ID   B9DNZ3_STACT            Unreviewed;       931 AA.
AC   B9DNZ3;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   RecName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000256|HAMAP-Rule:MF_01169};
DE            EC=1.2.4.2 {ECO:0000256|HAMAP-Rule:MF_01169};
DE   AltName: Full=Alpha-ketoglutarate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01169};
GN   Name=odhA {ECO:0000256|HAMAP-Rule:MF_01169,
GN   ECO:0000313|EMBL:CAL27966.1};
GN   OrderedLocusNames=Sca_1058 {ECO:0000313|EMBL:CAL27966.1};
OS   Staphylococcus carnosus (strain TM300).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=396513 {ECO:0000313|EMBL:CAL27966.1, ECO:0000313|Proteomes:UP000000444};
RN   [1] {ECO:0000313|EMBL:CAL27966.1, ECO:0000313|Proteomes:UP000000444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TM300 {ECO:0000313|EMBL:CAL27966.1,
RC   ECO:0000313|Proteomes:UP000000444};
RX   PubMed=19060169; DOI=10.1128/AEM.01982-08;
RA   Rosenstein R., Nerz C., Biswas L., Resch A., Raddatz G., Schuster S.C.,
RA   Goetz F.;
RT   "Genome analysis of the meat starter culture bacterium Staphylococcus
RT   carnosus TM300.";
RL   Appl. Environ. Microbiol. 75:811-822(2009).
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:0000256|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:0000256|HAMAP-Rule:MF_01169};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964, ECO:0000256|HAMAP-
CC         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:0000256|HAMAP-
CC       Rule:MF_01169}.
CC   -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01169}.
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DR   EMBL; AM295250; CAL27966.1; -; Genomic_DNA.
DR   RefSeq; WP_015900307.1; NC_012121.1.
DR   AlphaFoldDB; B9DNZ3; -.
DR   KEGG; sca:SCA_1058; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_9; -.
DR   OrthoDB; 9759785at2; -.
DR   BioCyc; SCAR396513:SCA_RS05300-MONOMER; -.
DR   Proteomes; UP000000444; 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   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; 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 {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP-
KW   Rule:MF_01169};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_01169};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052, ECO:0000256|HAMAP-
KW   Rule:MF_01169}.
FT   DOMAIN          588..784
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   REGION          509..546
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        509..537
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   931 AA;  105560 MW;  5F7C559FD4DF1E5E CRC64;
     MTKDKQVSEA PVNFGANLGV IIDLYDQYLQ DPTSVSEDLQ ILFSTINNDN REVAASPASS
     SSDSTIKQVM RLVDNIRQYG HLQSDIYPVN RPERKHVPKL TIEDFNLSKD DLEKISPGIV
     SDHFSDIYDY AYEAIKRMEK RYKGPIAFEY THINNNTERT WLKRRIETPY KADLNKNQKI
     NLFKTLAHVE GFEKYLHKNF VGAKRFSIEG VDTLVPMLQE TLRRAAKEEI KNIQIGMAHR
     GRLNVLTHVL EKPYEMMISE FMHTDPMKFL PEDGSLELTS GNAWTSDVKY HLGGIKTTDT
     YGTEQRISLA NNPSHLEIVA PVVLGKTRSV QDDTHEGGKV QTDFSKSMPI LIHGDAAYPG
     QGINFEAMNL GNLDGYSTGG SLHIITNNRI GFTTEARDGR STTYSTDVAK GYDIPIMHVN
     ADNVEATIEA IDIAMDFRKE FNKDVVIDLV GYRRYGHNEM DEPSITNPLP YHAIRKHPTV
     DKIYGEQLVD EGVISKEEME QTLDDVQKEL RNSHDKIDKN DKTTTKDMSK PESVEEPLQP
     DKNNVSYDDL KTINDALLTY PTGFEVLKKL NKVLEKRREP FEKEDGLVDW AQAEQLAFAT
     IMQNGTPIRL TGQDSERGTF SHRHAVLHNP DNGDEYVPLQ NVPNQKASFD VHNSPLSEAA
     VVGFEYGYNV ENKGTMNIWE AQYGDFANMA QMMFDNFLFS SYAKWGERSG LTLFLPHSYE
     GQGPEHSSAR LERFLQLSAE NNSTVVNLSS SANYYHLLRA QAASLDTDAM RPLVVMSPKS
     LLRNKTVADT IDKFTEGYFK PILPEAHDEK KIKKLILASG KMFIDLKERL QKEPDESILL
     VAVERLYPFP VEEVREVINS LPNLETIAWV QEEPQNQGAW SFVYPYLSDL ASDKYELQYS
     GRIKRSAPAE GDGENHKLVQ NSIIEESLNK N
//