ODO1_STAAN
ID ODO1_STAAN Reviewed; 910 AA.
AC Q99U74;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 108.
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=SA1245;
OS Staphylococcus aureus (strain N315).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N315;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=N315;
RA Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.;
RT "Shotgun proteomic analysis of total and membrane protein extracts of S.
RT aureus strain N315.";
RL Submitted (OCT-2007) to UniProtKB.
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; BA000018; BAB42505.1; -; Genomic_DNA.
DR PIR; E89918; E89918.
DR RefSeq; WP_000180688.1; NC_002745.2.
DR AlphaFoldDB; Q99U74; -.
DR SMR; Q99U74; -.
DR EnsemblBacteria; BAB42505; BAB42505; BAB42505.
DR KEGG; sau:SA1245; -.
DR HOGENOM; CLU_004709_1_0_9; -.
DR OMA; RDSYCRT; -.
DR Proteomes; UP000000751; 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 1: Evidence at protein level;
KW Glycolysis; Oxidoreductase; Thiamine pyrophosphate.
FT CHAIN 1..910
FT /note="2-oxoglutarate dehydrogenase E1 component"
FT /id="PRO_0000162178"
SQ SEQUENCE 910 AA; 103112 MW; 7803AAED537CF247 CRC64;
MTNERKEVSE APVNFGANLG LMLDLYDDFL QDPSSVPEDL QVLFSTIKRV MRLIDNIRQY
GHLKADIYPV NPPKRKHVPK LEIEDFDLDQ QTLEGISAGI VSDHFADIYD NAYEAILRME
KRYKGPIAFE YTHINNNTER GWLKRRIETP YKVTLNNNEK RALFKQLAYV EGFEKYLHKN
FVGAKRFSIE GVDALVPMLQ RTITIAAKEG IKNIQIGMAH RGRLNVLTHV LEKPYEMMIS
EFMHTDPMKF LPEDGSLQLT AGWTGDVKYH LGGIKTTDSY GTMQRIALAN NPSHLEIVAP
VVEGRTRAAQ DDTQRAGAPT TDHHKAMPII IHGDAAYPGQ GINFETMNLG NLKGYSTGGS
LHIITNNRIG FTTEPIDARS TTYSTDVAKG YDVPIFHVNA DDVEATIEAI DIAMEFRKEF
HKDVVIDLVG YRRFGHNEMD EPSITNPVPY QNIRKHDSVE YVFGKKLVNE GVISEDEMHS
FIEQVQKELR QAHDKINKAD KMDNPDMEKP AELALPLQAD EQSFTFDHLK EINDALLTYP
DGFNILKKLN KVLEKRHEPF NKEDGLVDWA QAEQLAFATI LQDGTPIRLT GQDSERGTFS
HRHAVLHDEQ TGETYTPLHH VPDQKATFDI HNSPLSEAAV VGFEYGYNVE NKKSFNIWEA
QYGDFANMSQ MIFDNFLFSS RSKWGERSGL TLFLPHAYEG QGPEHSSARL ERFLQLAAEN
NCTVVNLSSS SNYFHLLRAQ AASLDSEQMR PLVVMSPKSL LRNKTVAKPI DEFTSGGFEP
ILTESYQADK VTKVILATGK MFIDLKEALA KNPDESVLLV AIERLYPFPE EEIEALLAQL
PKLEEVSWVQ EEPKNQGAWL YVYPYVKVLV ADKYDLSYHG RIQRAAPAEG DGEIHKLVQN
KIIENALKNN
