ID   ODO1_STAEQ              Reviewed;         934 AA.
AC   Q5HPC6;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   02-SEP-2026, entry version 112.
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=SERP0986;
OS   Staphylococcus epidermidis (strain ATCC 35984 / DSM 28319 / BCRC 17069 /
OS   CCUG 31568 / BM 3577 / RP62A).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35984 / DSM 28319 / BCRC 17069 / CCUG 31568 / BM 3577 /
RC   RP62A;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
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=N(6)-[(R)-lipoyl]-L-lysyl-[protein] + 2-oxoglutarate + H(+) =
CC         N(6)-[(R)-S(8)-succinyldihydrolipoyl]-L-lysyl-[protein] + CO2;
CC         Xref=Rhea:RHEA:12188, Rhea:RHEA-COMP:10474, Rhea:RHEA-COMP:20092,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC         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; CP000029; AAW54333.1; -; Genomic_DNA.
DR   RefSeq; WP_002446425.1; NC_002976.3.
DR   AlphaFoldDB; Q5HPC6; -.
DR   SMR; Q5HPC6; -.
DR   STRING; 176279.SERP0986; -.
DR   PaxDb; 176279-SERP0986; -.
DR   KEGG; ser:SERP0986; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_9; -.
DR   Proteomes; UP000000531; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IEA:TreeGrafter.
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:TreeGrafter.
DR   CDD; cd02016; TPP_E1_OGDC_like; 1.
DR   FunFam; 3.40.50.970:FF:000036; 2-oxoglutarate dehydrogenase E1 component; 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; IPR011603; 2oxoglutarate_DH_E1.
DR   InterPro; IPR023784; 2oxoglutarate_DH_E1_bac.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR042179; KGD_C_sf.
DR   InterPro; IPR031717; ODO-1/KGD_C.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   NCBIfam; TIGR00239; 2oxo_dh_E1; 1.
DR   NCBIfam; NF006914; PRK09404.1; 1.
DR   NCBIfam; NF008907; PRK12270.1; 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..934
FT                   /note="2-oxoglutarate dehydrogenase E1 component"
FT                   /id="PRO_0000162182"
SQ   SEQUENCE   934 AA;  105671 MW;  711FD468A5FB2EC5 CRC64;
     MTKNKKEFTE APVNFGANLG LMLDLYDDYL QDPSSVPEDL QVLFSTIKTG EAHIEAKPTT
     DGGGSQAGDS TIKRVMRLID NIRQYGHLKA DIYPVNPPER QNVPKLEIED FDLDKETLEK
     ISSGIVSEHF KDIYDNAYDA IVRMERRYKG PIAFEYTHIN NNKERVWLKR RIETPYKASL
     NDNQKKELFK KLAHVEGFEK YLHKNFVGAK RFSIEGVDTL VPMLQHTITL AGNEGIKNIQ
     IGMAHRGRLN VLTHVLEKPY EMMISEFMHT DPMKFLPEDG SLELTSGWTS DVKYHLGGVK
     TTNSYGIEQR ISLANNPSHL EIVAPVVAGK TRAAQDNTHQ VGGPSTDFHK AMPIIIHGDA
     AYPGQGINFE TMNLGSLKGY STGGSLHIIT NNRIGFTTEP FDGRSTTYSS DVAKGYDVPI
     LHVNADDVEA TIEAIEIAME FRKEFHKDVV IDLVGYRRYG HNEMDEPSIT NPVPYQNIRK
     HDSVEILYGK KLVDEGIISE DEMNEVIDSV QKEMRTAHDK IDKNDKMNNP DMEKPESLQL
     PLQSDTKDFS FDHLKEINDA MLDYPKDFHV LKKLNKVLEK RREPFEKEGG LVDWAQAEQL
     AFATILQDGT SIRLTGQDSE RGTFSHRHAV LHDEENGNTF TPLHHVPQQQ ATFDIHNSPL
     SEAAVVGFEY GYNVENKGNF NIWEAQYGDF SNMSQMMFDN FLSSSRAKWG ERSGLTLFLP
     HAFEGQGPEH SSARLERFLQ LAAENNSTVV NLSSASNYFH LLRAQAASLD TLEMRPLIVM
     SPKSLLRNKT VAKPIDEFTS GGFKPIITED IDEQKVKKVI LASGKMYIDL KEYLAKNPND
     SILLIAVERL YPFPEEEIKE VLKSLPHLEN VSWVQEEPKN QGAWLFVYPY LKALVANKYD
     LTYHGRIQRA APAEGDGEIH KLVQTKIIES SINN
//