ID G3W346_SARHA Unreviewed; 921 AA.
AC G3W346;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 2.
DT 27-MAR-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:ENSSHAP00000009851.2};
OS Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus.
OX NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000009851.2, ECO:0000313|Proteomes:UP000007648};
RN [1] {ECO:0000313|Ensembl:ENSSHAP00000009851.2, ECO:0000313|Proteomes:UP000007648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21709235; DOI=10.1073/pnas.1102838108;
RA Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., Miller J.,
RA Walenz B., Knight J., Qi J., Zhao F., Wang Q., Bedoya-Reina O.C.,
RA Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., Woodbridge P.,
RA Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., Helgen K.M.,
RA Lesk A.M., Pringle T.H., Patterson N., Zhang Y., Kreiss A., Woods G.M.,
RA Jones M.E., Schuster S.C.;
RT "Genetic diversity and population structure of the endangered marsupial
RT Sarcophilus harrisii (Tasmanian devil).";
RL Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011).
RN [2] {ECO:0000313|Ensembl:ENSSHAP00000009851.2}
RP IDENTIFICATION.
RG Ensembl;
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 AlphaFoldDB; G3W346; -.
DR STRING; 9305.ENSSHAP00000009851; -.
DR Ensembl; ENSSHAT00000009938.2; ENSSHAP00000009851.2; ENSSHAG00000008531.2.
DR eggNOG; KOG0451; Eukaryota.
DR GeneTree; ENSGT00950000183125; -.
DR HOGENOM; CLU_004709_2_2_1; -.
DR InParanoid; G3W346; -.
DR TreeFam; TF314198; -.
DR Proteomes; UP000007648; 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: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:UP000007648};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 571..774
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 921 AA; 103324 MW; F389F1B710C6DA93 CRC64;
MAYSVAAVVA RRNLGWIPQH LLRCGYQTER GVYGYRPKQR ENGEPRGGPA RAGVDHGLAR
LVTAFCEHGH KAAKINPLFA GQSVMENVPE IQTLVETLQG PFNTTGLLSM GKEEVSLEEV
LAYLNHIYCG QISIETTQLQ TQEEKDWFSS RFEELKKETF TTEERKHLSR LMLESQEFDH
FLATKFATVK RYGGEGAESM MGFFHELLKT AAYSGVTDVI IGMPHRGRLN LLTGLLQFPP
ELMFRKMRGL SEFPESISAI GDVLSHLTSS VDLDFGSHRP LHVTMLPNPS HLEAVNPVAV
GKTRGRQQSQ LDGDYSTDSS AQPGDKVICL QVHGDASFCG QGIVPETFTL SNLPHFRIGG
SIHLIVNNQL GYTTPAERGR SSLYCSDIGK IVGCAVIHVN GDDPEEVVRA TRLAVEYQRQ
FRKDVIVDLL CYRQWGHNEL DEPFFTNPMM YKIIRSRKSI PDTYAETLIA HGLMTQDEVS
EIKTSYYSKL SDHLTNMTLY SPPATNLQAH WRGLVEPSAR ITTWDTGVPI DLLRFVGGKS
VEVPEEFQLH SHLLKTHVQS RIEKIKEGMK LDWATAEALA LGSLLAQGFN VRLSGQDVGR
GTFSQRHAMI VCQKTDDTYI PLNHMDPNQK GFLEVSNSPL SEEAVLGFEY GMSIESPKLL
PIWEAQFGDF FNGAQIIFDT FISGGESKWL LQSGIVILLP HGYDGAGPDH SSCRMERFLQ
MCDSVEEGVD GDNVNMFVVH PTTPAQYFHL LRRQMIRNFR KPLIVASPKI LLRFPAAVSS
FQEMVPGTTF KPVIGDSSVD PKNVKSIIFC FGKHFYALMK QRETLGKKKD ETAIIRIEEL
CPFPLEALQQ ELSKYKNAKD FIWSQEEPQN MGPWFFISPR FEKQLACKLR LVSRPPLPAP
AVGIGTIHLQ QQEEILTKTF A
//
