OGDHL_XENLA
ID OGDHL_XENLA Reviewed; 1018 AA.
AC Q68EW0;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=2-oxoglutarate dehydrogenase-like, mitochondrial {ECO:0000250|UniProtKB:D3ZQD3};
DE EC=1.2.4.2 {ECO:0000250|UniProtKB:D3ZQD3};
DE AltName: Full=2-oxoglutarate dehydrogenase complex component E1-like {ECO:0000250|UniProtKB:D3ZQD3};
DE Short=OGDC-E1-like {ECO:0000250|UniProtKB:D3ZQD3};
DE AltName: Full=Alpha-ketoglutarate dehydrogenase-like;
DE Flags: Precursor;
GN Name=ogdhl;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: 2-oxoglutarate dehydrogenase (E1-like) component of the 2-
CC oxoglutarate dehydrogenase multienzyme complex (OGDHC) which mediates
CC the decarboxylation of alpha-ketoglutarate in the tricarboxylic acid
CC cycle. The OGDHC complex catalyzes the overall conversion of 2-
CC oxoglutarate to succinyl-CoA and CO(2) while reducing NAD(+) to NADH.
CC The OGDHC complex is mainly active in the mitochondrion (By
CC similarity). Involved in the inhibition of cell proliferation and in
CC apoptosis (By similarity). {ECO:0000250|UniProtKB:D3ZQD3,
CC ECO:0000250|UniProtKB:Q9ULD0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue
CC succinyltransferase] + 2-oxoglutarate + H(+) = (R)-N(6)-(S(8)-
CC succinyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue
CC succinyltransferase] + CO2; Xref=Rhea:RHEA:12188, Rhea:RHEA-
CC COMP:10483, Rhea:RHEA-COMP:10484, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:83099,
CC ChEBI:CHEBI:83120; EC=1.2.4.2;
CC Evidence={ECO:0000250|UniProtKB:D3ZQD3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12189;
CC Evidence={ECO:0000250|UniProtKB:D3ZQD3};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250|UniProtKB:Q02218};
CC -!- SUBUNIT: The OGDHC complex comprises multiple copies of three catalytic
CC enzyme components, the 2-oxoglutarate dehydrogenase (OGDH/E1), the
CC dihydrolipoamide dehydrogenase (DLST/E2) and the dihydrolipoamide
CC dehydrogenase (DLD/E3). OGDHL/E1-like isoenzyme may replace OGDH in the
CC OGDHC complex in the brain. {ECO:0000250|UniProtKB:D3ZQD3}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q9ULD0}.
CC -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; BC080090; AAH80090.1; -; mRNA.
DR RefSeq; NP_001087546.1; NM_001094077.1.
DR AlphaFoldDB; Q68EW0; -.
DR SMR; Q68EW0; -.
DR MaxQB; Q68EW0; -.
DR GeneID; 447370; -.
DR KEGG; xla:447370; -.
DR CTD; 447370; -.
DR Xenbase; XB-GENE-984155; ogdhl.L.
DR OrthoDB; 134699at2759; -.
DR Proteomes; UP000186698; Chromosome 7L.
DR Bgee; 447370; Expressed in muscle tissue and 20 other tissues.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0006103; P:2-oxoglutarate metabolic process; ISS:UniProtKB.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; ISS:UniProtKB.
DR Gene3D; 3.40.50.11610; -; 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 PANTHER; PTHR23152; PTHR23152; 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; SSF52518; 2.
DR TIGRFAMs; TIGR00239; 2oxo_dh_E1; 1.
PE 2: Evidence at transcript level;
KW Calcium; Glycolysis; Metal-binding; Mitochondrion; Oxidoreductase;
KW Reference proteome; Thiamine pyrophosphate; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 74..1018
FT /note="2-oxoglutarate dehydrogenase-like, mitochondrial"
FT /id="PRO_0000310985"
FT BINDING 149
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q02218"
FT BINDING 151
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q02218"
FT BINDING 153
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q02218"
FT BINDING 174
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q02218"
FT BINDING 176
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q02218"
FT BINDING 178
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q02218"
SQ SEQUENCE 1018 AA; 115597 MW; 618973B4003CE6FE CRC64;
MSHLRSVAAK LKPYCTGLLV KHNSILRTLP PRCYVYSSGA KEPFLSGTNS SYVEEMYYAW
LENPKSVHKS WDAFFRSADN GTPQCEIQGV PSLADIESKL PSLSSQGLAT APAKAEKIVE
EHLAVQSLIR AYQIRGHHVA QLDPLGILDA DLDSFVPSDL ITTLDKLGFY GLHEGDLDKV
FRLPTTTYIG GTDSTLSLRE IIRRLENSYC QHIGLEFMFI NDVEQCQWIR QKFETPGIMK
FINEEKRTLL ARLIRSTRFE DFLARKWSSE KRFGLEGCEV MIPALKAIID KSSEMGLEYV
ILGMPHRGRL NVLANVIRKD LDQIFCQFDP KLEASDEGSG DVKYHLGMYH ERINRATNKK
ITLSLVANPS HLEAVDPVVQ GKTKAEQFYR GDTEGNKVMS ILVHGDAAFA GQGVVYETFH
LSDLPSYTTN GTIHIVVNNQ IGFTTDPRMA RSSPYPTDVA RVVNAPIFHV NADDPEAVMY
VCSVAAEWRN TFNKDVVVDL VCYRRSGHNE MDEPMFTQPL MYKQIHKQVP VLKKYADKMI
AEGTVTLQEF EEEIAKYDRI CEEAYARSKD KKILNIKHWL DSPWPGFFTL DGEPKSMTCP
PTGIPEDMLS HIGAIASSVP LKDFKIHGGL SRILKSRLEM TNSRTVDWAL AEYMTFGSLL
KEGIHVRLSG QDVERGTFSH RHHVLHDQEV DRWTCVPMNH LWPNQAPYTV CNSSLSEYGV
LGFELGFAMA SPNALVLWEA QFGDFYNTAQ CIIDQFISSG QAKWVRHNGI VLLLPHGMEG
MGPEHSSARP ERFLQMSNDD SDAYPEFTQD FDVSQLFDCN WIVVNCSNPA SYFHVLRRQI
LLPFRKPLII FTPKSLLRHP EAKSSFDDMK TGTNFQRVIP ENGAASHSPQ EVKRVIFCTG
KVYYELVKER HRKGLDSQVA ITRLEQISPF PFDLVKQEAE KYATSELVWC QEEHKNMGYY
DYVKARFLTI LNHARPVWYV GRDPAAAPAT GNKNTHHVEL RRFLDIAFDL EYFEGKPF
