ID J4D9M6_THEOR Unreviewed; 1042 AA.
AC J4D9M6;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=2-oxoglutarate dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00040267};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
DE AltName: Full=2-oxoglutarate dehydrogenase complex component E1 {ECO:0000256|ARBA:ARBA00042984};
GN ORFNames=TOT_030000747 {ECO:0000313|EMBL:BAM41485.1};
OS Theileria orientalis strain Shintoku.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=869250 {ECO:0000313|EMBL:BAM41485.1, ECO:0000313|Proteomes:UP000003786};
RN [1] {ECO:0000313|EMBL:BAM41485.1, ECO:0000313|Proteomes:UP000003786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Shintoku {ECO:0000313|EMBL:BAM41485.1,
RC ECO:0000313|Proteomes:UP000003786};
RX PubMed=22951932;
RA Hayashida K., Hara Y., Abe T., Yamasaki C., Toyoda A., Kosuge T.,
RA Suzuki Y., Sato Y., Kawashima S., Katayama T., Wakaguri H., Inoue N.,
RA Homma K., Tada-Umezaki M., Yagi Y., Fujii Y., Habara T., Kanehisa M.,
RA Watanabe H., Ito K., Gojobori T., Sugawara H., Imanishi T., Weir W.,
RA Gardner M., Pain A., Shiels B., Hattori M., Nene V., Sugimoto C.;
RT "Comparative genome analysis of three eukaryotic parasites with differing
RT abilities to transform leukocytes reveals key mediators of Theileria-
RT induced leukocyte transformation.";
RL MBio 3:e00204-e00212(2012).
CC -!- FUNCTION: The 2-oxoglutarate dehydrogenase complex catalyzes the
CC overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It
CC contains multiple copies of three enzymatic components: 2-oxoglutarate
CC dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and
CC lipoamide dehydrogenase (E3). {ECO:0000256|ARBA:ARBA00037426}.
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 EMBL; AP011948; BAM41485.1; -; Genomic_DNA.
DR RefSeq; XP_009691786.1; XM_009693491.1.
DR AlphaFoldDB; J4D9M6; -.
DR STRING; 869250.J4D9M6; -.
DR EnsemblProtists; BAM41485; BAM41485; TOT_030000747.
DR GeneID; 20715900; -.
DR KEGG; tot:TOT_030000747; -.
DR VEuPathDB; PiroplasmaDB:TOT_030000747; -.
DR eggNOG; KOG0450; Eukaryota.
DR OrthoDB; 3597773at2759; -.
DR Proteomes; UP000003786; Chromosome 3.
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 PANTHER; PTHR23152:SF4; 2-OXOADIPATE DEHYDROGENASE COMPLEX COMPONENT E1; 1.
DR PANTHER; PTHR23152; 2-OXOGLUTARATE DEHYDROGENASE; 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:UP000003786};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 649..854
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 1042 AA; 117744 MW; A8C8A8FBA3A39960 CRC64;
MRFGLLRISQ NLRQFVNFNG ESSNYLEYLY YVYRTDPNHL QKSWQNYFSF LEQGKNYPVH
HFDRNVIFKN IPLFSNQATS QASELISKVA EGVTGPEVLK LNELASAYRT YGHLVSTVDP
LNLPKRIPFF RVVEGMEERL NIKNYKLTPE ELAKTVPNLG LGGIFNTQGT VQSQIDKLRE
RYCGNISFEF GHISNSQAVA FLIDQIESDN FLNLSKEESL GCFKSICRAV KFEQFCAKAF
PTLKRFGMDG MESLLVLLES IEKSSREFGA NSILMTMSHR GRLGVLSNFL NKPLEESFAE
FRGANWFVDS NFRSGDVKYH NGYTCVKDGL DIQMISNSSH LQFSHPVLTG LVKAKQHFEN
DAKKDKTVPI AIHGNSAISG QGMPYEVVQM SKIKGFTVGG TINIVVNNQI GFTASPMEAS
SSRYPTDVAK VVEAPVIHVN AYSIEGVVFA GRLACLYRQK FHTDVFINLV GFRRFGHNEL
DMPKFTNAEM YNKVDQVPNL MVYYKKYLNT KMGIDMEELD KIENATGSDF QKSLDLSKSI
ERIKEPIQNE NWRDILTLIE GFYVDNSLHN RVMQRIEASK KGAQASSAVA DNGNQLTLNP
QVLRTGLDHD LLLKLGLKCT TIPEEIKLHN SIKKIFDQRL QALNSGTGID TAISEVLAFS
SLSHDGFHVR LSGQESKRGT FSHRHAQVQC QDTFKYYNVF EGMDVRILNS YLSELAAVGF
EYGYSLYSPK TLNIWEAQFG DFVNGAQVII DAFITSAETK WNYFSGVVMF LPHGYDGQGP
DHSSCRVERF LQSSNDSEDL SDNLGLGEDY AKLVNISVVN CSVASNLFHV LRRQMHRPYR
KPLICVTGKK LLKLRGAFSN LSEFETGTFF QRYIPDPLFN PNIMEHLYKG APGAGKAGGS
SKADVKQLDK VHKVILCSGQ IYYDLLEFRE NNKEAQKNLE HVAIARLEEI TPFPAQWVLD
DLRLYRNLKT VVWCQEEHEN GGCYYFVRER LNGLLKILRD DYGSKVDAAV KYAGRLPCAT
TAVGDPKTHN EEHALVQGAF YL
//
