ID   ODO1_SHOC1              Reviewed;         943 AA.
AC   Q5WG56;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   27-MAR-2024, entry version 105.
DE   RecName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000255|HAMAP-Rule:MF_01169};
DE            EC=1.2.4.2 {ECO:0000255|HAMAP-Rule:MF_01169};
DE   AltName: Full=Alpha-ketoglutarate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01169};
GN   Name=odhA {ECO:0000255|HAMAP-Rule:MF_01169};
GN   OrderedLocusNames=ABC2114;
OS   Shouchella clausii (strain KSM-K16) (Alkalihalobacillus clausii).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Shouchella.
OX   NCBI_TaxID=66692;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSM-K16;
RA   Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y.,
RA   Kawai S., Ito S., Horikoshi K.;
RT   "The complete genome sequence of the alkaliphilic Bacillus clausii KSM-
RT   K16.";
RL   Submitted (OCT-2003) 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:0000255|HAMAP-Rule:MF_01169}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-
CC         [dihydrolipoyllysine-residue succinyltransferase] = CO2 + N(6)-[(R)-
CC         S(8)-succinyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC         succinyltransferase]; Xref=Rhea:RHEA:12188, Rhea:RHEA-COMP:10483,
CC         Rhea:RHEA-COMP:10484, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:83099, ChEBI:CHEBI:83120; EC=1.2.4.2;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01169};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01169};
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:0000255|HAMAP-
CC       Rule:MF_01169}.
CC   -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01169}.
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DR   EMBL; AP006627; BAD64649.1; -; Genomic_DNA.
DR   RefSeq; WP_011246957.1; NC_006582.1.
DR   AlphaFoldDB; Q5WG56; -.
DR   SMR; Q5WG56; -.
DR   STRING; 66692.ABC2114; -.
DR   KEGG; bcl:ABC2114; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_9; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000001168; Chromosome.
DR   GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
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   HAMAP; MF_01169; SucA_OdhA; 1.
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; 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; Oxidoreductase; Reference proteome; Thiamine pyrophosphate.
FT   CHAIN           1..943
FT                   /note="2-oxoglutarate dehydrogenase E1 component"
FT                   /id="PRO_0000162168"
SQ   SEQUENCE   943 AA;  106584 MW;  3FF67A61E3A2C6D8 CRC64;
     MSSKEHSPEK PWRGFYGPNL GAVIELYDQY VEDPNSVDEQ TRAHFEKWGP PALEENVSSS
     NAKETIGADM ISAVVGAVRL ADYIRAKGHL VSDIQPIWKT DKNSNLLDYD RFNVTEEELK
     KVPVKLICKD APPHLKNGLE AIEHLKKVYT QTMAFEFGHV QDEEERNWLR KQVESEAYAD
     ELPNKEKKAL LERLTSVEGF EKFIHRTFVG QKRFSIEGLD TLVPMLDKAI REVRKEKTDH
     VMIGMAHRGR LNVLAHTLGK PYKAIFSEFL QAPNKLNAPS EGLGETYTGW TGDVKYHLGA
     DRQISDDKSA QTIVSLANNP SHLEFVSPIV EGYARAAQED RSSKGAPKQD TTRAYSILIH
     GDAAFPGQGV VTETLNLSRL NGYHVGGSLH IIANNNIGYT TEMHDSRSTT YASDPAKGFE
     IPIVHVNADD AEACVRAIKF AVEYRRKFQK DFLIDLIGYR RFGHNEGDEP AVTQPDLYAQ
     IRKHPTVRAI YAKQLEAEQV ITAKEAQKLD TDMYNYLLEE YNKVNSDKSE KKYELSPPDF
     IVDGLPKVKT AVEKEKLVAM NEQLLDWPSS FKPNQKLEKI LKRRANAFDG EGNVDWGLAE
     ILAFASILHD GTPVRLSGQD SERGTFAHRH FVLHDRETNE THVPLQTIKD ANASFAVYNS
     PLTEQACVGF EYGYNVFSKE TLVLWEAQFG DFVNGAQVMF DQWVSAGRAK WGQKSGLVVL
     LPHGYEGAGP EHSSGRVERF LSSAAENNWT VANCTSAAQY FHILRRQAKI LQKNTVRPLI
     IMTPKSLLRN QVVASPTSAF TEGEFQPILE EPTLGHDPNA VKRIILCSGK LAIELQDYVN
     KNDEDWSWVH IIRVEELYPF PRRAIRERLK EFPNLEEVKW VQEEPKNMGA WTFMEPRIRE
     ILPSGVPLSY IGRTYRSSPA EGVSNAHKVE QKRIVTESLT RKN
//