ID A0A287ALM2_PIG Unreviewed; 856 AA.
AC A0A287ALM2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2022, sequence version 2.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=2-oxoadipate dehydrogenase complex component E1 {ECO:0000256|ARBA:ARBA00040865};
DE AltName: Full=2-oxoadipate dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00041619};
DE AltName: Full=Alpha-ketoadipate dehydrogenase {ECO:0000256|ARBA:ARBA00042817};
DE AltName: Full=Dehydrogenase E1 and transketolase domain-containing protein 1 {ECO:0000256|ARBA:ARBA00042094};
DE AltName: Full=Probable 2-oxoglutarate dehydrogenase E1 component DHKTD1, mitochondrial {ECO:0000256|ARBA:ARBA00042537};
GN Name=DHTKD1 {ECO:0000313|Ensembl:ENSSSCP00000044926.2,
GN ECO:0000313|VGNC:VGNC:97966};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000044926.2, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000044926.2, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000044926.2,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000044926.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoadipate + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-
CC [dihydrolipoyllysine-residue succinyltransferase] = CO2 + N(6)-[(R)-
CC S(8)-glutaryldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC succinyltransferase]; Xref=Rhea:RHEA:69576, Rhea:RHEA-COMP:10483,
CC Rhea:RHEA-COMP:17726, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57499, ChEBI:CHEBI:83099, ChEBI:CHEBI:184385;
CC Evidence={ECO:0000256|ARBA:ARBA00043772};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69577;
CC Evidence={ECO:0000256|ARBA:ARBA00043772};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00006936}.
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DR AlphaFoldDB; A0A287ALM2; -.
DR STRING; 9823.ENSSSCP00000044926; -.
DR PaxDb; 9823-ENSSSCP00000011854; -.
DR Ensembl; ENSSSCT00000057195.3; ENSSSCP00000044926.2; ENSSSCG00000039539.3.
DR VGNC; VGNC:97966; DHTKD1.
DR GeneTree; ENSGT00950000183125; -.
DR InParanoid; A0A287ALM2; -.
DR Proteomes; UP000008227; Chromosome 10.
DR Bgee; ENSSSCG00000039539; Expressed in liver and 43 other cell types or tissues.
DR ExpressionAtlas; A0A287ALM2; baseline and differential.
DR GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:UniProtKB-EC.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR CDD; cd02016; TPP_E1_OGDC_like; 1.
DR Gene3D; 3.40.50.12470; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR Gene3D; 3.40.50.11610; Multifunctional 2-oxoglutarate metabolism enzyme, C-terminal domain; 2.
DR Gene3D; 1.10.287.1150; TPP helical domain; 1.
DR InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR031717; KGD_C.
DR InterPro; IPR042179; KGD_C_sf.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR PANTHER; PTHR23152:SF4; 2-OXOADIPATE DEHYDROGENASE COMPLEX COMPONENT E1; 1.
DR PANTHER; PTHR23152; 2-OXOGLUTARATE DEHYDROGENASE; 1.
DR Pfam; PF00676; E1_dh; 1.
DR Pfam; PF16870; OxoGdeHyase_C; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR PIRSF; PIRSF000157; Oxoglu_dh_E1; 2.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 569..753
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 856 AA; 95784 MW; 7586C09D62181678 CRC64;
MALATVAAAR LGLSRAPSLL RRGYQTERGV YGYRPRKRES REPQGGLARP SVDHGLARLV
TVYCEHGHKA AKINPLFTGQ ALQENVPEIQ ALVQTLQGPF NTAGLLNMGK EEASLEEVVA
YLNQIYCGQI SIETSQLQSQ EEKDWFAKRF EELKKEAFTT EERKHLSKLM LESQAFDHFL
ATKFATVKRY GGEGAESMMG FFYELLRTAA YSGVTDVIIG MPHRGRLNLL TGLLQFPPEL
MFRKMRGLSE FPENVSNVGD VLSHLTSSVD LDFGAHHPLH VTMLPNPSHL EAVNPVAVGK
TRGRQQSRQD GDYSPDSSAQ PGDKVICLQV HGDASFCGQG IVPETFTLSN LPHFRIGGSI
HLIVNNQLGY TTPAERGRSS LYCSDIGKLV GCAIIHVNGD SPEEVVHAAR LALEYQRQFR
KDVIVDLLCY RQWGHNELDE PLFTNPVMYQ IIRARKSIPD TYAENLVASG LMTQEEVSEI
KASYYAKLNG HLANMAHYSP PATHLQAHWQ GLVQPEASIT TWNTGVPPDL LRFIGKKSVE
VPEELQVHSH LLKMYVQSRL EKVMDGTKLD WATAEALALG SLLAEGFNVR LSGQDVGRGT
FSQRHAMVVC QKTDDTYIPL NHMDPNQKGF LEVSNSPLSE EAVLGFEYGM SIESPKLLPL
WEAQFGDFFN GAQIIFDTFI SGGEAKWLLQ SGLVVLLPHG YDGAGPDHSS CRIERFLQVF
LTLRYLSPPP TVPFLSNRVK SLVFCSGKHF YALLKQRDSL EAKRHDFAII RIEELCPFPL
ESLQQEMSRY KHVRDFIWSQ EEPQNMGPWF FVSPRFEKQL ACKLRLVSRP ALPVPAVGIG
TVHLQQQEEV LTKTFT
//
