ID ODO12_CORGL Reviewed; 1221 AA. AC Q8NRC3; P96746; Q6M641; DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 28-NOV-2012, sequence version 2. DT 27-MAR-2024, entry version 136. DE RecName: Full=2-oxoglutarate dehydrogenase E1/E2 component; DE Short=ODH E1/E2 component; DE Includes: DE RecName: Full=2-oxoglutarate dehydrogenase E1 component; DE Short=ODH E1 component; DE EC=1.2.4.2 {ECO:0000269|PubMed:20675489, ECO:0000269|PubMed:9004499}; DE AltName: Full=Alpha-ketoglutarate dehydrogenase E1 component; DE Short=KDH E1 component; DE Includes: DE RecName: Full=Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex; DE EC=2.3.1.61 {ECO:0000269|PubMed:20675489}; DE AltName: Full=2-oxoglutarate dehydrogenase complex E2 component; DE Short=ODH E2 component; DE Short=OGDC-E2; DE AltName: Full=Dihydrolipoamide succinyltransferase; GN Name=odhA {ECO:0000312|EMBL:CAF19835.1}; GN OrderedLocusNames=Cgl1129, cg1280; OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / OS JCM 1318 / LMG 3730 / NCIMB 10025). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; OC Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=196627; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CATALYTIC ACTIVITY. RC STRAIN=AJ12036; RX PubMed=9004499; DOI=10.1099/13500872-142-12-3347; RA Usuda Y., Tujimoto N., Abe C., Asakura Y., Kimura E., Kawahara Y., RA Kurahashi O., Matsui H.; RT "Molecular cloning of the Corynebacterium glutamicum ('Brevibacterium RT lactofermentum' AJ12036) odhA gene encoding a novel type of 2-oxoglutarate RT dehydrogenase."; RL Microbiology 142:3347-3354(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / RC NCIMB 10025; RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1; RA Ikeda M., Nakagawa S.; RT "The Corynebacterium glutamicum genome: features and impacts on RT biotechnological processes."; RL Appl. Microbiol. Biotechnol. 62:99-109(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / RC NCIMB 10025 {ECO:0000312|EMBL:CAF19835.1}; RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8; RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.; RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its RT impact on the production of L-aspartate-derived amino acids and vitamins."; RL J. Biotechnol. 104:5-25(2003). RN [4] RP PROTEIN SEQUENCE OF 2-8, FUNCTION AS E1 AND E2 COMPONENT OF ODH, CATALYTIC RP ACTIVITY, KINETIC PARAMETERS, DOMAIN, LACK OF LIPOYLATION, ACTIVE SITE, AND RP MUTAGENESIS OF THR-258; HIS-316 AND GLN-320. RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / RC NCIMB 10025; RX PubMed=20675489; DOI=10.1128/jb.00597-10; RA Hoffelder M., Raasch K., van Ooyen J., Eggeling L.; RT "The E2 domain of OdhA of Corynebacterium glutamicum has RT succinyltransferase activity dependent on lipoyl residues of the RT acetyltransferase AceF."; RL J. Bacteriol. 192:5203-5211(2010). RN [5] RP INHIBITION BY ODHI, AND IDENTIFICATION IN THE ODH/PDH COMPLEX. RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / RC NCIMB 10025; RX PubMed=16522631; DOI=10.1074/jbc.m512515200; RA Niebisch A., Kabus A., Schultz C., Weil B., Bott M.; RT "Corynebacterial protein kinase G controls 2-oxoglutarate dehydrogenase RT activity via the phosphorylation status of the OdhI protein."; RL J. Biol. Chem. 281:12300-12307(2006). RN [6] RP DISRUPTION PHENOTYPE. RC STRAIN=ATCC 13869 / DSMZ 1412 / NCIMB 9567; RX PubMed=17158630; DOI=10.1128/aem.01867-06; RA Asakura Y., Kimura E., Usuda Y., Kawahara Y., Matsui K., Osumi T., RA Nakamatsu T.; RT "Altered metabolic flux due to deletion of odhA causes L-glutamate RT overproduction in Corynebacterium glutamicum."; RL Appl. Environ. Microbiol. 73:1308-1319(2007). RN [7] RP DOMAIN, ACTIVITY REGULATION, AND INTERACTION WITH ODHI. RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / RC NCIMB 10025; RX PubMed=20303957; DOI=10.1016/j.febslet.2010.03.028; RA Krawczyk S., Raasch K., Schultz C., Hoffelder M., Eggeling L., Bott M.; RT "The FHA domain of OdhI interacts with the carboxyterminal 2-oxoglutarate RT dehydrogenase domain of OdhA in Corynebacterium glutamicum."; RL FEBS Lett. 584:1463-1468(2010). CC -!- FUNCTION: Catalyzes the E1 and E2 reactions as part of 2-oxoglutarate CC dehydrogenase (ODH) activity, to convert 2-oxoglutarate to succinyl-CoA CC and CO(2). OdhA has reductase activity with 2-oxoglutarate but does not CC react with pyruvate, and also displays transsuccinylase but no CC transacetylase activity. Since OdhA is not lipoylated, the CC succinyltransferase activity of its E2 domain is dependent on lipoyl CC residues of the acetyltransferase AceF. {ECO:0000269|PubMed:20675489}. 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:20675489, ECO:0000269|PubMed:9004499}; CC -!- CATALYTIC ACTIVITY: CC Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase CC complex component E2] + succinyl-CoA = CoA + N(6)-[(R)-S(8)- CC succinyldihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase complex CC component E2]; Xref=Rhea:RHEA:15213, Rhea:RHEA-COMP:10581, Rhea:RHEA- CC COMP:10582, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:83100, CC ChEBI:CHEBI:83120; EC=2.3.1.61; CC Evidence={ECO:0000269|PubMed:20675489}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- COFACTOR: CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; CC Evidence={ECO:0000250|UniProtKB:P0AFG3}; CC -!- ACTIVITY REGULATION: Inhibited by unphosphorylated OdhI, but not by CC phosphorylated OdhI. {ECO:0000269|PubMed:20303957}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.014 mM for 2-oxoglutarate {ECO:0000269|PubMed:20675489}; CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinyl- CC CoA from 2-oxoglutarate (dehydrogenase route): step 1/1. CC -!- SUBUNIT: Homodimer (By similarity). Part of an unusual ODH/PDH CC supercomplex, consisting of AceE (E1), AceF (E2), and Lpd (E3) together CC with OdhA (E1+E2). Interacts with the FHA domain of unphosphorylated CC OdhI via its C-terminal dehydrogenase domain. {ECO:0000250, CC ECO:0000269|PubMed:16522631, ECO:0000269|PubMed:20303957}. CC -!- INTERACTION: CC Q8NRC3; Q8NQJ3: odhI; NbExp=2; IntAct=EBI-7868591, EBI-7868645; CC -!- DOMAIN: OdhA is a fusion protein with two major domains exhibiting CC structural features of an E1 and E2 protein, and a short sequence CC stretch of E1 localized at the N-terminus, which is connected by a CC linker region to the rest of the protein. Deletion of individual parts CC of odhA show that all parts of odhA are required for a functional CC tricarboxylic acid cycle in C.glutamicum; the ODH activity is in fact CC completely abolished in each of these mutants, and the PDH activity is CC significantly reduced, which could indicate that the overall structure CC of the supercomplex is disturbed. {ECO:0000269|PubMed:20303957, CC ECO:0000269|PubMed:20675489}. CC -!- DISRUPTION PHENOTYPE: Strains lacking this gene completely lack 2- CC oxoglutarate dehydrogenase activity. Deletion of odhA also causes L- CC glutamate overproduction and accumulation during growth. CC {ECO:0000269|PubMed:17158630}. CC -!- MISCELLANEOUS: Is non-lipoylated. In contrast, the E2 component AceF is CC the prominent lipoylated protein in C.glutamicum. CC -!- SIMILARITY: In the N-terminal section; belongs to the alpha- CC ketoglutarate dehydrogenase family. {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the 2-oxoacid CC dehydrogenase family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB98522.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=CAF19835.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; D84102; BAA12222.2; -; Genomic_DNA. DR EMBL; BA000036; BAB98522.1; ALT_INIT; Genomic_DNA. DR EMBL; BX927151; CAF19835.1; ALT_INIT; Genomic_DNA. DR RefSeq; NP_600357.3; NC_003450.3. DR RefSeq; WP_011014138.1; NC_006958.1. DR PDB; 8P5S; X-ray; 2.46 A; A=98-1221. DR PDB; 8P5T; EM; 2.17 A; A/B/C/D/E/F=1-1221. DR PDB; 8P5U; EM; 2.17 A; A/B/C/D/E/F=1-1221. DR PDB; 8P5V; EM; 2.07 A; A/B/C/D/E/F=1-1221. DR PDB; 8P5W; EM; 2.26 A; A/B/C/D/E/F=1-1221. DR PDB; 8P5X; EM; 2.29 A; A/B/C/D/E/F=1-1221. DR PDBsum; 8P5S; -. DR PDBsum; 8P5T; -. DR PDBsum; 8P5U; -. DR PDBsum; 8P5V; -. DR PDBsum; 8P5W; -. DR PDBsum; 8P5X; -. DR AlphaFoldDB; Q8NRC3; -. DR EMDB; EMD-17452; -. DR EMDB; EMD-17453; -. DR EMDB; EMD-17454; -. DR EMDB; EMD-17455; -. DR EMDB; EMD-17456; -. DR SMR; Q8NRC3; -. DR IntAct; Q8NRC3; 1. DR MINT; Q8NRC3; -. DR STRING; 196627.cg1280; -. DR KEGG; cgb:cg1280; -. DR KEGG; cgl:Cgl1129; -. DR PATRIC; fig|196627.13.peg.1108; -. DR eggNOG; COG0508; Bacteria. DR eggNOG; COG0567; Bacteria. DR HOGENOM; CLU_004709_1_0_11; -. DR OrthoDB; 9759785at2; -. DR BioCyc; CORYNE:G18NG-10701-MONOMER; -. DR BRENDA; 1.2.1.105; 960. DR SABIO-RK; Q8NRC3; -. DR UniPathway; UPA00223; UER00997. DR Proteomes; UP000000582; Chromosome. DR Proteomes; UP000001009; Chromosome. DR GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt. 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:UniProtKB-UniPathway. DR CDD; cd02016; TPP_E1_OGDC_like; 1. DR Gene3D; 3.40.50.12470; -; 1. DR Gene3D; 3.40.50.970; -; 1. DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 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; IPR001078; 2-oxoacid_DH_actylTfrase. DR InterPro; IPR032106; 2-oxogl_dehyd_N. DR InterPro; IPR011603; 2oxoglutarate_DH_E1. DR InterPro; IPR023213; CAT-like_dom_sf. 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; PF00198; 2-oxoacid_dh; 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; SSF52777; CoA-dependent acyltransferases; 1. DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2. PE 1: Evidence at protein level; KW 3D-structure; Acyltransferase; Direct protein sequencing; Magnesium; KW Metal-binding; Multifunctional enzyme; Oxidoreductase; Reference proteome; KW Thiamine pyrophosphate; Transferase; Tricarboxylic acid cycle. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:20675489" FT CHAIN 2..1221 FT /note="2-oxoglutarate dehydrogenase E1/E2 component" FT /id="PRO_0000273521" FT REGION 2..40 FT /note="2-oxoglutarate dehydrogenase E1, N-terminal part" FT REGION 22..107 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 41..89 FT /note="Linker" FT REGION 90..337 FT /note="Succinyltransferase E2" FT REGION 338..1221 FT /note="2-oxoglutarate dehydrogenase E1, C-terminal part" FT COMPBIAS 22..36 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 41..55 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 316 FT /note="Proton acceptor; for succinyltransferase activity" FT /evidence="ECO:0000269|PubMed:20675489" FT BINDING 544 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000250|UniProtKB:A0R2B1" FT BINDING 583 FT /ligand="2-oxoglutarate" FT /ligand_id="ChEBI:CHEBI:16810" FT /evidence="ECO:0000250|UniProtKB:A0R2B1" FT BINDING 608 FT /ligand="2-oxoglutarate" FT /ligand_id="ChEBI:CHEBI:16810" FT /evidence="ECO:0000250|UniProtKB:A0R2B1" FT BINDING 608 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000250|UniProtKB:A0R2B1" FT BINDING 610 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000250|UniProtKB:A0R2B1" FT BINDING 645 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:A0R2B1" FT BINDING 645 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000250|UniProtKB:A0R2B1" FT BINDING 646 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000250|UniProtKB:A0R2B1" FT BINDING 647 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000250|UniProtKB:A0R2B1" FT BINDING 678 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:A0R2B1" FT BINDING 678 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000250|UniProtKB:A0R2B1" FT BINDING 680 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:A0R2B1" FT BINDING 1017 FT /ligand="2-oxoglutarate" FT /ligand_id="ChEBI:CHEBI:16810" FT /evidence="ECO:0000250|UniProtKB:A0R2B1" FT BINDING 1035 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /ligand_note="allosteric activator" FT /evidence="ECO:0000250|UniProtKB:A0R2B1" FT BINDING 1051 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /ligand_note="allosteric activator" FT /evidence="ECO:0000250|UniProtKB:A0R2B1" FT BINDING 1087 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /ligand_note="allosteric activator" FT /evidence="ECO:0000250|UniProtKB:A0R2B1" FT BINDING 1090 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /ligand_note="allosteric activator" FT /evidence="ECO:0000250|UniProtKB:A0R2B1" FT BINDING 1144 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /ligand_note="allosteric activator" FT /evidence="ECO:0000250|UniProtKB:A0R2B1" FT MUTAGEN 258 FT /note="T->A: Loss of E2 succinyltransferase activity, but FT nearly no effect on E1 dehydrogenase activity." FT /evidence="ECO:0000269|PubMed:20675489" FT MUTAGEN 316 FT /note="H->C: Loss of E2 succinyltransferase activity, and FT 2-fold reduction in E1 dehydrogenase activity." FT /evidence="ECO:0000269|PubMed:20675489" FT MUTAGEN 320 FT /note="Q->D: Slight reduction in E2 succinyltransferase FT activity and in E1 dehydrogenase activity." FT /evidence="ECO:0000269|PubMed:20675489" FT CONFLICT 44 FT /note="T -> A (in Ref. 1; BAA12222)" FT /evidence="ECO:0000305" FT CONFLICT 82 FT /note="D -> A (in Ref. 1; BAA12222)" FT /evidence="ECO:0000305" FT CONFLICT 238 FT /note="A -> T (in Ref. 1; BAA12222)" FT /evidence="ECO:0000305" FT CONFLICT 413 FT /note="N -> S (in Ref. 1; BAA12222)" FT /evidence="ECO:0000305" FT CONFLICT 424 FT /note="N -> S (in Ref. 1; BAA12222)" FT /evidence="ECO:0000305" FT CONFLICT 967 FT /note="I -> V (in Ref. 1; BAA12222)" FT /evidence="ECO:0000305" FT CONFLICT 1093 FT /note="N -> D (in Ref. 1; BAA12222)" FT /evidence="ECO:0000305" FT STRAND 103..106 FT /evidence="ECO:0007829|PDB:8P5V" FT HELIX 110..120 FT /evidence="ECO:0007829|PDB:8P5V" FT HELIX 121..123 FT /evidence="ECO:0007829|PDB:8P5V" FT STRAND 126..134 FT /evidence="ECO:0007829|PDB:8P5V" FT HELIX 136..152 FT /evidence="ECO:0007829|PDB:8P5V" FT HELIX 159..173 FT /evidence="ECO:0007829|PDB:8P5V" FT HELIX 175..178 FT /evidence="ECO:0007829|PDB:8P5V" FT STRAND 180..184 FT /evidence="ECO:0007829|PDB:8P5V" FT STRAND 187..192 FT /evidence="ECO:0007829|PDB:8P5V" FT STRAND 198..205 FT /evidence="ECO:0007829|PDB:8P5V" FT STRAND 207..209 FT /evidence="ECO:0007829|PDB:8P5T" FT STRAND 211..218 FT /evidence="ECO:0007829|PDB:8P5V" FT HELIX 221..223 FT /evidence="ECO:0007829|PDB:8P5V" FT HELIX 226..242 FT /evidence="ECO:0007829|PDB:8P5V" FT HELIX 247..250 FT /evidence="ECO:0007829|PDB:8P5V" FT STRAND 255..258 FT /evidence="ECO:0007829|PDB:8P5V" FT HELIX 260..262 FT /evidence="ECO:0007829|PDB:8P5V" FT STRAND 266..269 FT /evidence="ECO:0007829|PDB:8P5V" FT STRAND 277..282 FT /evidence="ECO:0007829|PDB:8P5V" FT HELIX 289..291 FT /evidence="ECO:0007829|PDB:8P5V" FT HELIX 296..302 FT /evidence="ECO:0007829|PDB:8P5V" FT STRAND 307..315 FT /evidence="ECO:0007829|PDB:8P5V" FT TURN 316..318 FT /evidence="ECO:0007829|PDB:8P5V" FT HELIX 321..334 FT /evidence="ECO:0007829|PDB:8P5V" FT HELIX 338..348 FT /evidence="ECO:0007829|PDB:8P5V" FT HELIX 368..382 FT /evidence="ECO:0007829|PDB:8P5V" FT HELIX 383..386 FT /evidence="ECO:0007829|PDB:8P5V" FT STRAND 391..393 FT /evidence="ECO:0007829|PDB:8P5V" FT STRAND 397..399 FT /evidence="ECO:0007829|PDB:8P5X" FT HELIX 405..407 FT /evidence="ECO:0007829|PDB:8P5V" FT HELIX 409..412 FT /evidence="ECO:0007829|PDB:8P5V" FT HELIX 416..418 FT /evidence="ECO:0007829|PDB:8P5V" FT STRAND 421..424 FT /evidence="ECO:0007829|PDB:8P5V" FT HELIX 428..430 FT /evidence="ECO:0007829|PDB:8P5V" FT STRAND 432..435 FT /evidence="ECO:0007829|PDB:8P5V" FT HELIX 436..447 FT /evidence="ECO:0007829|PDB:8P5V" FT STRAND 448..454 FT /evidence="ECO:0007829|PDB:8P5V" FT HELIX 461..473 FT /evidence="ECO:0007829|PDB:8P5V" FT HELIX 480..503 FT /evidence="ECO:0007829|PDB:8P5V" FT STRAND 505..507 FT /evidence="ECO:0007829|PDB:8P5T" FT HELIX 508..510 FT /evidence="ECO:0007829|PDB:8P5S" FT HELIX 518..531 FT /evidence="ECO:0007829|PDB:8P5V" FT STRAND 536..540 FT /evidence="ECO:0007829|PDB:8P5V" FT HELIX 546..552 FT /evidence="ECO:0007829|PDB:8P5V" FT HELIX 558..566 FT /evidence="ECO:0007829|PDB:8P5V" FT HELIX 581..583 FT /evidence="ECO:0007829|PDB:8P5V" FT STRAND 586..591 FT /evidence="ECO:0007829|PDB:8P5V" FT STRAND 598..603 FT /evidence="ECO:0007829|PDB:8P5V" FT TURN 610..612 FT /evidence="ECO:0007829|PDB:8P5V" FT HELIX 613..628 FT /evidence="ECO:0007829|PDB:8P5V" FT STRAND 637..644 FT /evidence="ECO:0007829|PDB:8P5V" FT HELIX 645..650 FT /evidence="ECO:0007829|PDB:8P5V" FT HELIX 653..658 FT /evidence="ECO:0007829|PDB:8P5V" FT TURN 659..662 FT /evidence="ECO:0007829|PDB:8P5V" FT TURN 664..666 FT /evidence="ECO:0007829|PDB:8P5V" FT STRAND 672..677 FT /evidence="ECO:0007829|PDB:8P5V" FT STRAND 681..683 FT /evidence="ECO:0007829|PDB:8P5V" FT HELIX 686..688 FT /evidence="ECO:0007829|PDB:8P5V" FT STRAND 691..694 FT /evidence="ECO:0007829|PDB:8P5V" FT HELIX 695..697 FT /evidence="ECO:0007829|PDB:8P5V" FT HELIX 698..702 FT /evidence="ECO:0007829|PDB:8P5V" FT STRAND 706..710 FT /evidence="ECO:0007829|PDB:8P5V" FT HELIX 714..731 FT /evidence="ECO:0007829|PDB:8P5V" FT STRAND 735..740 FT /evidence="ECO:0007829|PDB:8P5V" FT STRAND 747..750 FT /evidence="ECO:0007829|PDB:8P5S" FT TURN 753..756 FT /evidence="ECO:0007829|PDB:8P5V" FT HELIX 760..764 FT /evidence="ECO:0007829|PDB:8P5V" FT HELIX 770..780 FT /evidence="ECO:0007829|PDB:8P5V" FT HELIX 786..809 FT /evidence="ECO:0007829|PDB:8P5V" FT HELIX 837..845 FT /evidence="ECO:0007829|PDB:8P5V" FT TURN 846..848 FT /evidence="ECO:0007829|PDB:8P5V" FT TURN 858..860 FT /evidence="ECO:0007829|PDB:8P5V" FT HELIX 861..873 FT /evidence="ECO:0007829|PDB:8P5V" FT HELIX 878..892 FT /evidence="ECO:0007829|PDB:8P5V" FT STRAND 895..900 FT /evidence="ECO:0007829|PDB:8P5V" FT TURN 901..905 FT /evidence="ECO:0007829|PDB:8P5V" FT STRAND 913..916 FT /evidence="ECO:0007829|PDB:8P5V" FT TURN 918..920 FT /evidence="ECO:0007829|PDB:8P5V" FT HELIX 926..932 FT /evidence="ECO:0007829|PDB:8P5V" FT STRAND 934..936 FT /evidence="ECO:0007829|PDB:8P5V" FT STRAND 939..944 FT /evidence="ECO:0007829|PDB:8P5V" FT HELIX 950..962 FT /evidence="ECO:0007829|PDB:8P5V" FT STRAND 966..971 FT /evidence="ECO:0007829|PDB:8P5V" FT HELIX 975..981 FT /evidence="ECO:0007829|PDB:8P5V" FT HELIX 982..987 FT /evidence="ECO:0007829|PDB:8P5V" FT TURN 988..991 FT /evidence="ECO:0007829|PDB:8P5V" FT HELIX 992..996 FT /evidence="ECO:0007829|PDB:8P5V" FT STRAND 1003..1007 FT /evidence="ECO:0007829|PDB:8P5V" FT STRAND 1011..1013 FT /evidence="ECO:0007829|PDB:8P5V" FT HELIX 1022..1028 FT /evidence="ECO:0007829|PDB:8P5V" FT STRAND 1035..1037 FT /evidence="ECO:0007829|PDB:8P5V" FT HELIX 1042..1054 FT /evidence="ECO:0007829|PDB:8P5V" FT STRAND 1061..1065 FT /evidence="ECO:0007829|PDB:8P5V" FT HELIX 1069..1071 FT /evidence="ECO:0007829|PDB:8P5V" FT HELIX 1073..1075 FT /evidence="ECO:0007829|PDB:8P5V" FT HELIX 1080..1083 FT /evidence="ECO:0007829|PDB:8P5V" FT STRAND 1090..1092 FT /evidence="ECO:0007829|PDB:8P5V" FT HELIX 1100..1102 FT /evidence="ECO:0007829|PDB:8P5V" FT STRAND 1105..1109 FT /evidence="ECO:0007829|PDB:8P5V" FT HELIX 1113..1124 FT /evidence="ECO:0007829|PDB:8P5V" FT STRAND 1129..1134 FT /evidence="ECO:0007829|PDB:8P5V" FT STRAND 1136..1139 FT /evidence="ECO:0007829|PDB:8P5V" FT HELIX 1142..1150 FT /evidence="ECO:0007829|PDB:8P5V" FT STRAND 1157..1165 FT /evidence="ECO:0007829|PDB:8P5V" FT HELIX 1171..1181 FT /evidence="ECO:0007829|PDB:8P5V" FT STRAND 1188..1193 FT /evidence="ECO:0007829|PDB:8P5V" FT STRAND 1197..1200 FT /evidence="ECO:0007829|PDB:8P5V" FT HELIX 1204..1218 FT /evidence="ECO:0007829|PDB:8P5V" SQ SEQUENCE 1221 AA; 134664 MW; BF0A1827EA1B0080 CRC64; MSSASTFGQN AWLVDEMFQQ FQKDPKSVDK EWRELFEAQG GPNTTPATTE AQPSAPKESA KPAPKAAPAA KAAPRVETKP ADKTAPKAKE SSVPQQPKLP EPGQTPIRGI FKSIAKNMDI SLEIPTATSV RDMPARLMFE NRAMVNDQLK RTRGGKISFT HIIGYAMVKA VMAHPDMNNS YDVIDGKPTL IVPEHINLGL AIDLPQKDGS RALVVAAIKE TEKMNFSEFL AAYEDIVARS RKGKLTMDDY QGVTVSLTNP GGIGTRHSVP RLTKGQGTII GVGSMDYPAE FQGASEDRLA ELGVGKLVTI TSTYDHRVIQ GAVSGEFLRT MSRLLTDDSF WDEIFDAMNV PYTPMRWAQD VPNTGVDKNT RVMQLIEAYR SRGHLIADTN PLSWVQPGMP VPDHRDLDIE THNLTIWDLD RTFNVGGFGG KETMTLREVL SRLRAAYTLK VGSEYTHILD RDERTWLQDR LEAGMPKPTQ AEQKYILQKL NAAEAFENFL QTKYVGQKRF SLEGAEALIP LMDSAIDTAA GQGLDEVVIG MPHRGRLNVL FNIVGKPLAS IFNEFEGQME QGQIGGSGDV KYHLGSEGQH LQMFGDGEIK VSLTANPSHL EAVNPVMEGI VRAKQDYLDK GVDGKTVVPL LLHGDAAFAG LGIVPETINL AKLRGYDVGG TIHIVVNNQI GFTTTPDSSR SMHYATDYAK AFGCPVFHVN GDDPEAVVWV GQLATEYRRR FGKDVFIDLV CYRLRGHNEA DDPSMTQPKM YELITGRETV RAQYTEDLLG RGDLSNEDAE AVVRDFHDQM ESVFNEVKEG GKKQAEAQTG ITGSQKLPHG LETNISREEL LELGQAFANT PEGFNYHPRV APVAKKRVSS VTEGGIDWAW GELLAFGSLA NSGRLVRLAG EDSRRGTFTQ RHAVAIDPAT AEEFNPLHEL AQSKGNNGKF LVYNSALTEY AGMGFEYGYS VGNEDSIVAW EAQFGDFANG AQTIIDEYVS SGEAKWGQTS KLILLLPHGY EGQGPDHSSA RIERFLQLCA EGSMTVAQPS TPANHFHLLR RHALSDLKRP LVIFTPKSML RNKAAASAPE DFTEVTKFQS VINDPNVADA AKVKKVMLVS GKLYYELAKR KEKDGRDDIA IVRIEMLHPI PFNRISEALA GYPNAEEVLF VQDEPANQGP WPFYQEHLPE LIPNMPKMRR VSRRAQSSTA TGVAKVHQLE EKQLIDEAFE A //