ID   A0A1W1ZIE9_9SPHN        Unreviewed;       950 AA.
AC   A0A1W1ZIE9;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000256|ARBA:ARBA00013321};
DE   AltName: Full=Alpha-ketoglutarate dehydrogenase {ECO:0000256|ARBA:ARBA00030680};
GN   ORFNames=SAMN06272759_103179 {ECO:0000313|EMBL:SMC48103.1};
OS   Novosphingobium sp. B1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=1938756 {ECO:0000313|EMBL:SMC48103.1, ECO:0000313|Proteomes:UP000192500};
RN   [1] {ECO:0000313|Proteomes:UP000192500}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B1 {ECO:0000313|Proteomes:UP000192500};
RA   Varghese N., Submissions S.;
RL   Submitted (APR-2017) 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; FWXL01000003; SMC48103.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W1ZIE9; -.
DR   STRING; 1938756.SAMN06272759_103179; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000192500; 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   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          594..785
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   950 AA;  104433 MW;  DCFB07F7260C44FA CRC64;
     MGSELHEFDV DPAQEGPQPG PSWANKRWPI TDAASGDDLT QAMDPMALKL AIKESAKKGG
     APLDEAALQQ AATDSIRAMT LIRTYRVRGH LAADLDPLGL ARQKLPADIS PEYHGFTAAD
     AKRKIYIGGV LGLEWATLDE LVAILRANYC GHIGFEYMHI ADVEERRFIQ DRIEGGDKSI
     DFTPNGKKAI LAAVVRGEQY EKFLGRKYVG TKRFGLDGGE SMIPALEAVI KYGGQLGVKE
     IVYGMAHRGR LNVLANVMAK PYRVIFHEFS GGSANPQDVG GSGDVKYHLG TSTDREFDGT
     KVHMSLVPNP SHLETVDPIV LGKVRAQQVF RDDIGDDVGP DARHKQVLPV LIHGDAAFAG
     QGIVWECFGL SGVRGYNTGG CIHFIINNQI GFTTSPQFSR GSPYPSDVAK GVQAPILHVN
     GDDPEAVTFA CKMAIDYRQK FGRDIVIDMW CYRRFGHNEG DEPSFTQPLM YAKIRQHPGV
     SDIYAKRLVG EGVIDANYKG EIESHFVATL ETEFEAAKGY KANEADWFGG RWSGLNKPAD
     PVTARRNVAT GIDQKLFDSL GRTLTTVPAD LTVHKTLGRV IDAKREMFSS GQGFDWATGE
     ALAFGSLVSE GYGVRLSGQD CGRGTFSQRH AVWVDQTDER KYVPLKTLPH GTFEVLDSTL
     SEYGVLGFEY GYASADPKSL VLWEAQFGDF ANGAQIVIDQ YIAASEAKWL RANGLVMLLP
     HGYEGQGPEH SSARLERYLQ LCAEDNIQVC NITTPANYFH VLRRQMHRPF RKPLIIMTPK
     SLLRHPLAKS VASDFVGESH FMRILSDINP AADKDTRKVI LCSGKVAYDL IEARDAAGIT
     DTQIIRLEQL YPFPGEPLAL RLSRMPNLEE VVWCQEEPRN NGSWFFVEPM IEESLKAANS
     KVARPRYAGR AAAASPATGL ASRHASEQGA LVADALGLSV RGEIRRQKKN
//