ID ODO1_ECOLI Reviewed; 933 AA. AC P0AFG3; P07015; P78225; DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot. DT 20-DEC-2005, sequence version 1. DT 27-MAR-2024, entry version 141. DE RecName: Full=2-oxoglutarate dehydrogenase E1 component; DE EC=1.2.4.2 {ECO:0000269|PubMed:17367808}; DE AltName: Full=Alpha-ketoglutarate dehydrogenase; GN Name=sucA; OrderedLocusNames=b0726, JW0715; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=K12; RX PubMed=6376123; DOI=10.1111/j.1432-1033.1984.tb08199.x; RA Darlison M.G., Spencer M.E., Guest J.R.; RT "Nucleotide sequence of the sucA gene encoding the 2-oxoglutarate RT dehydrogenase of Escherichia coli K12."; RL Eur. J. Biochem. 141:351-359(1984). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=8905232; DOI=10.1093/dnares/3.3.137; RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H., RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., RA Horiuchi T.; RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to RT the 12.7-28.0 min region on the linkage map."; RL DNA Res. 3:137-155(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [5] RP IDENTIFICATION BY 2D-GEL. RX PubMed=9298644; DOI=10.1002/elps.1150180805; RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.; RT "Escherichia coli proteome analysis using the gene-protein database."; RL Electrophoresis 18:1243-1251(1997). RN [6] RP AMPYLATION AT THR-405, AND MUTAGENESIS OF SER-404 AND THR-405. RX PubMed=30270044; DOI=10.1016/j.cell.2018.08.046; RA Sreelatha A., Yee S.S., Lopez V.A., Park B.C., Kinch L.N., Pilch S., RA Servage K.A., Zhang J., Jiou J., Karasiewicz-Urbanska M., Lobocka M., RA Grishin N.V., Orth K., Kucharczyk R., Pawlowski K., Tomchick D.R., RA Tagliabracci V.S.; RT "Protein AMPylation by an Evolutionarily Conserved Pseudokinase."; RL Cell 175:809-821(2018). RN [7] RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, RP COFACTOR, ACTIVITY REGULATION, SUBUNIT, INTERACTION WITH SUCB, DISRUPTION RP PHENOTYPE, AND MUTAGENESIS OF HIS-260; HIS-298; HIS-313; ARG-337; TRP-533 RP AND ARG-710. RX PubMed=17367808; DOI=10.1016/j.jmb.2007.01.080; RA Frank R.A., Price A.J., Northrop F.D., Perham R.N., Luisi B.F.; RT "Crystal structure of the E1 component of the Escherichia coli 2- RT oxoglutarate dehydrogenase multienzyme complex."; RL J. Mol. Biol. 368:639-651(2007). CC -!- FUNCTION: E1 component of the 2-oxoglutarate dehydrogenase (OGDH) CC complex which catalyzes the decarboxylation of 2-oxoglutarate, the CC first step in the conversion of 2-oxoglutarate to succinyl-CoA and CC CO(2). {ECO:0000269|PubMed:17367808}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2-oxoglutarate + H(+) + N(6)-[(R)-lipoyl]-L-lysyl- CC [dihydrolipoyllysine-residue succinyltransferase] = CO2 + N(6)-[(R)- CC S(8)-succinyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue CC succinyltransferase]; Xref=Rhea:RHEA:12188, Rhea:RHEA-COMP:10483, CC Rhea:RHEA-COMP:10484, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, CC ChEBI:CHEBI:16810, ChEBI:CHEBI:83099, ChEBI:CHEBI:83120; EC=1.2.4.2; CC Evidence={ECO:0000269|PubMed:17367808}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12189; CC Evidence={ECO:0000269|PubMed:17367808}; CC -!- COFACTOR: CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; CC Evidence={ECO:0000305|PubMed:17367808}; CC -!- ACTIVITY REGULATION: Inhibited by oxaloacetate. CC {ECO:0000269|PubMed:17367808}. CC -!- SUBUNIT: Homodimer (PubMed:17367808). Part of the 2-oxoglutarate CC dehydrogenase (OGDH) complex composed of E1 (2-oxoglutarate CC dehydrogenase), E2 (dihydrolipoamide succinyltransferase) and E3 CC (dihydrolipoamide dehydrogenase); the complex contains multiple copies CC of the three enzymatic components (E1, E2 and E3) (Probable). Interacts CC (via N-terminus) with SucB, the E2 component of OGDH complex CC (PubMed:17367808). {ECO:0000269|PubMed:17367808, CC ECO:0000305|PubMed:17367808}. CC -!- INTERACTION: CC P0AFG3; P0AFG3: sucA; NbExp=2; IntAct=EBI-543523, EBI-543523; CC P0AFG3; P0AFG6: sucB; NbExp=7; IntAct=EBI-543523, EBI-558621; CC P0AFG3; P63389: yheS; NbExp=3; IntAct=EBI-543523, EBI-561198; CC -!- DISRUPTION PHENOTYPE: Impaired growth in minimal medium containing CC acetate as the sole carbon source. {ECO:0000269|PubMed:17367808}. CC -!- MISCELLANEOUS: Binds AMP; however it is not clear if the binding is CC physiologically relevant. {ECO:0000269|PubMed:17367808}. CC -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family. CC {ECO:0000305}. 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; J01619; AAA23897.1; -; Genomic_DNA. DR EMBL; X00661; CAA25280.1; -; Genomic_DNA. DR EMBL; U00096; AAC73820.1; -; Genomic_DNA. DR EMBL; AP009048; BAA35392.1; -; Genomic_DNA. DR PIR; E64808; DEECOG. DR RefSeq; NP_415254.1; NC_000913.3. DR RefSeq; WP_001181473.1; NZ_STEB01000035.1. DR PDB; 2JGD; X-ray; 2.60 A; A/B=1-933. DR PDB; 6VEF; EM; 4.08 A; A/B=84-933. DR PDBsum; 2JGD; -. DR PDBsum; 6VEF; -. DR AlphaFoldDB; P0AFG3; -. DR EMDB; EMD-21156; -. DR SMR; P0AFG3; -. DR BioGRID; 849680; 3. DR ComplexPortal; CPX-3921; 2-oxoglutarate dehydrogenase complex. DR DIP; DIP-36225N; -. DR IntAct; P0AFG3; 13. DR MINT; P0AFG3; -. DR STRING; 511145.b0726; -. DR jPOST; P0AFG3; -. DR PaxDb; 511145-b0726; -. DR EnsemblBacteria; AAC73820; AAC73820; b0726. DR GeneID; 75205557; -. DR GeneID; 945303; -. DR KEGG; ecj:JW0715; -. DR KEGG; eco:b0726; -. DR PATRIC; fig|1411691.4.peg.1547; -. DR EchoBASE; EB0972; -. DR eggNOG; COG0567; Bacteria. DR HOGENOM; CLU_004709_1_0_6; -. DR InParanoid; P0AFG3; -. DR OMA; RDSYCRT; -. DR OrthoDB; 9759785at2; -. DR PhylomeDB; P0AFG3; -. DR BioCyc; EcoCyc:E1O-MONOMER; -. DR BioCyc; MetaCyc:E1O-MONOMER; -. DR BRENDA; 1.2.1.105; 2026. DR BRENDA; 1.2.4.2; 2026. DR BRENDA; 2.2.1.5; 2026. DR SABIO-RK; P0AFG3; -. DR EvolutionaryTrace; P0AFG3; -. DR PRO; PR:P0AFG3; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0005737; C:cytoplasm; IDA:ComplexPortal. DR GO; GO:0005829; C:cytosol; IDA:EcoCyc. DR GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IPI:ComplexPortal. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IDA:EcoCyc. DR GO; GO:0030976; F:thiamine pyrophosphate binding; IDA:EcoCyc. DR GO; GO:0006099; P:tricarboxylic acid cycle; IDA:ComplexPortal. 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. DR SWISS-2DPAGE; P0AFG3; -. PE 1: Evidence at protein level; KW 3D-structure; Nucleotide-binding; Oxidoreductase; Phosphoprotein; KW Reference proteome; Thiamine pyrophosphate; Tricarboxylic acid cycle. FT CHAIN 1..933 FT /note="2-oxoglutarate dehydrogenase E1 component" FT /id="PRO_0000162191" FT MOD_RES 405 FT /note="O-AMP-threonine; by ydiU" FT /evidence="ECO:0000269|PubMed:30270044" FT MUTAGEN 260 FT /note="H->A: Loss of catalytic activity." FT /evidence="ECO:0000269|PubMed:17367808" FT MUTAGEN 298 FT /note="H->A: Loss of catalytic activity." FT /evidence="ECO:0000269|PubMed:17367808" FT MUTAGEN 313 FT /note="H->A: Mild reduction in growth in presence of FT acetate or glucose as sole source of carbon; when FT associated with A-337." FT /evidence="ECO:0000269|PubMed:17367808" FT MUTAGEN 313 FT /note="H->Q: No growth defect in presence of acetate or FT glucose as sole source of carbon." FT /evidence="ECO:0000269|PubMed:17367808" FT MUTAGEN 337 FT /note="R->A: Mild reduction in growth in presence of FT acetate or glucose as sole source of carbon; when FT associated with A-313." FT /evidence="ECO:0000269|PubMed:17367808" FT MUTAGEN 404 FT /note="S->A: No loss of AMPylation by YdiU." FT /evidence="ECO:0000269|PubMed:30270044" FT MUTAGEN 405 FT /note="T->A: Severe reduction in AMPylation by YdiU." FT /evidence="ECO:0000269|PubMed:30270044" FT MUTAGEN 533 FT /note="W->A: Mild reduction in growth in presence of FT acetate or glucose as sole source of carbon; when FT associated with A-710." FT /evidence="ECO:0000269|PubMed:17367808" FT MUTAGEN 533 FT /note="W->I: No growth defect in presence of acetate or FT glucose as sole source of carbon." FT /evidence="ECO:0000269|PubMed:17367808" FT MUTAGEN 710 FT /note="R->A: Mild reduction in growth in presence of FT acetate or glucose as sole source of carbon; when FT associated with A-533." FT /evidence="ECO:0000269|PubMed:17367808" FT CONFLICT 454 FT /note="C -> S (in Ref. 1; AAA23897/CAA25280)" FT /evidence="ECO:0000305" FT HELIX 85..102 FT /evidence="ECO:0007829|PDB:2JGD" FT HELIX 103..106 FT /evidence="ECO:0007829|PDB:2JGD" FT STRAND 111..113 FT /evidence="ECO:0007829|PDB:2JGD" FT HELIX 121..123 FT /evidence="ECO:0007829|PDB:2JGD" FT HELIX 126..129 FT /evidence="ECO:0007829|PDB:2JGD" FT HELIX 132..136 FT /evidence="ECO:0007829|PDB:2JGD" FT STRAND 137..140 FT /evidence="ECO:0007829|PDB:2JGD" FT STRAND 150..152 FT /evidence="ECO:0007829|PDB:2JGD" FT HELIX 153..165 FT /evidence="ECO:0007829|PDB:2JGD" FT STRAND 166..171 FT /evidence="ECO:0007829|PDB:2JGD" FT HELIX 178..188 FT /evidence="ECO:0007829|PDB:2JGD" FT HELIX 197..220 FT /evidence="ECO:0007829|PDB:2JGD" FT HELIX 235..247 FT /evidence="ECO:0007829|PDB:2JGD" FT TURN 248..250 FT /evidence="ECO:0007829|PDB:2JGD" FT STRAND 253..257 FT /evidence="ECO:0007829|PDB:2JGD" FT HELIX 263..269 FT /evidence="ECO:0007829|PDB:2JGD" FT HELIX 275..282 FT /evidence="ECO:0007829|PDB:2JGD" FT HELIX 296..298 FT /evidence="ECO:0007829|PDB:2JGD" FT STRAND 301..307 FT /evidence="ECO:0007829|PDB:2JGD" FT STRAND 310..316 FT /evidence="ECO:0007829|PDB:2JGD" FT STRAND 321..324 FT /evidence="ECO:0007829|PDB:2JGD" FT HELIX 326..338 FT /evidence="ECO:0007829|PDB:2JGD" FT STRAND 341..343 FT /evidence="ECO:0007829|PDB:2JGD" FT HELIX 346..348 FT /evidence="ECO:0007829|PDB:2JGD" FT STRAND 349..356 FT /evidence="ECO:0007829|PDB:2JGD" FT HELIX 357..362 FT /evidence="ECO:0007829|PDB:2JGD" FT HELIX 365..372 FT /evidence="ECO:0007829|PDB:2JGD" FT TURN 376..378 FT /evidence="ECO:0007829|PDB:2JGD" FT STRAND 384..389 FT /evidence="ECO:0007829|PDB:2JGD" FT HELIX 408..413 FT /evidence="ECO:0007829|PDB:2JGD" FT TURN 414..416 FT /evidence="ECO:0007829|PDB:2JGD" FT STRAND 419..423 FT /evidence="ECO:0007829|PDB:2JGD" FT HELIX 427..444 FT /evidence="ECO:0007829|PDB:2JGD" FT STRAND 448..453 FT /evidence="ECO:0007829|PDB:2JGD" FT HELIX 474..478 FT /evidence="ECO:0007829|PDB:2JGD" FT HELIX 483..492 FT /evidence="ECO:0007829|PDB:2JGD" FT TURN 493..495 FT /evidence="ECO:0007829|PDB:2JGD" FT HELIX 499..515 FT /evidence="ECO:0007829|PDB:2JGD" FT HELIX 528..530 FT /evidence="ECO:0007829|PDB:2JGD" FT HELIX 534..536 FT /evidence="ECO:0007829|PDB:2JGD" FT HELIX 551..560 FT /evidence="ECO:0007829|PDB:2JGD" FT HELIX 572..585 FT /evidence="ECO:0007829|PDB:2JGD" FT HELIX 593..605 FT /evidence="ECO:0007829|PDB:2JGD" FT TURN 606..608 FT /evidence="ECO:0007829|PDB:2JGD" FT STRAND 611..615 FT /evidence="ECO:0007829|PDB:2JGD" FT TURN 616..620 FT /evidence="ECO:0007829|PDB:2JGD" FT STRAND 629..631 FT /evidence="ECO:0007829|PDB:2JGD" FT STRAND 633..636 FT /evidence="ECO:0007829|PDB:2JGD" FT HELIX 641..643 FT /evidence="ECO:0007829|PDB:2JGD" FT STRAND 652..655 FT /evidence="ECO:0007829|PDB:2JGD" FT HELIX 661..674 FT /evidence="ECO:0007829|PDB:2JGD" FT STRAND 678..683 FT /evidence="ECO:0007829|PDB:2JGD" FT HELIX 687..693 FT /evidence="ECO:0007829|PDB:2JGD" FT HELIX 694..699 FT /evidence="ECO:0007829|PDB:2JGD" FT TURN 700..703 FT /evidence="ECO:0007829|PDB:2JGD" FT HELIX 704..708 FT /evidence="ECO:0007829|PDB:2JGD" FT STRAND 715..719 FT /evidence="ECO:0007829|PDB:2JGD" FT STRAND 723..725 FT /evidence="ECO:0007829|PDB:2JGD" FT HELIX 734..739 FT /evidence="ECO:0007829|PDB:2JGD" FT STRAND 747..749 FT /evidence="ECO:0007829|PDB:2JGD" FT HELIX 754..766 FT /evidence="ECO:0007829|PDB:2JGD" FT STRAND 773..777 FT /evidence="ECO:0007829|PDB:2JGD" FT HELIX 780..783 FT /evidence="ECO:0007829|PDB:2JGD" FT HELIX 791..796 FT /evidence="ECO:0007829|PDB:2JGD" FT STRAND 801..803 FT /evidence="ECO:0007829|PDB:2JGD" FT HELIX 811..813 FT /evidence="ECO:0007829|PDB:2JGD" FT STRAND 816..820 FT /evidence="ECO:0007829|PDB:2JGD" FT HELIX 824..834 FT /evidence="ECO:0007829|PDB:2JGD" FT STRAND 839..845 FT /evidence="ECO:0007829|PDB:2JGD" FT STRAND 847..850 FT /evidence="ECO:0007829|PDB:2JGD" FT HELIX 853..860 FT /evidence="ECO:0007829|PDB:2JGD" FT HELIX 861..863 FT /evidence="ECO:0007829|PDB:2JGD" FT STRAND 868..876 FT /evidence="ECO:0007829|PDB:2JGD" FT STRAND 879..881 FT /evidence="ECO:0007829|PDB:2JGD" FT HELIX 882..890 FT /evidence="ECO:0007829|PDB:2JGD" FT STRAND 898..904 FT /evidence="ECO:0007829|PDB:2JGD" FT STRAND 908..911 FT /evidence="ECO:0007829|PDB:2JGD" FT HELIX 915..930 FT /evidence="ECO:0007829|PDB:2JGD" SQ SEQUENCE 933 AA; 105062 MW; EAEF8429EC31E749 CRC64; MQNSALKAWL DSSYLSGANQ SWIEQLYEDF LTDPDSVDAN WRSTFQQLPG TGVKPDQFHS QTREYFRRLA KDASRYSSTI SDPDTNVKQV KVLQLINAYR FRGHQHANLD PLGLWQQDKV ADLDPSFHDL TEADFQETFN VGSFASGKET MKLGELLEAL KQTYCGPIGA EYMHITSTEE KRWIQQRIES GRATFNSEEK KRFLSELTAA EGLERYLGAK FPGAKRFSLE GGDALIPMLK EMIRHAGNSG TREVVLGMAH RGRLNVLVNV LGKKPQDLFD EFAGKHKEHL GTGDVKYHMG FSSDFQTDGG LVHLALAFNP SHLEIVSPVV IGSVRARLDR LDEPSSNKVL PITIHGDAAV TGQGVVQETL NMSKARGYEV GGTVRIVINN QVGFTTSNPL DARSTPYCTD IGKMVQAPIF HVNADDPEAV AFVTRLALDF RNTFKRDVFI DLVCYRRHGH NEADEPSATQ PLMYQKIKKH PTPRKIYADK LEQEKVATLE DATEMVNLYR DALDAGDCVV AEWRPMNMHS FTWSPYLNHE WDEEYPNKVE MKRLQELAKR ISTVPEAVEM QSRVAKIYGD RQAMAAGEKL FDWGGAENLA YATLVDEGIP VRLSGEDSGR GTFFHRHAVI HNQSNGSTYT PLQHIHNGQG AFRVWDSVLS EEAVLAFEYG YATAEPRTLT IWEAQFGDFA NGAQVVIDQF ISSGEQKWGR MCGLVMLLPH GYEGQGPEHS SARLERYLQL CAEQNMQVCV PSTPAQVYHM LRRQALRGMR RPLVVMSPKS LLRHPLAVSS LEELANGTFL PAIGEIDELD PKGVKRVVMC SGKVYYDLLE QRRKNNQHDV AIVRIEQLYP FPHKAMQEVL QQFAHVKDFV WCQEEPLNQG AWYCSQHHFR EVIPFGASLR YAGRPASASP AVGYMSVHQK QQQDLVNDAL NVE //