ID   H8KC99_RICMS            Unreviewed;       928 AA.
AC   H8KC99;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000256|ARBA:ARBA00013321};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
DE   AltName: Full=Alpha-ketoglutarate dehydrogenase {ECO:0000256|ARBA:ARBA00030680};
GN   Name=sucA {ECO:0000313|EMBL:AFC73890.1};
GN   OrderedLocusNames=MCI_05375 {ECO:0000313|EMBL:AFC73890.1};
OS   Rickettsia montanensis (strain OSU 85-930).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=1105114 {ECO:0000313|EMBL:AFC73890.1, ECO:0000313|Proteomes:UP000008008};
RN   [1] {ECO:0000313|Proteomes:UP000008008}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OSU 85-930 {ECO:0000313|Proteomes:UP000008008};
RA   Johnson S.L., Munk A.C., Han S., Bruce D.C., Dasch G.A.;
RT   "Complete genome sequence of Rickettsia montanensis strain OSU 85-930.";
RL   Submitted (FEB-2012) 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};
CC   -!- SUBUNIT: Homodimer. Part of the 2-oxoglutarate dehydrogenase (OGDH)
CC       complex composed of E1 (2-oxoglutarate dehydrogenase), E2
CC       (dihydrolipoamide succinyltransferase) and E3 (dihydrolipoamide
CC       dehydrogenase); the complex contains multiple copies of the three
CC       enzymatic components (E1, E2 and E3). {ECO:0000256|ARBA:ARBA00011301}.
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DR   EMBL; CP003340; AFC73890.1; -; Genomic_DNA.
DR   RefSeq; WP_014409955.1; NC_017043.1.
DR   AlphaFoldDB; H8KC99; -.
DR   KEGG; rmo:MCI_05375; -.
DR   HOGENOM; CLU_004709_1_0_5; -.
DR   Proteomes; UP000008008; 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: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   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   Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:AFC73890.1};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          585..778
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   928 AA;  103858 MW;  893ABFE2FA87F900 CRC64;
     MEEDLKKTGY LFGGNAVFVE ELYKQYLANP ASVDQTWQEF FAGIKDNNTL LNKSTAKIII
     PDEIKKESLN NNLSSEDLNS LKAKEMINAY RKHAHYLANL DPLGLELRKT KNDLKLNIET
     FGLDSGQLEE NINITDEFVG TWNCKLSELV TKFDKVYTGS IGVEFEQIEN VEGKNWLYNK
     LESEVTFSSE DKKTILNDLV EVEGFEQYLH TKFPGAKRFS VEGGDASIVA MSKAIDLSMH
     QGVSEIVIGM AHRGRLNTLT KVVGKPYKAV IAGFISGSVF PDELNISGDV KYHLGYSSDR
     TLEDKKIHLS LAYNPSHLEA VNPIVAGKVR AKQDILGDTK RSKVKAILVH GDAAFCGQGV
     VAESLSMSPL AAYDIGGILH FVINNQLGFT ANTADTRASR YSTEFAKIIA APILHVNGDD
     IEAVLKATNI AVEYRQKFGK DVVVEIICYR KYGHNEGDEP MYTQGKMYNI IKNKLTPGNI
     YANELVKSGV IDNNYFAKLK EEFKAKLDKE YEQAKSYKQE AHFLGGLWQG ISRTRTQATI
     TGISKKILHD LGTKLCEIPK DFAVNPKLVK LFKARKATLT ADQPIDWATA EQLAFASLLA
     SGTNIRLTGQ DSGRGTFSHR HSVLHNQIDD TTYIPLNNLS KEQAKYEVAD SNLSEYATLG
     FEYGYSLANP KNLVLWEAQF GDFANGAQII FDQFISSSET KWLRMSGLVV LLPHAFEGQG
     PEHSSARLER FLQLAAENNM YVTYPTTPAS IFHLLRRQIL DDTRKPLIVM SPKSLLRHKY
     AVSKLDELGE NTTFLPVLDE VTKVDTNNIT KVILCSGKVY YDLFEMRGNN SNIAIIRLEQ
     LYPFEKKLVA SLLKKYNRTQ EFIWCQEEPK NMGTWCYIVS HLNDALKEAG INNEFKYVGR
     AESASPAVGS LQAHNKQQEK LLRAALGI
//