ID G3T8N6_LOXAF Unreviewed; 917 AA.
AC G3T8N6;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 50.
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:ENSLAFP00000010064.3};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000010064.3, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000010064.3, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000010064.3,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000010064.3}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000010064.3};
RG Ensembl;
RL Submitted (JUL-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:ARBA00036608};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69577;
CC Evidence={ECO:0000256|ARBA:ARBA00036608};
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; G3T8N6; -.
DR STRING; 9785.ENSLAFP00000010064; -.
DR Ensembl; ENSLAFT00000012040.3; ENSLAFP00000010064.3; ENSLAFG00000012038.3.
DR eggNOG; KOG0451; Eukaryota.
DR GeneTree; ENSGT00950000183125; -.
DR HOGENOM; CLU_004709_0_0_1; -.
DR InParanoid; G3T8N6; -.
DR OMA; GMAIDNP; -.
DR TreeFam; TF314198; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
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:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
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; 1.
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 NCBIfam; TIGR00239; 2oxo_dh_E1; 1.
DR PANTHER; PTHR23152; 2-OXOGLUTARATE DEHYDROGENASE; 1.
DR PANTHER; PTHR23152:SF4; 2-OXOGLUTARATE DEHYDROGENASE E1 COMPONENT DHKTD1, MITOCHONDRIAL-RELATED; 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; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000007646};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 568..771
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 298..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 917 AA; 102973 MW; F845ACE57AE8812E CRC64;
ASATVAAATR GLGRVPCLLR RGYQTERGVY GYRPRKAESR EPRAGLERPT VDHGLARLVT
VYREHGHKAA KINPLFTGQA LLENVPEIQG LVETLQGPFN TTGLLNMGKE EASLEEVLVY
LNLIYCGQVS IETSQLQSQE EKHWFAKRFE ELKKETFTTE ERKYLSKLML ESQEFDHFLA
TKFATVKRYG GEGAESMMGF FHELLKMSAY SGITDVIIGM PHRGRLNLLT GLLQLPPELM
FRKMRGLSEF PKDFSATGDV LSHLTSSVDL DFGAHHPLHV TMLPNPSHLE AVNPVAVGKT
RGRQQSRQDG DYSPDSSAQP GDKVICLQVH GDASFCGQGI VPETFTLSNL PHFRIGGSFH
LIVNNQLGYT TPAERGRSSL YCSDIGKLVG CAIIHVNGDS PEEVVRATQL AFEYQRRFRK
DVIIDLLCYR QWGHNELDEP FFTNPVMYKI IRARKSIPDT YAEHLIATGL MTQEEVSEIK
ASYYAKLNDH LTNMAHYSPP ATNLQAHWRG LVQPEACVTT WNTGVPLELL RFIGAKSVQV
PEELQMHSHL LKMYVQSRME KVMDGTKLDW ATAEALALGS LLVQGFNVRL SGQDVGRGTF
SQRHAMIVCQ KTDDTYIPLN HMDPNQNGFL EISNSPLSEE AVLGFEYGMS IESPKLLPLW
EAQFGDFFNG AQIIFDTFIS GGEAKWLLQS GIVILLPHGY EGAGPEHSSC RIERFLQMCD
SAEEGVDGDT VNMFVVHPTT PAQYFHLLRR QMVRNFRKPL IVASPKMLLR FPAAVSTLQE
MAPGTTFKPV IGDSSMDPKN VKRLVFCCGK HFYALLKQRE SLGAKKHDFA IIRIEELCPF
PLDSLQQEMS KYKHVKDFIW SQEEPQNMGP WFFVSPRFEK QLACKLRLVS RPPLPAPAVG
IGAVHLQQQE DILTKTF
//