ID   A0A1G6SR06_9PROT        Unreviewed;       901 AA.
AC   A0A1G6SR06;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000256|ARBA:ARBA00013321};
DE   AltName: Full=Alpha-ketoglutarate dehydrogenase {ECO:0000256|ARBA:ARBA00030680};
GN   ORFNames=SAMN04487779_1005126 {ECO:0000313|EMBL:SDD19340.1};
OS   Belnapia rosea.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Belnapia.
OX   NCBI_TaxID=938405 {ECO:0000313|EMBL:SDD19340.1, ECO:0000313|Proteomes:UP000198925};
RN   [1] {ECO:0000313|EMBL:SDD19340.1, ECO:0000313|Proteomes:UP000198925}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CPCC 100156 {ECO:0000313|EMBL:SDD19340.1,
RC   ECO:0000313|Proteomes:UP000198925};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00003906}.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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|ARBA:ARBA00011301}.
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DR   EMBL; FMZX01000005; SDD19340.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G6SR06; -.
DR   STRING; 938405.SAMN02927895_02436; -.
DR   Proteomes; UP000198925; Unassembled WGS sequence.
DR   GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:UniProtKB-EC.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
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   InterPro; IPR011603; 2oxoglutarate_DH_E1.
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   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198925};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          556..748
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   901 AA;  97330 MW;  F06CF8E3E403DFB8 CRC64;
     MVADIYRQYA TDPSALDNSF GAVFEGLEGA ELAAGARPDP EVMDPYRTAL VLGRVIEGYR
     WRGHQNARLD PLGLAEPKLD ADLQLDRELL RLADQQVAPA LAGTLGLKQG TVPQILERLD
     RIYCGTIGFE YMQVRDPVAR EWLRRAIEAG PAMPGREARR DAARQLIRAD ELEAFMHRRF
     VGKKRFGAEG CESLICALWA VLARGAALGV RSVVMGGTSR ARLNQLANVV GKPLHAIFAE
     VKGLSPVPEG VRASGDVAYH QGFRGEQQVG GVTVSIDYTA NPSHLETVDG VAAGRLRAMQ
     EARGGAGWRE ALGLVVHTDA AFAGQGIVAE VAQLSALRHY SVGGTIHVIV NNQVGFTTDP
     ADGRSSAYCS DLARAVGSPV FHVNGDDVDA VIRVGQLAAE YRQRFGQDAI IDLVCYRRRG
     HNEMDEPSFT QPLMAARIAG HPTTRRLYLD RLAAEGAVTA AEEQSITAAV QQEMSDAYEA
     AQSYRLNAMP EDAWAASPER FAEETAGPEI PTGIDLPLLQ ALGTAISTAP PGIGLNPKVE
     RVFAERLEML ARKREVAWAF AEGLALASLA SEGTAIRFSG QDTPRGAFSQ RHFAVHDASS
     GAGASIFANL PSGSAACTVF GSPLSEYATL GFEYGYSLEA PGTLVLWEAQ FGDFANVAQP
     VFDQFIASGE DKWLQQSSLV TLLPHGLEGQ GAEHSSGRIE RFLQLCAAGN IMVANASTPA
     SYFHLLRRQA KGRRRPLVVF TPKSLLRHRF AVSGLAEFGP GTAFRPVIGP QPGQHRRLVL
     CSGKLYWELE AARQERNLAD VGLVRLEQLY PFPARELAAI FRMAPGAEIL WCQEEPRNMG
     AWDFVDRRIE AVMRASGCSA PWPACIGRPA NPSPALGTEK QHMADQARLI EAALTGPSPA
     R
//