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
//