DHTK1_DANRE
ID DHTK1_DANRE Reviewed; 920 AA.
AC Q5PRA2;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 94.
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; ORFNames=zgc:101818;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Olfactory epithelium;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (DEC-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 -!- SEQUENCE CAUTION:
CC Sequence=AAH86742.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC086742; AAH86742.1; ALT_INIT; mRNA.
DR RefSeq; NP_001008619.1; NM_001008619.1.
DR AlphaFoldDB; Q5PRA2; -.
DR SMR; Q5PRA2; -.
DR STRING; 7955.ENSDARP00000025776; -.
DR PaxDb; Q5PRA2; -.
DR GeneID; 494076; -.
DR KEGG; dre:494076; -.
DR CTD; 55526; -.
DR ZFIN; ZDB-GENE-041212-44; dhtkd1.
DR eggNOG; KOG0451; Eukaryota.
DR InParanoid; Q5PRA2; -.
DR OrthoDB; 134699at2759; -.
DR PhylomeDB; Q5PRA2; -.
DR Reactome; R-DRE-389661; Glyoxylate metabolism and glycine degradation.
DR PRO; PR:Q5PRA2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
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 ?..920
FT /note="2-oxoadipate dehydrogenase complex component E1"
FT /id="PRO_0000307940"
FT REGION 299..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 920 AA; 102964 MW; 7753F5D8CB29A2A7 CRC64;
MLIHLPRLLH RSFGARRSFL ASLYHTQRGV YGFRPRDGPE RRAELTQISA LNRDHGLARL
VEAYRAHGHK VAKINPLLPQ SPVLESVPEI SLLNGAVRGV LNTTGLRHFG KAEATAEEVV
AYLESTYCGG ISVETSQLQT LEEREWFADR FEELKKEAFS PEERRMLAKL MLESQEFDHF
LATKFATVKR YGGEGAESMM GFFYELFRSS VYSGVTDVVM GMPHRGRLNL LTGLLQFPPE
LMFRKMRGLS EFPEHSPSIG DVLSHLTSTV ELDFGAGHPL HVTMLPNPSH LEAINPVTQG
KTRGRQQVKQ DGDYSTDPHS RPGDKVICLQ VHGDASFSGQ GIVPETFTLS NLPHYRVGGS
IHLIVNNQVG YTTPSERGRS SLYCSDVGKM VGCAIIHVNG DDAEEVLRAT RLAVEYQRRF
RKDVIVDLLC YRQWGHNELD EPFFTNPAMY KIIRSRKSIP DSYADQLISE GLMTDEERSQ
IKTSYYATLN NQLTNMTLYS PPPTNLQGRW GDLVEPQNRV SCWDTGVAQP LLQFVGAKSV
DIPEEIILHS HLRKTHVQAR LQKLEEGTKL DWSTAEALAF GTLLCQGFNI RISGQDVGRG
TFSQRHAMVV CQETNDMFIP LNHISSEQKG HLEVCNSALS EEAVLGFEYG MSIAQPRLLP
IWEAQFGDFF NGAQIIFDTF LSGGEAKWLL QSGLVILLPH GYDGAGPEHS SCRIERFLQL
CDSKEEGVDG DTVNMAVVNP TLPAQYFHLL RRQMIRNFRK PLIVASPKTL LRFSGAVSGL
SDMGPGTSFK PIIGDSSVNP ASVQRVLFCS GKHYYALLKH RETIPEAEKN TALVRVEELC
PFPTEALQQE LNKYTNAKEF IWSQEEPQNM GCWSFVSPRF EKQLACKLRL VSRPALPAPA
VGIGTLHHQQ HEAILTSSFS
