DHTK1_RAT
ID DHTK1_RAT Reviewed; 920 AA.
AC Q4KLP0;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=2-oxoadipate dehydrogenase complex component E1;
DE Short=E1a {ECO:0000250|UniProtKB:Q96HY7};
DE Short=OADC-E1;
DE Short=OADH-E1;
DE EC=1.2.4.- {ECO:0000250|UniProtKB:Q96HY7};
DE AltName: Full=2-oxoadipate dehydrogenase, mitochondrial;
DE AltName: Full=Alpha-ketoadipate dehydrogenase;
DE Short=Alpha-KADH-E1;
DE AltName: Full=Dehydrogenase E1 and transketolase domain-containing protein 1;
DE AltName: Full=Probable 2-oxoglutarate dehydrogenase E1 component DHKTD1, mitochondrial;
DE Flags: Precursor;
GN Name=Dhtkd1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: 2-oxoadipate dehydrogenase (E1a) component of the 2-
CC oxoadipate dehydrogenase complex (OADHC). Participates in the first
CC step, rate limiting for the overall conversion of 2-oxoadipate (alpha-
CC ketoadipate) to glutaryl-CoA and CO(2) catalyzed by the whole OADHC.
CC Catalyzes the irreversible decarboxylation of 2-oxoadipate via the
CC thiamine diphosphate (ThDP) cofactor and subsequent transfer of the
CC decarboxylated acyl intermediate on an oxidized dihydrolipoyl group
CC that is covalently amidated to the E2 enzyme (dihydrolipoyllysine-
CC residue succinyltransferase or DLST). Can catalyze the decarboxylation
CC of 2-oxoglutarate in vitro, but at a much lower rate than 2-oxoadipate.
CC Responsible for the last step of L-lysine, L-hydroxylysine and L-
CC tryptophan catabolism with the common product being 2-oxoadipate.
CC {ECO:0000250|UniProtKB:Q96HY7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue
CC succinyltransferase] + 2-oxoadipate + H(+) = (R)-N6-(S8-
CC glutaryldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue
CC succinyltransferase] + CO2; Xref=Rhea:RHEA:69576, Rhea:RHEA-
CC COMP:10483, Rhea:RHEA-COMP:17726, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57499, ChEBI:CHEBI:83099,
CC ChEBI:CHEBI:184385; Evidence={ECO:0000250|UniProtKB:Q96HY7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69577;
CC Evidence={ECO:0000250|UniProtKB:Q96HY7};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250|UniProtKB:Q96HY7};
CC -!- PATHWAY: Amino-acid degradation. {ECO:0000250|UniProtKB:Q96HY7}.
CC -!- SUBUNIT: The 2-oxoadipate dehydrogenase complex is composed of OADH (2-
CC oxoadipate dehydrogenase; E1a), DLST (dihydrolipoamide
CC succinyltransferase; E2) and DLD (dihydrolipoamide dehydrogenase; E3).
CC E1a functional unit is a dimer. {ECO:0000250|UniProtKB:Q96HY7}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q96HY7}.
CC -!- MISCELLANEOUS: The mitochondrial 2-oxoglutarate and 2-oxoadipate
CC dehydrogenase complexes (OGDHC and OADHC, respectively) share their E2
CC (DLST) and E3 (dihydrolipoyl dehydrogenase or DLD) components, but the
CC E1 component is specific to each complex (E1o and E1a, respectively).
CC {ECO:0000250|UniProtKB:Q96HY7}.
CC -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
CC {ECO:0000250|UniProtKB:Q96HY7}.
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DR EMBL; BC099075; AAH99075.1; -; mRNA.
DR RefSeq; NP_001020891.1; NM_001025720.1.
DR AlphaFoldDB; Q4KLP0; -.
DR SMR; Q4KLP0; -.
DR STRING; 10116.ENSRNOP00000059952; -.
DR iPTMnet; Q4KLP0; -.
DR PhosphoSitePlus; Q4KLP0; -.
DR PRIDE; Q4KLP0; -.
DR GeneID; 361272; -.
DR KEGG; rno:361272; -.
DR CTD; 55526; -.
DR RGD; 1308092; Dhtkd1.
DR VEuPathDB; HostDB:ENSRNOG00000023587; -.
DR eggNOG; KOG0451; Eukaryota.
DR HOGENOM; CLU_004709_0_0_1; -.
DR InParanoid; Q4KLP0; -.
DR OMA; GMAIDNP; -.
DR OrthoDB; 134699at2759; -.
DR PhylomeDB; Q4KLP0; -.
DR Reactome; R-RNO-389661; Glyoxylate metabolism and glycine degradation.
DR PRO; PR:Q4KLP0; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Bgee; ENSRNOG00000023587; Expressed in liver and 19 other tissues.
DR Genevisible; Q4KLP0; RN.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
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:0006091; P:generation of precursor metabolites and energy; ISS:UniProtKB.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; ISO:RGD.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR Gene3D; 3.40.50.11610; -; 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; PTHR23152; 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; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; SSF52518; 2.
DR TIGRFAMs; TIGR00239; 2oxo_dh_E1; 1.
PE 2: Evidence at transcript level;
KW Glycolysis; Mitochondrion; Oxidoreductase; Reference proteome;
KW Thiamine pyrophosphate; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..920
FT /note="2-oxoadipate dehydrogenase complex component E1"
FT /id="PRO_0000307939"
FT REGION 299..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 183
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:A2ATU0"
FT MOD_RES 188
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:A2ATU0"
FT MOD_RES 800
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:A2ATU0"
FT MOD_RES 818
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:A2ATU0"
SQ SEQUENCE 920 AA; 102642 MW; AA4A70E36AA41104 CRC64;
MASATVAAAG RALRRAVPLL RRSYQTERGV YGYRPRKAGS GEPRGDRARP SVDHGLARLV
TVYCEHGHKA AQINPLFPGQ ALLDTVPEIQ ALVQTLQGPF TTTGLLNMGK EEASLEEVLA
YLNHIYCGPI SIETAQLQSQ EEKDWFARRF EELKKETFTT EERKHLSKLL LESQEFDHFL
ATKFATVKRY GGEGAESMMG FFHELLKLSA YGGITDIIIG MPHRGRLNLL TGLLQLPPEL
MFRKMRGLSE FPENVAAIGD VLSHLTSSVD LDFGAHRPLH VTMLPNPSHL EAINPVAVGK
TRGRQQSQED GDYSPNGSAQ PGDKVICLQV HGDASFCGQG IVLETFTLSN LPHFRIGGSI
HLIVNNQLGY TTPAERGRSS LYSSDIGKLV GCAIIHVNGD SPEEVVRATR LAFEYQRQFR
KDVIIDLLCY RQWGHNELDE PFFTNPVMYK IIRARKSIPD TYAEHLIASG LMTQEEVSDI
KASYYAKLNG HLANVAHYSP PAPHLQARWQ GLVQPAACVT TWDTGVPLEL LRFVGVKSVE
VPEELQLHSH LLKMYVQSRM EKVKNGTNLD WATAETLALG SLLAQGFNVR LSGQDVGRGT
FSQRHAMVVC QNTDDVYIPL NHMDPNQKGF LEVSNSPLSE EAVLGFEYGM SIESPKLLPL
WEAQFGDFFN GAQIIFDTFI SGGEAKWLLQ SGLVILLPHG YDGAGPDHSS CRIERFLQMC
DSAEEGVDSD TVNMFVVHPT TPAQYFHLLR RQMMRNFRKP LIVASPKMLL RYPVAVSTLE
EMAPGTAFKP VIGDSSVDPK NVKTLIFCSG KHFYALLKQR ESLGAKKRDF AIIRLEELCP
FPLDSLQQEM GKYKHVQDII WSQEEPQNMG PWSFVYPRFE KQLACKLRLV SRPPLPAPAV
GIGTVHQQQH EAILFKTFTS
