ID A0A1H7M588_9SPHI Unreviewed; 931 AA.
AC A0A1H7M588;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN ORFNames=SAMN05421740_103373 {ECO:0000313|EMBL:SEL06450.1};
OS Parapedobacter koreensis.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Parapedobacter.
OX NCBI_TaxID=332977 {ECO:0000313|EMBL:SEL06450.1, ECO:0000313|Proteomes:UP000198916};
RN [1] {ECO:0000313|EMBL:SEL06450.1, ECO:0000313|Proteomes:UP000198916}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Jip14 {ECO:0000313|EMBL:SEL06450.1,
RC ECO:0000313|Proteomes:UP000198916};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR EMBL; FNZR01000003; SEL06450.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7M588; -.
DR STRING; 332977.SAMN05421740_103373; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000198916; 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; IPR032106; 2-oxogl_dehyd_N.
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; PF16078; 2-oxogl_dehyd_N; 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 573..765
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 931 AA; 106158 MW; FC711A01260BC9F8 CRC64;
MDKLSYLSNA DSAYIDSLYR AYKEDPNAID FGWQKFFEGF DFGQNGTATA ANTTPDHVLK
EINVLNMING YRDRGHLFTE TNPVRQRRKY YPGKELETFG LSEADMDTIF NAGVEIGLGP
AKLRDIRQLI EDTYCRSIGA EFKYIRSPEK IKWLQDRMEG ERNTPNFPLE KKKRILQKLN
EAVVFENFLG TKFLGQKRFS LEGAESLIPA LDSVIEKGAD LGIQEFVLGM AHRGRLNVLT
NILRKSYETV FSEFEGKTYA EEAEQDFGGD VKYHLGYSTD ITTDNGANVH LSLVPNPSHL
ETVDPVVEGI VRSKIDMKYE GDATKIAPIL IHGDAAVAGQ GIVYEVIQMS KLEGFRTGGT
IHIVVNNQVG FTTNFKDGRS STYCTDIAKV TLSPVFHVNG DDVEALVYAI NMAVEYRQKY
HTDVFIDLLC YRRYGHNEAD EPKFTQPLLY KAIEQHANPR EIYNKKLLEQ GSVDANLAKE
MEKDFRKLLQ ARLDESKEEE NLTQDNPMYS GAWKGLRKAK YEDIFVPAKT GIAEKTFLNL
AKEISTLPKD KKFFRKISRL FDERLKMVEQ KTFDWAMGEL MAYATLLSEG ARVRVSGQDV
KRGTFSHRHA VLTLEDSEEE YTPLQQLSGG ERFNIYNSHL SEYGVLGFEY GYALANPQSL
TIWEAQFGDF YNGAQIIVDQ YISSAETKWR RSNGLVMLLP HGLEGQGPEH SSARIERFLE
LCAENNMQIV NCTTPANFFH VLRRQIKRDY RKPLIVFTPK SLLRHPKVVS DISEFTAKSQ
FQEVIDDSYV KLADVKRVLF CSGKIYYDLL EKQQTDTRTD VAVVRVEQLY PTPMDKLRAI
RNKYKNATEF FWVQEEPENM GAWPYICRKF RNRNIALEVI SRKESSSTAT GYAKQHITQQ
LAVVGRAFED KAGPEVKEKI KANVKVAAKV D
//
