ID   U2JAP8_9SPHI            Unreviewed;       912 AA.
AC   U2JAP8;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   ORFNames=M472_13225 {ECO:0000313|EMBL:ERJ59733.1};
OS   Sphingobacterium paucimobilis HER1398.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Sphingobacterium.
OX   NCBI_TaxID=1346330 {ECO:0000313|EMBL:ERJ59733.1, ECO:0000313|Proteomes:UP000016584};
RN   [1] {ECO:0000313|EMBL:ERJ59733.1, ECO:0000313|Proteomes:UP000016584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HER1398 {ECO:0000313|EMBL:ERJ59733.1,
RC   ECO:0000313|Proteomes:UP000016584};
RX   PubMed=23929486;
RA   White R.A.III., Suttle C.A.;
RT   "The Draft Genome Sequence of Sphingomonas paucimobilis Strain HER1398
RT   (Proteobacteria), Host to the Giant PAU Phage, Indicates That It Is a
RT   Member of the Genus Sphingobacterium (Bacteroidetes).";
RL   Genome Announc. 1:e00598-13(2013).
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:ERJ59733.1}.
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DR   EMBL; ATDL01000014; ERJ59733.1; -; Genomic_DNA.
DR   RefSeq; WP_021070067.1; NZ_ATDL01000014.1.
DR   AlphaFoldDB; U2JAP8; -.
DR   STRING; 1346330.M472_13225; -.
DR   PATRIC; fig|1346330.5.peg.1896; -.
DR   eggNOG; COG0567; Bacteria.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000016584; 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:UP000016584};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          576..768
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   912 AA;  103677 MW;  2E45318ACEC33701 CRC64;
     MDKLTYLSNA DSSYIDGLYQ AYRQDPNSVD FGWQKFFEGF EFGQGAEAVS IDTENVSEHA
     LKEINVLNMI HGYRDRGHLF THTNPVRERR KYYPGKELET FGLSEADMDT VFNAGIEVGL
     GPAKLRDIRQ LIEDTYCRSI GAEFKYIRNP EKIKWLQDRM EADRNTPSYS TEQKKRILQK
     LNRAVVFESF LGTKFLGQKR FSLEGAESLI PALDSVMEKG ADLGLQEFMI GMAHRGRLNV
     LANIMGKPYK TILSEFEGKM YKEEDPELKF GGDVKYHLGY SSDITTDKGK HIHLSLAPNP
     SHLETVDPIV EGMVRSKIDM KYDGDSSKIA PILIHGDAAI AGQGVVYEVT QMSKLDGYKT
     GGTIHIVINN QVGFTTNYKD ARSGTYCTDV AKITSSPVFH VNGDDAEAVV YAINLAVEYR
     QKYKTDVFID LLCYRRYGHN EADEPKFTQP LLYKLIEKHA NPKEVYAKKL IDEGSIETSY
     AKEVEKEFKD YLQSQLDASK AVENLEEEVP MFGGAWKGLR PAKRADIFQT TETKVSDKVF
     KELATQITSL PKDKKFFRKI SKLFEDRAAM IGKDSYDWAM GELMAYATLL NDGKRVRISG
     QDVQRGTFSH RHAVLTLEDS EEKYVPLANV KGGDKFSIYN SLLSEYGVLG FEYGYASANP
     QALTVWEAQF GDFYNGAQII VDQYLSSAET KWKRSNGLVM MLPHGMEGQG PEHSSGRIER
     FLELCANDNM IIANCTTPAN YFHLLRRQLV RDFRKPLIVF TPKSLLRHPK VVSKQADFTK
     VNFQEVIDDT AVKAASVKRV LFCSGKIYYD LLEKQQADKR NDVAIVRIEQ LYPAPVEQLQ
     AIHKKYNKAS EFIWVQEENE NMGAWPYYCR TFRKSDIEFT DVISRKESGS PATGYMKQHI
     AQQETIINKA FE
//