ID A0A2T3HPI6_9SPHI Unreviewed; 931 AA.
AC A0A2T3HPI6;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN ORFNames=C7T94_06565 {ECO:0000313|EMBL:PST84370.1};
OS Pedobacter yulinensis.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=2126353 {ECO:0000313|EMBL:PST84370.1, ECO:0000313|Proteomes:UP000240912};
RN [1] {ECO:0000313|EMBL:PST84370.1, ECO:0000313|Proteomes:UP000240912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YL28-9 {ECO:0000313|EMBL:PST84370.1,
RC ECO:0000313|Proteomes:UP000240912};
RA Keele B.F.;
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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:PST84370.1}.
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DR EMBL; PYLS01000004; PST84370.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T3HPI6; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000240912; 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:UP000240912};
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; 105425 MW; 3C59A7C407EAFA74 CRC64;
MDHFSYLNGA NAEYIESLYQ SYQKDPASVE FGWQKFFEGF DFGRGSEPAA ASADTPEHFL
KEVNVLNLID GYRTRGHLFT HTNPVRERRK HLPTLELSNF GLSDADLETV FNAGVEIGIG
PAKLKDIISL LEQTYKRSIG AEFKFLRTPE VLSWLQEKME SVRNTPNFSI EEKKRILTKL
NQAVSFENFL GTKFLGQKRF SLEGAEALIP ALDSVIEKGA DLGIEEFVIG MAHRGRLNVL
ANIMQKTYKD IFAEFEGKGY SADSPFGGDV KYHLGYSTDV NTNDGKSVHL SLCPNPSHLE
TVNSVVEGMT RSKIDFKYGG DNARIAPILI HGDASIAGQG IVYEVIQMAG LEGYKTGGTI
HLIINNQIGF TTNYKDARTS TYCTDIAKVT LSPVFHVNGD DVEALVYAIN LAMEYRQKYR
NDVFIDILCY RRFGHNESDE PKFTQPLLYK TIEKHPNPRE IYVQQLTKEG KLEAGLAKEM
EKEFRAMLQE RLNEAKEVTT TSTEVKFGGA WADMRMATPN DFNESPDTSV KKSTLLEIGK
RVTSLPADKK FFRKIEKLFD ERRKMVEETE VFDWAMGEQL AYGTLLAEGK RVRLSGQDVE
RGTFSHRHAV LTLEDSEEEY IPLANLSDQQ APFDIYNSHL SEYGVLGFEY GYAMANPNAL
TIWEAQFGDF FNGAQIVIDQ YIASAETKWQ RENGLVMLLP HGYEGQGPEH SSARIERFME
LCADYNMQVV NCTTPANFFH VLRRQFKRDF RKPLVVFSPK SLLRHPQCVS PLADFTAGGF
KEVIADQHVK AGDVKRVIFC SGKIYYELAE KQKADQIKNV AIVRVEQLYP TPVEQMEAVV
KKYKHADDIV WVQEEPENMG AWPYLLRRLR KTSLSHIDVI SRKESSSTAT GYAKQHANQQ
AYILAKAFET QVSEQEKKIA KKSVNKVFSV D
//