LOCUS       NP_001017461            1023 aa            linear   ROD 27-APR-2025
DEFINITION  2-oxoglutarate dehydrogenase complex component E1 precursor [Rattus
            norvegicus].
ACCESSION   NP_001017461 XP_573650
VERSION     NP_001017461.1
DBSOURCE    REFSEQ: accession NM_001017461.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1023)
  AUTHORS   Artiukhov,A.V., Grabarska,A., Gumbarewicz,E., Aleshin,V.A.,
            Kahne,T., Obata,T., Kazantsev,A.V., Lukashev,N.V., Stepulak,A.,
            Fernie,A.R. and Bunik,V.I.
  TITLE     Synthetic analogues of 2-oxo acids discriminate metabolic
            contribution of the 2-oxoglutarate and 2-oxoadipate dehydrogenases
            in mammalian cells and tissues
  JOURNAL   Sci Rep 10 (1), 1886 (2020)
   PUBMED   32024885
  REMARK    GeneRIF: Synthetic analogues of 2-oxo acids discriminate metabolic
            contribution of the 2-oxoglutarate and 2-oxoadipate dehydrogenases
            in mammalian cells and tissues.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1023)
  AUTHORS   Wang,Y., Guo,Y.R., Liu,K., Yin,Z., Liu,R., Xia,Y., Tan,L., Yang,P.,
            Lee,J.H., Li,X.J., Hawke,D., Zheng,Y., Qian,X., Lyu,J., He,J.,
            Xing,D., Tao,Y.J. and Lu,Z.
  TITLE     KAT2A coupled with the alpha-KGDH complex acts as a histone H3
            succinyltransferase
  JOURNAL   Nature 552 (7684), 273-277 (2017)
   PUBMED   29211711
REFERENCE   3  (residues 1 to 1023)
  AUTHORS   Tsepkova,P.M., Artiukhov,A.V., Boyko,A.I., Aleshin,V.A.,
            Mkrtchyan,G.V., Zvyagintseva,M.A., Ryabov,S.I., Ksenofontov,A.L.,
            Baratova,L.A., Graf,A.V. and Bunik,V.I.
  TITLE     Thiamine Induces Long-Term Changes in Amino Acid Profiles and
            Activities of 2-Oxoglutarate and 2-Oxoadipate Dehydrogenases in Rat
            Brain
  JOURNAL   Biochemistry (Mosc) 82 (6), 723-736 (2017)
   PUBMED   28601082
  REMARK    GeneRIF: Thiamine Induces Long-Term Changes in Amino Acid Profiles
            and Activities of 2-Oxoglutarate and 2-Oxoadipate Dehydrogenases in
            Rat Brain
REFERENCE   4  (residues 1 to 1023)
  AUTHORS   Denton,R.M., Pullen,T.J., Armstrong,C.T., Heesom,K.J. and
            Rutter,G.A.
  TITLE     Calcium-insensitive splice variants of mammalian E1 subunit of
            2-oxoglutarate dehydrogenase complex with tissue-specific patterns
            of expression
  JOURNAL   Biochem J 473 (9), 1165-1178 (2016)
   PUBMED   26936970
  REMARK    GeneRIF: Tissue-specific expression of OGDH splice variants may
            thus provide a mechanism that tunes the control of the enzyme to
            the specialized metabolic and signalling needs of individual cell
            types
REFERENCE   5  (residues 1 to 1023)
  AUTHORS   Quinlan,C.L., Goncalves,R.L., Hey-Mogensen,M., Yadava,N.,
            Bunik,V.I. and Brand,M.D.
  TITLE     The 2-oxoacid dehydrogenase complexes in mitochondria can produce
            superoxide/hydrogen peroxide at much higher rates than complex I
  JOURNAL   J Biol Chem 289 (12), 8312-8325 (2014)
   PUBMED   24515115
  REMARK    GeneRIF: H2O2 production from Ogdh can be considerable but may
            previously have been misattributed to complex I.
REFERENCE   6  (residues 1 to 1023)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   7  (residues 1 to 1023)
  AUTHORS   Sheu,K.F. and Blass,J.P.
  TITLE     The alpha-ketoglutarate dehydrogenase complex
  JOURNAL   Ann N Y Acad Sci 893, 61-78 (1999)
   PUBMED   10672230
  REMARK    Review article
REFERENCE   8  (residues 1 to 1023)
  AUTHORS   Bruschi,S.A., Lindsay,J.G. and Crabb,J.W.
  TITLE     Mitochondrial stress protein recognition of inactivated
            dehydrogenases during mammalian cell death
  JOURNAL   Proc Natl Acad Sci U S A 95 (23), 13413-13418 (1998)
   PUBMED   9811814
REFERENCE   9  (residues 1 to 1023)
  AUTHORS   Andersson,U., Leighton,B., Young,M.E., Blomstrand,E. and
            Newsholme,E.A.
  TITLE     Inactivation of aconitase and oxoglutarate dehydrogenase in
            skeletal muscle in vitro by superoxide anions and/or nitric oxide
  JOURNAL   Biochem Biophys Res Commun 249 (2), 512-516 (1998)
   PUBMED   9712727
REFERENCE   10 (residues 1 to 1023)
  AUTHORS   Ono,K., Hakozaki,M., Kimura,A. and Kochi,H.
  TITLE     Purification, resolution, and reconstitution of rat liver
            branched-chain alpha-keto acid dehydrogenase complex
  JOURNAL   J Biochem 101 (1), 19-27 (1987)
   PUBMED   3571202
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083811.1.
            
            On Apr 29, 2005 this sequence version replaced XP_573650.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083811.1, FQ222842.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1023
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="14"
                     /map="14q21"
     Protein         1..1023
                     /product="2-oxoglutarate dehydrogenase complex component
                     E1 precursor"
                     /EC_number="1.2.4.2"
                     /note="2-oxoglutarate dehydrogenase E1 component,
                     mitochondrial; 2-oxoglutarate dehydrogenase,
                     mitochondrial; alpha-ketoglutarate dehydrogenase; OGDC-E1;
                     2-oxoglutarate dehydrogenase complex component E1;
                     2-oxoglutarate dehydrogenase, mitochondrial-like;
                     oxoglutarate dehydrogenase (lipoamide); oxoglutarate
                     (alpha-ketoglutarate) dehydrogenase (lipoamide);
                     alpha-KGDH-E1; thiamine diphosphate (ThDP)-dependent
                     2-oxoglutarate dehydrogenase"
                     /calculated_mol_wt=111687
     transit_peptide 1..40
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q5XI78.1)"
                     /calculated_mol_wt=4627
     mat_peptide     41..1023
                     /product="2-oxoglutarate dehydrogenase complex component
                     E1. /id=PRO_0000271367"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI78.1)"
                     /calculated_mol_wt=111687
     Region          49..1016
                     /region_name="SucA"
                     /note="2-oxoglutarate dehydrogenase complex, dehydrogenase
                     (E1) component, and related enzymes [Energy production and
                     conversion]; COG0567"
                     /db_xref="CDD:440333"
     Site            100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q60597; propagated from
                     UniProtKB/Swiss-Prot (Q5XI78.1)"
     Site            401
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q60597; propagated from
                     UniProtKB/Swiss-Prot (Q5XI78.1)"
     Site            970
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q02218; propagated from
                     UniProtKB/Swiss-Prot (Q5XI78.1)"
     CDS             1..1023
                     /gene="Ogdh"
                     /gene_synonym="E1o; OGDH-E1"
                     /coded_by="NM_001017461.1:79..3150"
                     /db_xref="GeneID:360975"
                     /db_xref="RGD:1561359"
ORIGIN      
        1 mfhlrtcaak lrpltasqtv ktfsqnkpaa irtfqqircy sapvaaepfl sgtssnyvee
       61 mycawlenpk svhkswdiff rntnagappg tayqsplsls rsslatmaha qslveaqpnv
      121 dklvedhlav qslirayqir ghhvaqldpl gildadldss vpadiisstd klgfyglhes
      181 dldkvfhlpt ttfiggqepa lplreiirrl emaycqhigv efmfindleq cqwirqkfet
      241 pgimqftnee krtllarlvr strfeeflqr kwssekrfgl egcevlipal ktiidmssan
      301 gvdyvimgmp hrgrlnvlan virkeleqif cqfdskleaa degsgdmkyh lgmyhrrinr
      361 vtdrnitlsl vanpshleaa dpvvmgktka eqfycgdteg kkvmsillhg daafagqgiv
      421 yetfhlsdlp sytthgtvhv vvnnqigftt dprmarsspy ptdvarvvna pifhvnsddp
      481 eavmyvckva aewrntfhkd vvvdlvcyrr nghnemdepm ftqplmykqi rkqkpvlqky
      541 aellvsqgvv nqpeyeeeis kydkiceeaf trskdekilh ikhwldspwp gfftldgqpr
      601 smtcpstgle edilthignv assvpvenft ihgglsrilk trrelvtnrt vdwalaeyma
      661 fgsllkegih vrlsgqdver gtfshrhhvl hdqnvdkrtc ipmnhlwpnq apytvcnssl
      721 seygvlgfel gfamaspnal vlweaqfgdf nnmaqciidq ficpgqakwv rqngivlllp
      781 hgmegmgpeh ssarperflq mcnddpdvlp nlqeenfdis qlydcnwivv ncstpgnffh
      841 vlrrqillpf rkplivftpk sllrhpeart sfdemlpgth fqrvipedgp aaqnpdkvkr
      901 llfctgkvyy dltrerkard maeevaitri eqlspfpfdl llkeaqkypn aelawcqeeh
      961 knqgyydyvk prlrttidra kpvwyagrdp aaapatgnkk thltelqrfl dtafdldafk
     1021 kfs
//
