ID F6R5L4_XENTR Unreviewed; 1018 AA.
AC F6R5L4;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 4.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN Name=ogdhl {ECO:0000313|Ensembl:ENSXETP00000012378,
GN ECO:0000313|RefSeq:XP_002933951.2,
GN ECO:0000313|Xenbase:XB-GENE-984152};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364 {ECO:0000313|Ensembl:ENSXETP00000012378};
RN [1] {ECO:0000313|Ensembl:ENSXETP00000012378}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000012378};
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [2] {ECO:0000313|Ensembl:ENSXETP00000012378}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUN-2011) to UniProtKB.
RN [3] {ECO:0000313|RefSeq:XP_002933951.2}
RP IDENTIFICATION.
RC STRAIN=Nigerian {ECO:0000313|RefSeq:XP_002933951.2};
RC TISSUE=Liver and blood {ECO:0000313|RefSeq:XP_002933951.2};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-
CC [dihydrolipoyllysine-residue succinyltransferase] = CO2 + N(6)-[(R)-
CC S(8)-succinyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC succinyltransferase]; Xref=Rhea:RHEA:12188, Rhea:RHEA-COMP:10483,
CC Rhea:RHEA-COMP:10484, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:83099, ChEBI:CHEBI:83120; EC=1.2.4.2;
CC Evidence={ECO:0000256|ARBA:ARBA00043712};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12189;
CC Evidence={ECO:0000256|ARBA:ARBA00043712};
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_002933951.2; XM_002933905.5.
DR STRING; 8364.ENSXETP00000012378; -.
DR Ensembl; ENSXETT00000012378; ENSXETP00000012378; ENSXETG00000005613.
DR KEGG; xtr:100497480; -.
DR AGR; Xenbase:XB-GENE-984152; -.
DR Xenbase; XB-GENE-984152; ogdhl.
DR eggNOG; KOG0450; Eukaryota.
DR HOGENOM; CLU_004709_1_1_1; -.
DR OMA; IRIRRHN; -.
DR OrthoDB; 3597773at2759; -.
DR TreeFam; TF300695; -.
DR Proteomes; UP000008143; Chromosome 7.
DR Bgee; ENSXETG00000005613; Expressed in mesonephros and 10 other cell types or tissues.
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 Gene3D; 1.10.287.1150; TPP helical domain; 1.
DR InterPro; IPR032106; 2-oxogl_dehyd_N.
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:SF5; 2-OXOGLUTARATE DEHYDROGENASE-LIKE, MITOCHONDRIAL; 1.
DR Pfam; PF16078; 2-oxogl_dehyd_N; 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:UP000008143};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 646..859
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 1018 AA; 115340 MW; BA499DB60BC84DD7 CRC64;
MSHLRTVAAK LKPYCTGLLV KHSSTPRTLP QRCSVYSSGA KEPFLSGTNS SYVEEMYYAW
LENPKSVHKS WDIFFQSADA GTPQCETRGV PSLTGIESKL QSLSSQGLAT APAKAEKIVE
EHLAVQSLIR AYQIRGHHVA QLDPLGILDA DLDSFVPSDL ITTLDKLGFY GLHEGDLDKV
FRLPTTTYIG GIDSTLSLRE IIRRLENSYC QHIGLEFMFI NDVEQCQWIR QKFETPGIMK
FTNEEKRTLL ARLVRSTRFE DFLARKWSSE KRFGLEGCEV MIPALKVIID KSSEMGLEYV
ILGMPHRGRL NVLANVIRKD LDQIFCQFDP KLEASDEGSG DVKYHLGMYH ERINRATNKK
ITLSLVANPS HLEAADPVVQ GKTKAEQFYR GDSQGNKVMS VLVHGDAAFA GQGVVYETFH
LSDLPSYTTN GTIHIVVNNQ IGFTTDPRMA RSSPYPTDVA RVVNAPIFHV NADDPEAVMY
VCSVAAEWRN TFNKDVVVDL VCYRRSGHNE MDEPMFTQPL MYKQIHKQVP VLKKYADKMI
AEGMVSLQEF EEEIAKYDRI CEEAYARSKD KKILNIKHWL DSPWPGFFTL DGEPKSMTCP
PTGIPEDLLS HIGNIASSVP VTDFKIHGGL SRILKSRLEM TKNRTVDWAL AEYMAFGSLL
KEGIHVRLSG QDVERGTFSH RHHVLHDQEV DRKTCVPMNH LWPNQAPYTV CNSSLSEYGV
LGFELGFAMA SPNALVLWEA QFGDFYNTAQ CIIDQFISSG QAKWVRHNGI VLLLPHGMEG
MGPEHSSARP ERFLQMSNDD SDAYPEFTND FEVCQLYDCN WIVVNCSTPA SYFHVLRRQI
LLPFRKPLII FTPKSLLRHP EAKSSFDDMN TGTNFQRVIP ENGAASHNPQ AVKRVIFCTG
KIYYELVKER HNKGLDNQVA ITRLEQLSPF PFDLVKQEAE KYATSELVWC QEEHKNMGYY
DYVKARFLTI LNHARPVWYV GRDPAAAPAT GNKNTHHVEL KRFLDVAFNL QYFEGKPF
//
