OGDHL_PONAB
ID OGDHL_PONAB Reviewed; 1010 AA.
AC Q5R9L8; Q5R854;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 80.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain cortex, and Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-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. The presence of either ODGH/E1 or ODGHL/E1-
CC like isoenzyme in the complex may depend on its tissular distribution.
CC {ECO:0000250|UniProtKB:D3ZQD3}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q9ULD0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5R9L8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5R9L8-2; Sequence=VSP_029368;
CC -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAH91542.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CR859369; CAH91542.1; ALT_INIT; mRNA.
DR EMBL; CR859900; CAH92056.1; -; mRNA.
DR RefSeq; NP_001126195.1; NM_001132723.1.
DR RefSeq; NP_001128819.1; NM_001135347.1.
DR AlphaFoldDB; Q5R9L8; -.
DR SMR; Q5R9L8; -.
DR STRING; 9601.ENSPPYP00000002634; -.
DR GeneID; 100173162; -.
DR GeneID; 100189729; -.
DR KEGG; pon:100173162; -.
DR CTD; 55753; -.
DR eggNOG; KOG0450; Eukaryota.
DR InParanoid; Q5R9L8; -.
DR OrthoDB; 134699at2759; -.
DR Proteomes; UP000001595; Unplaced.
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 Alternative splicing; Calcium; Glycolysis; Metal-binding; Mitochondrion;
KW Oxidoreductase; Reference proteome; Thiamine pyrophosphate;
KW Transit peptide.
FT TRANSIT 1..73
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 74..1010
FT /note="2-oxoglutarate dehydrogenase-like, mitochondrial"
FT /id="PRO_0000310984"
FT BINDING 141
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q02218"
FT BINDING 143
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q02218"
FT BINDING 145
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q02218"
FT BINDING 166
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q02218"
FT BINDING 168
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q02218"
FT BINDING 170
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q02218"
FT VAR_SEQ 862
FT /note="V -> VSGP (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_029368"
FT CONFLICT 40
FT /note="L -> F (in Ref. 1; CAH92056)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="W -> R (in Ref. 1; CAH92056)"
FT /evidence="ECO:0000305"
FT CONFLICT 633
FT /note="I -> T (in Ref. 1; CAH92056)"
FT /evidence="ECO:0000305"
FT CONFLICT 657
FT /note="R -> H (in Ref. 1; CAH92056)"
FT /evidence="ECO:0000305"
FT CONFLICT 856
FT /note="F -> S (in Ref. 1; CAH92056)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1010 AA; 114621 MW; 1E4320855FEFDA43 CRC64;
MSQLRLLPSR LGAQAARLLA AHDIPVFGWR SRSSRPPATL PSSKGGGGSS YMEEMYFAWL
ENPRSVHKSW DSFFRKASEE AFSGSAQPRP PSVVHESRSA VSSRTKTSKL VEDHLAVQSL
IRAYQIRGHH VAQLDPLGIL DADLDSFVPS DLITTIDKLA FYDLQEADLD KEFQLPTTTF
IGGSENTLSL REIIRRLENT YCQHIGLEFM FINDVEQCQW IRQKFETPGV MQFSSEEKRT
LLARLVRSMR FEDFLARKWS SEKRFGLEGC EVMIPALKTI IDKSSEMGIE NVILGMPHRG
RLNVLANVIR KDLEQIFCQF DPKLEAADEG SGDVKYHLGM YHERINRVTN RNITLSLVAN
PSHLEAVDPV VQGKTKAEQF YRGDAQGKKV MSILVHGDAA FAGQGVVYET FHLSDLPSYT
TNGTVHVVVN NQIGFTTDPR MARSSPYPTD VARVVNAPIF HVNADDPEAV IYVCSVAAEW
RNTFNKDVVV DLVCYRRRGH NEMDEPMFTQ PLMYKQIHRQ VPVLKKYADK LIAEGTVTLQ
EFEEEIAKYD RICEEAYGRS KDKKILHIKH WLDSPWPGFF NVDGEPKSMT CPATGIPEDM
LTHIGSVASS VPLEDFKIHT GLSRILRGRA DMIKNRTVDW ALAEYMAFGS LLKEGIRVRL
SGQDVERGTF SHRHHVLHDQ EVDRRTCVPM NHLWPDQAPY TVCNSSLSEY GVLGFELGYA
MASPNALVLW EAQFGDFHNT AQCIIDQFIS TGQAKWVRHN GIVLLLPHGM EGMGPEHSSA
RPERFLQMSN DDSDAYPAFT KDFEVSQLYD CNWIVVNCST PANYFHVLRR QILLPFRKPL
IIFTPKSLLR HPEAKFSFDQ MVSGTSFQRV IPEDGAAARA PEQVRRLIFC TGKVYYDLVK
ERSSQGLEEK VAITRLEQIS PFPFDLIKQE AEKYPGAELA WCQEEHKNMG YYDYISPRFM
TILRRARPIW YVGRDPAAAP ATGNRNTHLV SLKKFLDTAF NLQAFEGKTF
