ID G6E994_9SPHN Unreviewed; 953 AA.
AC G6E994;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000256|ARBA:ARBA00013321};
DE AltName: Full=Alpha-ketoglutarate dehydrogenase {ECO:0000256|ARBA:ARBA00030680};
GN ORFNames=NSU_0915 {ECO:0000313|EMBL:EHJ62318.1};
OS Novosphingobium pentaromativorans US6-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1088721 {ECO:0000313|EMBL:EHJ62318.1, ECO:0000313|Proteomes:UP000004030};
RN [1] {ECO:0000313|EMBL:EHJ62318.1, ECO:0000313|Proteomes:UP000004030}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=US6-1 {ECO:0000313|EMBL:EHJ62318.1,
RC ECO:0000313|Proteomes:UP000004030};
RX PubMed=22275104; DOI=10.1128/JB.06476-11;
RA Luo Y.R., Kang S.G., Kim S.J., Kim M.R., Li N., Lee J.H., Kwon K.K.;
RT "Genome sequence of benzo(a)pyrene-degrading bacterium Novosphingobium
RT pentaromativorans US6-1.";
RL J. Bacteriol. 194:907-907(2012).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHJ62318.1}.
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DR EMBL; AGFM01000009; EHJ62318.1; -; Genomic_DNA.
DR AlphaFoldDB; G6E994; -.
DR STRING; 1088721.JI59_15545; -.
DR PATRIC; fig|1088721.3.peg.905; -.
DR eggNOG; COG0567; Bacteria.
DR Proteomes; UP000004030; 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:UP000004030};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 597..788
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 953 AA; 105593 MW; C3FEB20052FA9128 CRC64;
MIPMGNENLD FTPDLGMDEP QPGPSWQRSN WPRVGAEFED DLTQGLDPTA LKVQIEKAAA
KGGKKVDQAS LDQAAADAIR AMMLIRTYRV RGHLAADLDP LGLNQRKLPQ DLTPEYHGFT
GDALDRPVFV GGNLGLEWTT VRELVQILRA NYCGKVGLEY MHIADVEERR FLQERMEGAD
KEIEFTPEGK KAILQAVVRG EQYEKFLGKK YVGTKRFGLD GGESMIPALE SVIKYGGAQG
VKEIVYGMAH RGRLNVLANV MAKPYKVIFH EFSGGTANPE DVGGSGDVKY HLGTSTDREF
DGIKVHMSLM PNPSHLETVD PVVLGKVRAY QVFHDDIGDD VGPGAKHKQV LPVLIHGDAA
FAGQGVVWEC FGLSGVAGYN TGGCIHFVIN NQIGFTTTPN FARNSPYPTD VAKGVQAPIL
HVNGDDPAAV TFACKLAIDY RQTFGRDIVI DMWCYRRFGH NEGDEPSFTQ PLMYAQIKKH
PSVSTIYAER LKAEGVIDDA FLAATVEGFN NHLEEEFEAA KTYKANHADW FGGRWSGFNK
PVDPETARRN VHTGIEGKLF DSLGRTLTTV PDDLTIHKTL ARVIQAKDEM FKTGEGFDWA
TAEALAFGSL VSEGYGVRLS GQDCERGTFS QRHAVWVDQK TERKYTPLET LPHGTFEVLN
STLSEYGVLG FEYGYASADP KTLVLWEAQF GDFANGAQII IDQYIAASEA KWLRANGLVM
LLPHGYEGQG PEHSSARLER YLQLCASDNL QVCNITTPAN YFHVLRRQMH RPFRKPLIIM
TPKSLLRHPM AKSPASDFVG EGHFFRILSD PKAPSDEKTK KVILCSGKVA YDLFEARDQN
DIDDTQIIRI EQLYPFPGEP LALRLSRMKN LEEIVWCQEE PKNNGAWFFV ESLIEESAKE
AGVSACRPRY AGRGASASPA TGLAKRHAAE QAALVADALH LSVRDELRRK QKA
//
