQTGAIL PPAPFQEIQT PPPAAPTAAA
     AAARPLSIPP AVKPPPITKP AFTGKDVTEP LKGFHKAMVK TMTAALKIPH FGYCDEVDLS
     RLVSLRSELK SVSESRGVRL SYMPFFIKAA SLGLLHFPVL NASVDEGCQN ITYKASHNIG
     LAMDTSQGLL VPNVKNVQLL SVLEIAQELN RLQTLGAAGQ LGAADLSGGT FTLSNIGSIG
     GTYTKPVILP PEVAIGALGK IQVLPRFDAA GQVFRAHIMQ VSWSADHRII DGATMCRFSN
     LWRDYLENPA TMVLDLK
//
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