ID H2RYZ2_TAKRU Unreviewed; 490 AA.
AC H2RYZ2;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
DT 27-MAR-2024, entry version 61.
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:ENSTRUP00000005363.3};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000005363.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000005363.3, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000005363.3}
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 AlphaFoldDB; H2RYZ2; -.
DR STRING; 31033.ENSTRUP00000074680; -.
DR Ensembl; ENSTRUT00000005396.3; ENSTRUP00000005363.3; ENSTRUG00000002330.3.
DR eggNOG; KOG0557; Eukaryota.
DR GeneTree; ENSGT00940000156046; -.
DR OMA; TIKQKPW; -.
DR OrthoDB; 5483022at2759; -.
DR TreeFam; TF332256; -.
DR Proteomes; UP000005226; Chromosome 9.
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:UP000005226};
KW Transferase {ECO:0000256|RuleBase:RU003423};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 49..125
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 179..216
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 137..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..176
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..258
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 490 AA; 52349 MW; 7DD1D1F70D889984 CRC64;
MAASLRLGRQ GVLFGFKLSK FNKCLWSTYP WKEHARFLFQ SPWSLGVAPV KIQMPALSPT
MEEGNIVKWL KKEGEAVAAG DALCEIETDK AVVTMESNDD GVMAKILMEE GSRSVRLGTL
IALMVEEGQD WKQVEIPPPE VVAPPPEAVA PPPAPAAPAP VTPPAAAPPP RPATSGPLRL
SPAARHILET HGLDPKLATP TGPRGLITKE DALNLLKTSP VPKTTPAPPP PSPLQPKAAA
PPAPGSRPNI PPLSTPGKPG APGTFTEIPA SNIRRVIAQR LTQSKTTIPH AYASVDCDMA
AVMSLRKTLA KEEIKVSVND FIIKAAAVTL KEMPEVNVTW SDNGPRPLDS IHIAIAVATD
KGLITPIIKD AANKGVQEIS ANAKALAQKA RDGKLLPEEY QGGSFSISNL GMFGISGFSA
VINPPQSCIL AVGTSRSELR LHEDDQTLRT QQLMTVTLSS DGRLVDDELA SRFLDKFRAN
LEQPQRMILV
//
