ID   DHTK1_XENLA             Reviewed;         927 AA.
AC   Q6P286;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 72.
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   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
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; BC064683; AAH64683.1; -; mRNA.
DR   RefSeq; NP_001084395.1; NM_001090926.1.
DR   AlphaFoldDB; Q6P286; -.
DR   SMR; Q6P286; -.
DR   MaxQB; Q6P286; -.
DR   DNASU; 403360; -.
DR   GeneID; 403360; -.
DR   KEGG; xla:403360; -.
DR   CTD; 403360; -.
DR   Xenbase; XB-GENE-980614; dhtkd1.L.
DR   OMA; GMAIDNP; -.
DR   OrthoDB; 134699at2759; -.
DR   Proteomes; UP000186698; Chromosome 3L.
DR   Bgee; 403360; Expressed in blastula and 19 other tissues.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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:0006096; P:glycolytic process; IEA:UniProtKB-KW.
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           ?..927
FT                   /note="2-oxoadipate dehydrogenase complex component E1"
FT                   /id="PRO_0000307941"
SQ   SEQUENCE   927 AA;  104104 MW;  43AEFD67A73A0EF3 CRC64;
     MNVFAHRCSS CRRAVVLWRP GLHRLYRTER GVYGYRPKIS AGSQLQESST RGKQAASPTV
     DHGLARLVTA YREHGHKAAK INPLFTGQAV MDMVPEIQEI MEILHGPFST TGLLNMGKSE
     ATIEEVLAYL DHTYCGQISI ETSQLQNYKE REWFSRRFEE LKQESFSTEE RKHLARLMLE
     CQEFDHFLAT KFSTVKRYGG EGAESMMGFF HEMLKMCSFG GVTDVIIGMP HRGRLNLLTG
     LLQFPPELMF RKMRGLSEFP ENSPSIGDVL SHLTSSVDLD FGSHRPLHVT MLPNPSHLEA
     INPVAVGKTR ARQQSLSDGD YSTESSAQPG DKVVCLQVHG DASISGQGIV TETFTLSNLP
     HYRIGGSIHL IVNNQLGYTT PAERGRSSLY SSDVGKIVGC AVIHVNGDDP EEVLRATRLA
     VEYQRCFRKD VIIDLLCYRQ WGHNELDEPF FTNPSMYKII RSRKSIPDVY SERLIAEGLM
     TEEEATEIRT TYYSKFNDHL SNMTLYSPPS TNLQAHWREM IEPSARTTTW DTGLPADLLK
     FIGAKSVEVP EEFKMHSHLL KMHAQSRVQK LQEATKLDWA TAEALAFGSL LCQGFNIRIS
     GQDVGRGTFS QRHAMLVCQE TNDTYIPLNH MTPDQKGFLE VSNSALSEEA VLGFEYGMSI
     ESPKLLPIWE AQFGDFFNGA QIIFDTFISG GEAKWLLQSG IVILLPHGYD GAGPEHSSCR
     IERFLQMCDS TEEGVDGDTV NMFVVHPTTP AQYFHLLRRQ MVRSFRKPLI VASPKMLLRY
     PAAVSSLEDI APGKTFRSVI GDSSADPKSV SKVILCSGKH YYALHKQREA LGEQGRSSAI
     IRVEELCPFP LEALQQEIHR YPKAKDFIWS QEEPQNMGAW TFVAPRFEKQ LACKLRLVSR
     PALPAPAVGI GTLHQQQQEE ITVKTLS