ID A0A1I2ZCG6_9SPHI Unreviewed; 931 AA.
AC A0A1I2ZCG6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN ORFNames=SAMN04489864_109142 {ECO:0000313|EMBL:SFH35295.1};
OS Pedobacter insulae.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=414048 {ECO:0000313|EMBL:SFH35295.1, ECO:0000313|Proteomes:UP000199666};
RN [1] {ECO:0000313|EMBL:SFH35295.1, ECO:0000313|Proteomes:UP000199666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18684 {ECO:0000313|EMBL:SFH35295.1,
RC ECO:0000313|Proteomes:UP000199666};
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; FOPP01000009; SFH35295.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2ZCG6; -.
DR STRING; 414048.SAMN04489864_109142; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000199666; 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 Reference proteome {ECO:0000313|Proteomes:UP000199666};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 572..765
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 931 AA; 104902 MW; 9CC53030ECB63373 CRC64;
MDNLSYLNGA NAEYIESLYQ SYKEDPNSVE FGWQKFFEGF DFGRGSGAGN ATNEAPEHFL
KEINVLSLIN GYRQRGHLFT KTNPVRERRK HLPTLAIENF GLAQTDLQVV FNSSVALGIG
PAKLSDIIAF LEQTYCGTIG VEYKYVRTPE ILNWLETKME TERNTPQLSI DEKKRILSKL
NEAVSFENFL GTKFLGQKRF SLEGAEAVIP ALDSVIEKGA ELGIEEFVIG MAHRGRLNVL
ANIMQKTYKD IFAEFEGKGY SADSPFGGDV KYHLGYSTDV TTNAGRSVHL SLCPNPSHLE
TVNGVVEGMS RSKIDFKYGG DNSRLAPILI HGDASVAGQG IVYEVIQMAS LEGYKTGGTI
HLVINNQIGF TTNYKDARSS TYCTDIAKVT LSPVFHVNGD DVEALVYAIN LAMEYRQKYR
NDVFIDILCY RRFGHNEADE PKFTQPLLYK AIEKHANPRD IYIEKLTKTG ELEAGLAKEM
EKQFKGLLQD RLNEAKELTS TYSDVKFGGA WADMRLATAK DFDVSPDTSV KKTTLLEIAK
RISTLPKDKT FFKKIQKLFD ERNKMATTTH IFDWAMAEQL AYGTLLAEGK RVRLSGQDVK
RGTFSHRHAV LTLEDSEEEY TPLANISDQQ AQFDIYNSHL SEYGVLGFEY GYAMANPNAL
TIWEAQFGDF FNGAQIVVDQ YLASAETKWQ RENGLVLLLP HGYEGQGPEH SSARIERFME
LCADYNMQIT NCTTPANFFH ALRRQFKRDF RKPLVVFSPK SLLRHPLCVS PLADFTDGKF
KEVIDDATVK PANVKRVVFC SGKIYYDLLE TQKANDKGDV ALVRVEQLYP TPVAQMEAVY
KRYKNAIDAV WVQEEPENMG AWPYLLRRLR KTSFSQMEVI SRKESSSTAT GYAKQHANQQ
AYIVATAFDI PVTEKIKEVV AKATKKLVNI D
//
