OGDHL_RAT
ID OGDHL_RAT Reviewed; 1010 AA.
AC D3ZQD3;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2015, sequence version 2.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=2-oxoglutarate dehydrogenase-like, mitochondrial {ECO:0000303|PubMed:18783430};
DE EC=1.2.4.2 {ECO:0000305|PubMed:18783430};
DE AltName: Full=2-oxoglutarate dehydrogenase complex component E1-like {ECO:0000303|PubMed:18783430};
DE Short=OGDC-E1-like {ECO:0000303|PubMed:18783430};
DE AltName: Full=Alpha-ketoglutarate dehydrogenase-like;
DE Flags: Precursor;
GN Name=Ogdhl {ECO:0000312|RGD:1310916};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND TISSUE SPECIFICITY.
RX PubMed=18783430; DOI=10.1111/j.1742-4658.2008.06632.x;
RA Bunik V., Kaehne T., Degtyarev D., Shcherbakova T., Reiser G.;
RT "Novel isoenzyme of 2-oxoglutarate dehydrogenase is identified in brain,
RT but not in heart.";
RL FEBS J. 275:4990-5006(2008).
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 (PubMed:18783430). The OGDHC complex catalyzes the overall
CC conversion of 2-oxoglutarate to succinyl-CoA and CO(2) while reducing
CC NAD(+) to NADH (PubMed:18783430). The OGDHC complex is mainly active in
CC the mitochondrion (PubMed:18783430). Involved in the inhibition of cell
CC proliferation and in apoptosis (By similarity).
CC {ECO:0000250|UniProtKB:Q9ULD0, ECO:0000305|PubMed:18783430}.
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:0000305|PubMed:18783430};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12189;
CC Evidence={ECO:0000305|PubMed:18783430};
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) (Probable). OGDHL/E1-like isoenzyme may replace
CC OGDH in the OGDHC complex in the brain. The presence of either ODGH/E1
CC or ODGHL/E1-like isoenzyme in the complex may depend on its tissular
CC distribution (Probable). {ECO:0000305|PubMed:18783430}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q9ULD0}.
CC -!- TISSUE SPECIFICITY: The OGDHL-containing OGDHC complex is present in
CC the brain, but not in the heart. {ECO:0000269|PubMed:18783430}.
CC -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AABR07024604; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006252646.1; XM_006252584.3.
DR AlphaFoldDB; D3ZQD3; -.
DR SMR; D3ZQD3; -.
DR STRING; 10116.ENSRNOP00000027054; -.
DR jPOST; D3ZQD3; -.
DR PaxDb; D3ZQD3; -.
DR PeptideAtlas; D3ZQD3; -.
DR PRIDE; D3ZQD3; -.
DR GeneID; 290566; -.
DR UCSC; RGD:1310916; rat.
DR CTD; 55753; -.
DR RGD; 1310916; Ogdhl.
DR VEuPathDB; HostDB:ENSRNOG00000019955; -.
DR eggNOG; KOG0450; Eukaryota.
DR HOGENOM; CLU_004709_1_1_1; -.
DR InParanoid; D3ZQD3; -.
DR OMA; IMIDQYI; -.
DR OrthoDB; 134699at2759; -.
DR TreeFam; TF300695; -.
DR Proteomes; UP000002494; Chromosome 16.
DR Bgee; ENSRNOG00000019955; Expressed in frontal cortex and 18 other tissues.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IBA:GO_Central.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0006103; P:2-oxoglutarate metabolic process; IDA:UniProtKB.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IDA: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 1: Evidence at protein level;
KW Calcium; Glycolysis; Metal-binding; Mitochondrion; Oxidoreductase;
KW Reference proteome; Thiamine pyrophosphate; Transit peptide.
FT TRANSIT 1..107
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 108..1010
FT /note="2-oxoglutarate dehydrogenase-like, mitochondrial"
FT /evidence="ECO:0000255"
FT /id="PRO_0000452343"
FT REGION 28..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
SQ SEQUENCE 1010 AA; 114637 MW; 358F47023F46C534 CRC64;
MSQLRLLLFR LGPQARKLLA TRDIAAFGGR RRSSGPPTTI PRSRGGVSPS YVEEMYFAWL
ENPQSVHKSW DNFFQRATKE ASVGPAQPQP PAVIQESRAS VSSCTKTSKL VEDHLAVQSL
IRAYQIRGHH VAQLDPLGIL DADLDSFVPS DLITTIDKLA FYDLQEADLD KEFRLPTTTF
IGGSENTLSL REIIRRLEST YCQHIGLEFM FINDVEQCQW IRQKFETPGV MKFSIEEKRT
LLARLVRSMR FEDFLARKWS SEKRFGLEGC EVMIPALKTI IDKSSEMGVE NVILGMPHRG
RLNVLANVIR KDLEQIFCQF DPKLEAADEG SGDVKYHLGM YHERINRVTN RNITLSLVAN
PSHLEAVDPV VQGKTKAEQF YRGDAQGRKV MSILVHGDAA FAGQGVVYET FHLSDLPSYT
TNGTVHVVVN NQIGFTTDPR MARSSPYPTD VARVVNAPIF HVNADDPEAV IYVCSVAAEW
RNTFNKDVVV DLVCYRRRGH NEMDEPMFTQ PLMYKQIHKQ VPVLKKYADK LIAEGTVTLQ
EFEEEIAKYD RICEEAYGRS KDKKILHIKH WLDSPWPGFF NVDGEPKSMT YPTTGIPEDT
LSHIGNVASS VPLEDFKIHT GLSRILRGRA DMTKKRTVDW ALAEYMAFGS LLKEGIHVRL
SGQDVERGTF SHRHHVLHDQ DVDRRTCVPM NHLWPDQAPY TVCNSSLSEY GVLGFELGYA
MASPNALVLW EAQFGDFHNT AQCIIDQFIS TGQAKWVRHN GIVLLLPHGM EGMGPEHSSA
RPERFLQMSN DDSDAYPVFT EDFEVSQLYD CNWIVVNCST PASYFHVLRR QVLLPFRKPL
IVFTPKSLLR HPDAKSSFDQ MVSGTSFQRM IPEDGPAAQS PERVERLIFC TGKVYYDLVK
ERSSQGLEKQ VAITRLEQIS PFPFDLIMRE AEKYSGAELV WCQEEHKNMG YYDYISPRFM
TLLGHSRPIW YVGREPAAAP ATGNKNTHLV SLRKFLDTAF NLKAFEGKTF
