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Database: UniProt
Entry: A0A3B3D7N6_ORYME
LinkDB: A0A3B3D7N6_ORYME
Original site: A0A3B3D7N6_ORYME 
ID   A0A3B3D7N6_ORYME        Unreviewed;       498 AA.
AC   A0A3B3D7N6;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE            EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
OS   Oryzias melastigma (Marine medaka).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC   Oryzias.
OX   NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000025489.1, ECO:0000313|Proteomes:UP000261560};
RN   [1] {ECO:0000313|Ensembl:ENSOMEP00000025489.1}
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   AlphaFoldDB; A0A3B3D7N6; -.
DR   STRING; 30732.ENSOMEP00000025489; -.
DR   PaxDb; 30732-ENSOMEP00000025489; -.
DR   Ensembl; ENSOMET00000006979.1; ENSOMEP00000025489.1; ENSOMEG00000006766.1.
DR   GeneTree; ENSGT00940000156750; -.
DR   OMA; MPFCIKA; -.
DR   Proteomes; UP000261560; 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   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"
FT   REGION          223..266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        225..240
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   498 AA;  54401 MW;  6945B6B334EFBF7D CRC64;
     MAAVTRSSYI FVSRLLSQHL CRRSFRLQNF RSSRTLQQIT FRCSREPQVF SRRALHAASA
     CCGPVVQFKL SDIGEGIMEV TVKEWYVKEG DKVSQFDSIC EVQSDKASVT ITSRYDGVIK
     KLYYDVDATA LVGKPLVDIE TESSSEVIQE EDVVETPAMA REEHTHQEIK GHKTQATPAV
     RRLAMENNIK LSEVVGTGKD GRILKEDILN FLAKQTGAIL PPAPVQEIQT PPPSPPSTAA
     PVGRPVSTST VAKAPPPRAT PVFTGKDVTE PVKGFHKAMV KTMTAALKIP HFGYCDEVDL
     SRLVALRTEL KPIAESRGVK LSYMPFFIKA ASLGLLHFPI LNASVDEDCQ NITYRASHNI
     GLAMDTSQGL LVPNVKNVQL LSVFEIAQEL NRLQALGTAG QLSTAHLTGG TFTLSNIGSI
     GGTYAKPVIL PPEVAIGALG KIQVLPRFGA GNQVVPAHIM KVSWSADHRV IDGATMCRFS
     NLWREYLENP ASMVLDLK
//
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