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Database: UniProt
Entry: G3T8N6_LOXAF
LinkDB: G3T8N6_LOXAF
Original site: G3T8N6_LOXAF 
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
//
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