ID A0A1U8D381_ALLSI Unreviewed; 837 AA.
AC A0A1U8D381;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 2.
DT 27-MAR-2024, entry version 28.
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|RefSeq:XP_014374731.2};
OS Alligator sinensis (Chinese alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_014374731.2};
RN [1] {ECO:0000313|RefSeq:XP_014374731.2}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-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:ARBA00043772};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69577;
CC Evidence={ECO:0000256|ARBA:ARBA00043772};
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 RefSeq; XP_014374731.2; XM_014519245.2.
DR AlphaFoldDB; A0A1U8D381; -.
DR STRING; 38654.A0A1U8D381; -.
DR KEGG; asn:102376609; -.
DR eggNOG; KOG0451; Eukaryota.
DR InParanoid; A0A1U8D381; -.
DR OrthoDB; 3597773at2759; -.
DR Proteomes; UP000189705; Unplaced.
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: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 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:SF4; 2-OXOADIPATE DEHYDROGENASE COMPLEX COMPONENT E1; 1.
DR PANTHER; PTHR23152; 2-OXOGLUTARATE DEHYDROGENASE; 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:UP000189705};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 487..690
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 837 AA; 93652 MW; 93FCB1459220D2EE CRC64;
MDMVPEIRML SEVLQGPFNI TGLLNMGKEE VSLEDVLAYL DHIYCGHISI ETSQLPSPEE
RDWFAKRFEE LKQEAFTTEE KKHLSKVMLE SQEFDHFLAT KFATVKRYGG EGAESMMGFF
HELFKMCAYS GVTDVVLGMP HRGRLNLLAG LLQFPPELMF RKMRGLSEFP ENSPAIGDVL
SHLTSSVDLD FGSHRPVHVT LLPNPSHLEA INPVAVGKTR GRQQSVLDGD YSPDSSAQPG
DKVICLQVHG DGAFSGQGIV PETLTLSNLP HFRVGGSIHL IVNNQLGYTT PPERGRSSLY
CSDIGKIIGC AIIHVNADDP EEVIRATRLA VEYQRNFRRD VVVDLLCYRQ WGHNELDEPF
FTNPGMYKII RSRKSIPDTY AEQLVTGGLM TEDEVSEIKT SYYSKLNNHL ANMTLYTPPP
TNLQAHWSGM VEPTARITTW DTGVPVSLLQ FIGIKSVEVP EELQMHSHLL KTYVQARKQK
VEEGTKLDWA TAEALAFGAL LSQGFNIRLS GQDVGRGTFS QRHAMLVCQE TDDTYIPLNH
MSPDQKGFLE VSNSPLSEEA VLGFEYGMSI ESPKLLPIWE AQFGDFFNGA QIIFDTFISG
GEAKWLLQSG IVILLPHGYD GAGPEHSSCR LERFLQMCDS SEEGVDGDNV NMSVVHPTTP
AQYFHLLRRQ MIRNFRKPLI IASPKMLLRL PAAVSGLQEL APGTTFRPVI GDSSIDPKSV
TRVVLCSGKH YYALVKQREA LGEQQRSTAI IRLEELCPFP LEALQQEMNK YKNAKDFIWS
QEEPQNMGPW TFVSPRFEKQ LACKLHLVSR PPLPAPAVGI GTLHQQQQEH ILTKTFA
//
