ID   ODO1_STAS1              Reviewed;         933 AA.
AC   Q49XM5;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, 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}; OrderedLocusNames=SSP1325;
OS   Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS   20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=342451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX   PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA   Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA   Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT   "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT   pathogenesis of uncomplicated urinary tract infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(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; AP008934; BAE18470.1; -; Genomic_DNA.
DR   RefSeq; WP_011303106.1; NZ_MTGA01000038.1.
DR   AlphaFoldDB; Q49XM5; -.
DR   SMR; Q49XM5; -.
DR   STRING; 342451.SSP1325; -.
DR   EnsemblBacteria; BAE18470; BAE18470; SSP1325.
DR   KEGG; ssp:SSP1325; -.
DR   PATRIC; fig|342451.11.peg.1328; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_9; -.
DR   OMA; RDSYCRT; -.
DR   OrthoDB; 29166at2; -.
DR   Proteomes; UP000006371; 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..933
FT                   /note="2-oxoglutarate dehydrogenase E1 component"
FT                   /id="PRO_0000162185"
SQ   SEQUENCE   933 AA;  105479 MW;  603C12A85D1562EB CRC64;
     MSNESQVSEA PVNFGANLGY VLDLYDIYLD NPSAVPEDLQ VLFSTIKNGE ANIATNTEGQ
     SNVTKGDSTI KRVMRLIDNI RQYGHLLADI YPVNRPQREN VPKLNMEDFN LDQETLESIS
     AGIVSEHFKD IYDNAYEAIV RMEKRYKGPI AFEYTHINNN RERVWLKRRI ETPYKATLND
     NQKIELFKNL AHVEGFEKYL HKNFVGAKRF SIEGVDTLVP MLQQTLRIAS DEGIQNIQIG
     MAHRGRLNVL THVLEKPYEM MISEFMHIDP MKFLPEDGSL QLTSGWTGDV KYHLGGVKTT
     QSYGSEQRIS LANNPSHLEI VAPVVLGKTR ANQDTTDKPG AVTTEFKKSM PILIHGDAAY
     PGQGINFEAM NLGNLEGYST GGSLHIITNN RIGFTTEPED GRSTTYSSDV AKGYDVPIMH
     VNADNVEATI EAIEIAMAFR KEFNKDVVID LVGYRRYGHN EMDEPSITNP LQYYEIRKHE
     SVDILYGKQL VNENIISENQ MNQIFDDVQN TLRAAHDKID KNDKMDNPDM QKPDSLAEPI
     QTKDEEVSYE QLKEINDAML SYPSDFNVLK KLNKVLEKRR EPFESEDGLV DWAQAEQLAF
     ATITQNGRPI RLTGQDSERG TFSHRHAVLH DPDTGAQYVP LHNVPDQKAT FEVRNSPLSE
     AAVVGFEYGY NIQNKSCMTI WEAQYGDFSN MAQMIFDNFL FSSRAKWGER SGLTLFLPHS
     FEGQGPEHSS ARLERFLQLA GENNSTIVNL SSSSNYFHLL RAQAANLGTQ SMRPLVVMSP
     KSLLRNKTVA DPISKFTSGK FEPILPEAHD KASVKKVILA SGKMFIDLKE YLTKNPNKSI
     LLVAVERLYP FPADEIDALL SELPNLEHVA WVQEEPKNQG AWSFVYPYLK ELTTDKYDLS
     YHGRIQRSAP AEGDGEIHKL VQNMIIEQST NIN