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Database: UniProt
Entry: A0A2T3HPI6_9SPHI
LinkDB: A0A2T3HPI6_9SPHI
Original site: A0A2T3HPI6_9SPHI 
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
//
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