ID   Q0I3A6_HISS1            Unreviewed;       931 AA.
AC   Q0I3A6;
DT   03-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   Name=sucA {ECO:0000313|EMBL:ABI25234.1};
GN   OrderedLocusNames=HS_0959 {ECO:0000313|EMBL:ABI25234.1};
OS   Histophilus somni (strain 129Pt) (Haemophilus somnus).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Histophilus.
OX   NCBI_TaxID=205914 {ECO:0000313|EMBL:ABI25234.1};
RN   [1] {ECO:0000313|EMBL:ABI25234.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=129PT {ECO:0000313|EMBL:ABI25234.1};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA   Dalin E., Tice H., Pitluck S., Brettin T.S., Bruce D., Challacombe J.F.,
RA   Chertkov O., Detter J.C., Gilna P., Han S., Misra M., Tapia R.,
RA   Thayer N.N., Xie G., Inzana T.J., Duncan A.J., Siddaramppa S.,
RA   Richardson P.;
RT   "Complete genome sequence of Haemophilus somnus 129PT.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: E1 component of the 2-oxoglutarate dehydrogenase (OGDH)
CC       complex which catalyzes the decarboxylation of 2-oxoglutarate, the
CC       first step in the conversion of 2-oxoglutarate to succinyl-CoA and
CC       CO(2). {ECO:0000256|ARBA:ARBA00003906}.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR   EMBL; CP000436; ABI25234.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0I3A6; -.
DR   KEGG; hso:HS_0959; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_6; -.
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:ABI25234.1};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          591..784
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   931 AA;  106010 MW;  A50F155829E93408 CRC64;
     MKKNSPISEW LASSALGGAN QSYVEDLYED YLDNPQAVDE SWQQVFNSLP KQNALEQPHS
     KVRDYFKRLA RDTSQNGVGV IDPNVSARLV NVLKWINGHR NRGHLHADLD PLKMWQRMEA
     PTLDYKFYGF SDNDLDEVFD IGGYVYNKEQ ISLRDLADSL KKTYCSTIGL EFMHVNDLDA
     RTWLQRKVER LLDKPLFTRE EQLKFLEELI AADGLERYLG AKFPGAKRFS LEGSDAFILL
     MKEMIRHSSR NGVKEIVMGM AHRGRLNLLV NVLGKKPSEL FDEFAGKHSG SGTGDVKYHQ
     GFSSDFMTDD GIVHLALAFN PSHLEIVNPV VLGSVRARQN RIQDVERSQV LPITVHGDSA
     VAGQGIVQET LNMSEVRGYT VGGTIRVVIN NQIGFTTSNL QDTRSTEYCT DIAKMIEAPV
     IHVNGDDPEA VAYAARMAVE FRAKFKRDIF IDLVSYRRHG HNEADEPAVT QPLMYERIRK
     HPTPPKVYTN RLVTEGIIDE AYAIELANKY RDALDNGGCV VPEWREADIE TKDWTKYLTQ
     EWTEYDGSFD SERFVGLAKK VCDYPSSHSL HPRVKKLYDD RLSMAQGDKL FDWGMAETMA
     YATLLDEGYN VRLSGEDAGR GTFFHRHSVL HNQKDATLYI PLTQLHAQQG RFEVWDSVLS
     EEAVLAYEYG YATAAPRTLT IWEAQFGDFA NVAQVVIDQF ISSGEQKWGR MCGLVMLLPH
     GYEGQGPEHS SARLERYLQL CAQQNMQVCV PSTPAQIYHL LRRQMLRKVR RPLVVITPKS
     LLRRPLVVST MEELIHGKYQ NVIAEIDAID PQKVRRVVMC SGKVYYDLLE QRRENNQMDV
     AIIRIEQLYP YPHEEMKEAL APYSHVTDYV WCQEEPLNQG AWYCCQHNFW TSLPPHGKLR
     YVGRPASASP AVGYLSLHNE QQRALVTEAL A
//