ID   A0A0K0GAE9_9FIRM        Unreviewed;       962 AA.
AC   A0A0K0GAE9;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   ORFNames=WH51_08710 {ECO:0000313|EMBL:KKE79144.1};
OS   Bacilli bacterium VT-13-104.
OC   Bacteria; Bacillota; Bacilli.
OX   NCBI_TaxID=1637974 {ECO:0000313|EMBL:KKE79144.1, ECO:0000313|Proteomes:UP000034981};
RN   [1] {ECO:0000313|Proteomes:UP000034981}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VT-13-104 {ECO:0000313|Proteomes:UP000034981};
RA   Tetz V., Tetz G.;
RT   "Bacilli bacterium VT-13-104.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKE79144.1}.
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DR   EMBL; LAZH01000034; KKE79144.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0K0GAE9; -.
DR   PATRIC; fig|1637974.4.peg.1832; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000034981; Unassembled WGS sequence.
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:0006096; P:glycolytic process; IEA:UniProtKB-KW.
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   HAMAP; MF_01169; SucA_OdhA; 1.
DR   InterPro; IPR032106; 2-oxogl_dehyd_N.
DR   InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR   InterPro; IPR023784; 2oxoglutarate_DH_E1_bac.
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   3: Inferred from homology;
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034981};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          606..801
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   962 AA;  109555 MW;  1ED33D3CB625BA37 CRC64;
     MGVFIVVVGL EESARGFWEQ FYGPNIGYVQ QQYELFKKDP EAVEPSIREI FEKYGSPEKL
     NQQNIENSTN IATPNAPSNF DVKKLTSALK LVEAIRRYGH LEADIYPVYQ HKDPMSHEID
     PETYGITEED LRNMPANWLW EQSPAGVENG LDVYNTLKKY YTGTITFEYD HVNNDEERKW
     LFDLIESGNA RLELSKEERI QLLERLAHVE GFELFLQKTF VGQKRFSIQG LEMMVPMLDE
     LVNFGNQDNV EDIMMGMAHR GRLSVLAHVL GKPIDKIFSE FHHSSDKELI PSDESSRKIN
     YGWTGDVKYH FGAQRIVKNG DHTTRVTLAH NPSHLEFVNP IVEGLARAAQ DDRSKAGYPK
     RDVDKAFSVL IHGDAAFIGE GVVAETLNLS GLPGYHTGGT VHIIANNLLG YTTDREDGRS
     TRYASDMAKG FEIPIIRVNA DDPISCMSAI KIAYEYRKKF KKDFLIDLVG YRRYGHNEMD
     EPRTTQPLLY KEIDNRPSVT YVYAASLEKN GYINEGDIKQ ITDKVEQEFR EIYNSMIEND
     SVDSEPTPMP SVLRNGLNKF ETGVELESLR KLNKDLLKRP EGFKGFKKTE RILKRREDAL
     EEGNKADWGT GEALAYASIL KDGIPIRITG QDTERGTFAH RHMVLYDVET GEKYCPLHGI
     EDAKATFEIR NSPLSEVAVL GFEYGYSIHS PETLVIWEAQ FGDFANVAQV MFDQFISSAR
     AKWGDKSNLV MLLPHGFEGQ GPEHSSARLE RFLQMAAENN WIIAYPTSSA QFFHLIRRQA
     KLGGEDVARP LVVMTPKSSM IRNPRMASEA AEFTDVKFKS LRNQPNFAIS KDAKRLLIGT
     GKIMVDIEET MDGSSENYDW LRIVRLEQIY PFPQKELEEI INELPNLEEI VWVQEEPRNM
     GAWDFVDDYV RPLLKDGQKI RYIGRPDRSA PAVGLPNVHK FEQNQIIQQA INPEGGKSSA
     RN
//