ID   F2NR08_MARHT            Unreviewed;       930 AA.
AC   F2NR08;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   OrderedLocusNames=Marky_1855 {ECO:0000313|EMBL:AEB12586.1};
OS   Marinithermus hydrothermalis (strain DSM 14884 / JCM 11576 / T1).
OC   Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Marinithermus.
OX   NCBI_TaxID=869210 {ECO:0000313|EMBL:AEB12586.1, ECO:0000313|Proteomes:UP000007030};
RN   [1] {ECO:0000313|EMBL:AEB12586.1, ECO:0000313|Proteomes:UP000007030}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14884 / JCM 11576 / T1 {ECO:0000313|Proteomes:UP000007030};
RX   PubMed=22675595; DOI=10.4056/sigs.2435521;
RA   Copeland A., Gu W., Yasawong M., Lapidus A., Lucas S., Deshpande S.,
RA   Pagani I., Tapia R., Cheng J.F., Goodwin L.A., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Pan C., Brambilla E.M., Rohde M., Tindall B.J., Sikorski J.,
RA   Goker M., Detter J.C., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Woyke T.;
RT   "Complete genome sequence of the aerobic, heterotroph Marinithermus
RT   hydrothermalis type strain (T1(T)) from a deep-sea hydrothermal vent
RT   chimney.";
RL   Stand. Genomic Sci. 6:21-30(2012).
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR   EMBL; CP002630; AEB12586.1; -; Genomic_DNA.
DR   RefSeq; WP_013704632.1; NC_015387.1.
DR   AlphaFoldDB; F2NR08; -.
DR   STRING; 869210.Marky_1855; -.
DR   KEGG; mhd:Marky_1855; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_0; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000007030; Chromosome.
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   NCBIfam; TIGR00239; 2oxo_dh_E1; 1.
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   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:AEB12586.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007030};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          589..782
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   REGION          49..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..70
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   930 AA;  104409 MW;  D1975B586CDEE580 CRC64;
     MARARDAQQW PETPNLLYIE ELYTTYQKDP TAVPPEWRQY FDALEHDLAR PVPAPPPRPA
     AQPAPRPAAA APSPAAMEAA GFQERVDELV EAYRELGHLA AQLDPLGSRR PEPAELDPAY
     YGFTEADLAR PVPEGIVPGV QLRTLGELVA HLRETYCRTI GVEFMHIDDS AARNWLIERM
     ESTANRTPLD AETRKRILAR LTEAAVFEEF VQKKYLGAKT FSLEGSETLI PLIDLAIEHA
     AERGVVEIVM AMAHRGRLNV LANIFKKPAR DIFLEFEEVF PEDYRGDVKY HLGYSSDHTT
     RTGKPVHLSL CFNPSHLEYI NTVALGRTRA KQDRFGDAAR TRGMALIVHG DAAFAGEGIV
     QETLNLSRLP AYEVGGTLHV IVNNQVGFTT SPEEGRSTLY ATDVAKMLQV PIFHVNGEDP
     EAVAHVVALA LEFRKTFHRD VVIDLYAFRR RGHNEADEPS FTQPLMYKAI ARHEPLYKRY
     RAQLVQEGVI REAEAEAIAR AYREHLEAEL EAAKREPTPP KPVGLGGIWN GYVGGLEKDV
     PDVDTGVKKR RLVEVLEGIT RVPQGFHLHP KLKRFMKQRE EMAQEKRPVD WATAEALAFG
     TLVTEGYRVR MSGQDSRRGT FSQRHAALYD YETGEPYIPL ANLAPDQAPF EIYNSPLSEA
     GVLGFEYGYS LDTPDGLVLW EAQFGDFVNV AQVIIDQFIA SAEAKWNRLS GLVMLLPHGL
     EGQGPEHSSA RLERFLMLAA ADNIQVTYPT TPAQYFHLLR RQVLRPWRKP LVVLTPKSLL
     RHPEATSPLE AFTQGRFRRV IPDAAANPEK VKKILLVSGK LYYELEAKRR AEGIEHVAIV
     RLEQLYPFPE AELEAALAPY KDGTPVVWVQ EEPVNMGAWP YLRMRFCQEI LGRFPLSGVS
     RPESASPATG SSRIHKLEQE RLLTEALKAE
//