DHTK1_PONAB
ID DHTK1_PONAB Reviewed; 919 AA.
AC Q5R7H0;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 71.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR860147; CAH92290.1; -; mRNA.
DR RefSeq; NP_001126339.1; NM_001132867.1.
DR AlphaFoldDB; Q5R7H0; -.
DR SMR; Q5R7H0; -.
DR STRING; 9601.ENSPPYP00000003298; -.
DR PRIDE; Q5R7H0; -.
DR GeneID; 100173320; -.
DR KEGG; pon:100173320; -.
DR CTD; 55526; -.
DR eggNOG; KOG0451; Eukaryota.
DR InParanoid; Q5R7H0; -.
DR OrthoDB; 134699at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProt.
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: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 ?..919
FT /note="2-oxoadipate dehydrogenase complex component E1"
FT /id="PRO_0000307938"
FT REGION 299..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..316
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 919 AA; 103036 MW; 6F111B5B0A5A3198 CRC64;
MASATAAAAR RCLGRAPPLL WRGYQTERGV YGYRPRKPES RKPQGALERP PVDHGLARLV
TVYREHGHKA AKINPLFTGQ ALLENVPEIQ ALVQTLQGPF HTAGLLNMGK EEASLEEVLV
YLNQIYCGQI SIETSQLQSQ EEKDWFAKRF EELQKETFTT EERKHLSKLM LESQEFDHFL
ATKFSTVKRY GGEGAESMMG FFYELLKMSA YSGITDVIIG MPHRGRLNLL TGLLQFPPEL
MFRKMRGLSE FPENFSATGD VLSHLTSSVD LDFGAHHPLH VTMLPNPSHL EAVNPVAVGK
TRGRQQSRQD GDYSPDNSAQ PGDRVICLQV HGDASFCGQG IVPETFTLSN LPHFRIGGSV
HLIVNNQLGY TTPAERGRSS LYCSDIGKLV GCAIIHVNGD SPEEVVRATR LAFEYQRQFR
KDVIIDLLCY RQWGHNELDE PFFTNPIMYK IIRARKSIPD TYAEHLIAGG LMTQEEVSEI
KSSYYAKLND HLNNMAHYSP PAQNLQAHWQ GLAQPEARIT TWSTGVPLDL LRFVGVKSVE
VPRQLQMHSH LLKTHVQSRM EKVMDGTKLD WATAEALALG SLLAQGFNVR LSGQDVGRGT
FSQRHAMVVC QETDDTYIPL NHMDPNQKGF LEVSNSPLSE EAVLGFEYGM SIESPKLLPL
WEAQFGDFFN GAQIIFDTFI SGGEAKWLLQ SGIVTLLPHG HDGAGPDHSS CRIERFLQMC
DSAEEGVDGD TVNMFVVHPT TPAQYFHLLR RQMVRNFRKP LIVASPKMLL RLPAAVSTLQ
EMAPGTTFNP VIGDSSVDPK KVKTLVFCSG KHFYSLMKQR ESLGAKKHDF AIIRVEELCP
FPLDSLQQEM SKYKHVKDHI WSQEEPQNMG PWLFVSPRFE KQLACKLRLV GRPPLPVPAV
GIGTVHLHQH EDILAKTFA
