ODO1_STAEQ
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 25-MAY-2022, entry version 97.
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}; OrderedLocusNames=SERP0986;
OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35984 / 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=(R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue
CC succinyltransferase] + 2-oxoglutarate + H(+) = (R)-N(6)-(S(8)-
CC succinyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue
CC succinyltransferase] + CO2; Xref=Rhea:RHEA:12188, Rhea:RHEA-
CC COMP:10483, Rhea:RHEA-COMP:10484, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:83099,
CC ChEBI:CHEBI:83120; EC=1.2.4.2; Evidence={ECO:0000255|HAMAP-
CC 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 EnsemblBacteria; AAW54333; AAW54333; SERP0986.
DR KEGG; ser:SERP0986; -.
DR eggNOG; COG0567; Bacteria.
DR HOGENOM; CLU_004709_1_0_9; -.
DR OMA; RDSYCRT; -.
DR OrthoDB; 29166at2; -.
DR Proteomes; UP000000531; 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 Gene3D; 3.40.50.11610; -; 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 PANTHER; PTHR23152; PTHR23152; 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; SSF52518; 2.
DR TIGRFAMs; TIGR00239; 2oxo_dh_E1; 1.
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
