ID Q2IP24_ANADE Unreviewed; 939 AA. AC Q2IP24; DT 07-MAR-2006, integrated into UniProtKB/TrEMBL. DT 07-MAR-2006, sequence version 1. DT 27-MAR-2024, entry version 97. DE RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280}; DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280}; GN OrderedLocusNames=Adeh_0781 {ECO:0000313|EMBL:ABC80556.1}; OS Anaeromyxobacter dehalogenans (strain 2CP-C). OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae; OC Anaeromyxobacteraceae; Anaeromyxobacter. OX NCBI_TaxID=290397 {ECO:0000313|EMBL:ABC80556.1, ECO:0000313|Proteomes:UP000001935}; RN [1] {ECO:0000313|EMBL:ABC80556.1, ECO:0000313|Proteomes:UP000001935} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2CP-C {ECO:0000313|EMBL:ABC80556.1, RC ECO:0000313|Proteomes:UP000001935}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., RA Gilna P., Kiss H., Schmutz J., Larimer F., Land M., Kyrpides N., RA Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R., RA Zhulin I.B., Loeffler F.E., Richardson P.; RT "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C."; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000001935} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2CP-C {ECO:0000313|Proteomes:UP000001935}; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., RA Gilna P., Kiss H., Schmutz J., Larimer F., Land M., Kyrpides N., RA Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R., RA Zhulin I.B., Loeffler F.E., Richardson P.; RT "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C."; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; CC Evidence={ECO:0000256|ARBA:ARBA00001964}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000251; ABC80556.1; -; Genomic_DNA. DR RefSeq; WP_011419839.1; NC_007760.1. DR AlphaFoldDB; Q2IP24; -. DR STRING; 290397.Adeh_0781; -. DR KEGG; ade:Adeh_0781; -. DR eggNOG; COG0567; Bacteria. DR HOGENOM; CLU_004709_1_0_7; -. DR OrthoDB; 9759785at2; -. DR Proteomes; UP000001935; Chromosome. 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 ECO:0000313|EMBL:ABC80556.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001935}; KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}. FT DOMAIN 584..777 FT /note="Transketolase-like pyrimidine-binding" FT /evidence="ECO:0000259|SMART:SM00861" FT REGION 47..78 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 890..909 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 939 AA; 103091 MW; 22045495532E3F27 CRC64; MSSPPEPQAL PSAPSLSFVE DLYYAWLADP RSVDESWRRY FEGLPAAPGA APAPASFPRR RPDGAAGPQA APGAGGDAAF QSKVDRLVQA YREYGHLRAN LDPLGLVRPA EPFALEAFGL GPADLDRPCA DADGRGDRTL RDLVARLEET YCRTLGVELA HMHDQDLRGW LEQRMERTRN RLSLAPDVKK LLLRKIVEAE SLEQFLGTKF LGAKRFSVEG AEGFVALLEF LVDRAVGHGV RNVVIGMAHR GRLNVLANVV GKPLRQIFAE FRDNAIVNAT GGDVKYHLGH STDRETPDGV LVHLSLAFNP SHLEWINTVV QGRVRAKQDR YHDFDRVRSL PVLVHGDASF AGQGIVAEAL NMSQLEAYGV GGTIHVIVNN QVGFTTSPRD ARSTTYCTGP ARMLQIPIIH VNGEDLEAVA QAVLLAADFR QRFHRDVVID LWAYRRHGHN EGDEPSFTQP VMYRAISKRP TLRQLYAEAL EREGTATRAE VDAMAAEYRA RLDEAYQASA QIAVQPGAQE AAGFWAGVKG GAITGPEPET GVAPAVLAQA AAGITQVPQG FHVHPKLAKV LEARAEMGRG ERPLDWATAE ALAFATLSLE GRRVRLVGQD SRRGTFSHRH AVLYDHQTGT PYSPLAHLRE GQGVVEIRDS LLSEAAALGY EYGYSLEMPD ALTLWEAQFG DFVNAAQVII DQFLSSGEAK WNRLSGLALL LPHGMEGQGP EHSSARLERF LELSVDDNWY VVNVTTPAQY FHALRRQVYS PWRKPLVVMS PKSLLRHPKA VSPIGELAEA RFRPVVADPV ADPSEITRVV LCSGKLYYDL AAAREAQGAR HVALVRLEQL YPLAADEILD AIAAFRPGTE MVWAQEEPSN MGAWDYVDLH LSPRLPSRLD LVSRPPSASP ASGSATRHKL EQQQLVLEAL GDPVPRIHRT DTRAAAHEH //