ID SDHA_ECOLI Reviewed; 588 AA. AC P0AC41; P10444; P78282; DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 08-NOV-2005, sequence version 1. DT 27-MAR-2024, entry version 151. DE RecName: Full=Succinate dehydrogenase flavoprotein subunit; DE EC=1.3.5.1 {ECO:0000305|PubMed:19710024}; GN Name=sdhA; OrderedLocusNames=b0723, JW0713; 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=6383359; DOI=10.1042/bj2220519; RA Wood D., Darlison M.G., Wilde R.J., Guest J.R.; RT "Nucleotide sequence encoding the flavoprotein and hydrophobic subunits of RT the succinate dehydrogenase of Escherichia coli."; RL Biochem. J. 222:519-534(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 578-588. RC STRAIN=K12; RX PubMed=6388571; DOI=10.1042/bj2230507; RA Darlison M.G., Guest J.R.; RT "Nucleotide sequence encoding the iron-sulphur protein subunit of the RT succinate dehydrogenase of Escherichia coli."; RL Biochem. J. 223:507-517(1984). RN [6] RP PROTEIN SEQUENCE OF 1-12. RC STRAIN=K12 / EMG2; RX PubMed=9298646; DOI=10.1002/elps.1150180807; RA Link A.J., Robison K., Church G.M.; RT "Comparing the predicted and observed properties of proteins encoded in the RT genome of Escherichia coli K-12."; RL Electrophoresis 18:1259-1313(1997). RN [7] RP PROTEIN SEQUENCE OF 1-4. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=9600841; DOI=10.1006/jmbi.1998.1726; RA Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C., RA Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L., RA Hochstrasser D.F.; RT "Protein identification with N and C-terminal sequence tags in proteome RT projects."; RL J. Mol. Biol. 278:599-608(1998). RN [8] 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 [9] RP SUBUNIT, AND SUBCELLULAR LOCATION. RC STRAIN=BL21-DE3; RX PubMed=16079137; DOI=10.1074/jbc.m506479200; RA Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L., RA von Heijne G., Daley D.O.; RT "Protein complexes of the Escherichia coli cell envelope."; RL J. Biol. Chem. 280:34409-34419(2005). RN [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-267, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076; RX PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200; RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., RA Grishin N.V., Zhao Y.; RT "Lysine acetylation is a highly abundant and evolutionarily conserved RT modification in Escherichia coli."; RL Mol. Cell. Proteomics 8:215-225(2009). RN [11] RP FUNCTION, AND DISRUPTION PHENOTYPE. RC STRAIN=K12 / BW25113; RX PubMed=24374335; DOI=10.1016/j.febslet.2013.12.019; RA McNeil M.B., Hampton H.G., Hards K.J., Watson B.N., Cook G.M., RA Fineran P.C.; RT "The succinate dehydrogenase assembly factor, SdhE, is required for the RT flavinylation and activation of fumarate reductase in bacteria."; RL FEBS Lett. 588:414-421(2014). RN [12] RP COFACTOR, SUBUNIT, AND MUTAGENESIS OF GLU-186 AND THR-187. RC STRAIN=K12 / RP437; RX PubMed=26644464; DOI=10.1074/jbc.m115.690396; RA Maklashina E., Rajagukguk S., Starbird C.A., McDonald W.H., Koganitsky A., RA Eisenbach M., Iverson T.M., Cecchini G.; RT "Binding of the covalent flavin assembly factor to the flavoprotein subunit RT of complex II."; RL J. Biol. Chem. 291:2904-2916(2016). RN [13] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH FAD AND OXALOACETATE, RP FUNCTION, COFACTOR, ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND SUBUNIT. RX PubMed=12560550; DOI=10.1126/science.1079605; RA Yankovskaya V., Horsefield R., Toernroth S., Luna-Chavez C., Miyoshi H., RA Leger C., Byrne B., Cecchini G., Iwata S.; RT "Architecture of succinate dehydrogenase and reactive oxygen species RT generation."; RL Science 299:700-704(2003). RN [14] RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH FAD AND OXALOACETATE, RP FUNCTION, COFACTOR, AND SUBUNIT. RX PubMed=16407191; DOI=10.1074/jbc.m508173200; RA Horsefield R., Yankovskaya V., Sexton G., Whittingham W., Shiomi K., RA Omura S., Byrne B., Cecchini G., Iwata S.; RT "Structural and computational analysis of the quinone-binding site of RT complex II (succinate-ubiquinone oxidoreductase): a mechanism of electron RT transfer and proton conduction during ubiquinone reduction."; RL J. Biol. Chem. 281:7309-7316(2006). RN [15] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH FAD AND MALATE-LIKE RP INTERMEDIATE, FUNCTION, COFACTOR, CATALYTIC ACTIVITY, PATHWAY, SUBUNIT, AND RP ACTIVE SITE. RX PubMed=19710024; DOI=10.1074/jbc.m109.010058; RA Ruprecht J., Yankovskaya V., Maklashina E., Iwata S., Cecchini G.; RT "Structure of Escherichia coli succinate:quinone oxidoreductase with an RT occupied and empty quinone-binding site."; RL J. Biol. Chem. 284:29836-29846(2009). CC -!- FUNCTION: Two distinct, membrane-bound, FAD-containing enzymes are CC responsible for the catalysis of fumarate and succinate CC interconversion; the fumarate reductase is used in anaerobic growth, CC and the succinate dehydrogenase is used in aerobic growth. CC {ECO:0000269|PubMed:24374335, ECO:0000305|PubMed:12560550, CC ECO:0000305|PubMed:16407191, ECO:0000305|PubMed:19710024}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a quinone + succinate = a quinol + fumarate; CC Xref=Rhea:RHEA:40523, ChEBI:CHEBI:24646, ChEBI:CHEBI:29806, CC ChEBI:CHEBI:30031, ChEBI:CHEBI:132124; EC=1.3.5.1; CC Evidence={ECO:0000305|PubMed:19710024}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000269|PubMed:12560550, ECO:0000269|PubMed:16407191, CC ECO:0000269|PubMed:19710024}; CC Note=Flavinylated by SdhE, about 5% flavinylation occurs in the absence CC of SdhE. {ECO:0000269|PubMed:26644464}; CC -!- ACTIVITY REGULATION: Inhibited by oxaloacetate. CC {ECO:0000269|PubMed:12560550}. CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; fumarate CC from succinate (bacterial route): step 1/1. CC {ECO:0000305|PubMed:19710024}. CC -!- SUBUNIT: Part of an enzyme complex containing four subunits: a CC flavoprotein, an iron-sulfur, cytochrome b-556, and a hydrophobic CC anchor protein. The complex forms trimers. Can be cross-linked to SdhE CC (PubMed:26644464). {ECO:0000269|PubMed:12560550, CC ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:16407191, CC ECO:0000269|PubMed:19710024, ECO:0000269|PubMed:26644464}. CC -!- INTERACTION: CC P0AC41; P07014: sdhB; NbExp=2; IntAct=EBI-371263, EBI-1035514; CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:12560550, CC ECO:0000269|PubMed:16079137}; Peripheral membrane protein CC {ECO:0000269|PubMed:12560550, ECO:0000269|PubMed:16079137}; Cytoplasmic CC side {ECO:0000269|PubMed:12560550, ECO:0000269|PubMed:16079137}. CC -!- DISRUPTION PHENOTYPE: No effect on anaerobic growth on glycerol CC fumarate medium. {ECO:0000269|PubMed:18723842}. CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family. CC FRD/SDH subfamily. {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; AAA23895.1; -; Genomic_DNA. DR EMBL; X00980; CAA25487.1; -; Genomic_DNA. DR EMBL; U00096; AAC73817.1; -; Genomic_DNA. DR EMBL; AP009048; BAA35390.1; -; Genomic_DNA. DR EMBL; X01070; CAA25533.1; -; Genomic_DNA. DR PIR; B64808; DEECSF. DR RefSeq; NP_415251.1; NC_000913.3. DR RefSeq; WP_000775540.1; NZ_STEB01000035.1. DR PDB; 1NEK; X-ray; 2.60 A; A=1-588. DR PDB; 1NEN; X-ray; 2.90 A; A=1-588. DR PDB; 2ACZ; X-ray; 3.10 A; A=1-588. DR PDB; 2WDQ; X-ray; 2.40 A; A/E/I=1-588. DR PDB; 2WDR; X-ray; 3.20 A; A/E/I=1-588. DR PDB; 2WDV; X-ray; 3.20 A; A/E/I=1-588. DR PDB; 2WP9; X-ray; 2.70 A; A/E/I=1-588. DR PDB; 2WS3; X-ray; 3.20 A; A/E/I=1-588. DR PDB; 2WU2; X-ray; 2.50 A; A/E/I=1-588. DR PDB; 2WU5; X-ray; 2.80 A; A/E/I=1-588. DR PDB; 6C12; X-ray; 2.15 A; A/B=1-588. DR PDB; 7JZ2; EM; 2.50 A; A/E/I=1-588. DR PDBsum; 1NEK; -. DR PDBsum; 1NEN; -. DR PDBsum; 2ACZ; -. DR PDBsum; 2WDQ; -. DR PDBsum; 2WDR; -. DR PDBsum; 2WDV; -. DR PDBsum; 2WP9; -. DR PDBsum; 2WS3; -. DR PDBsum; 2WU2; -. DR PDBsum; 2WU5; -. DR PDBsum; 6C12; -. DR PDBsum; 7JZ2; -. DR AlphaFoldDB; P0AC41; -. DR EMDB; EMD-22528; -. DR SMR; P0AC41; -. DR BioGRID; 4262907; 31. DR BioGRID; 849776; 2. DR ComplexPortal; CPX-1931; Respiratory chain complex II. DR DIP; DIP-31877N; -. DR IntAct; P0AC41; 91. DR MINT; P0AC41; -. DR STRING; 511145.b0723; -. DR DrugBank; DB07671; 2-[1-METHYLHEXYL]-4,6-DINITROPHENOL. DR DrugBank; DB04631; Atpenin A5. DR DrugBank; DB08690; Ubiquinone Q2. DR iPTMnet; P0AC41; -. DR jPOST; P0AC41; -. DR PaxDb; 511145-b0723; -. DR EnsemblBacteria; AAC73817; AAC73817; b0723. DR GeneID; 75205555; -. DR GeneID; 945402; -. DR KEGG; ecj:JW0713; -. DR KEGG; eco:b0723; -. DR PATRIC; fig|1411691.4.peg.1549; -. DR EchoBASE; EB0924; -. DR eggNOG; COG1053; Bacteria. DR HOGENOM; CLU_014312_6_1_6; -. DR InParanoid; P0AC41; -. DR OMA; FHPTGIW; -. DR OrthoDB; 9806724at2; -. DR PhylomeDB; P0AC41; -. DR BioCyc; EcoCyc:SDH-FLAVO; -. DR BioCyc; MetaCyc:SDH-FLAVO; -. DR BRENDA; 1.3.5.1; 2026. DR UniPathway; UPA00223; UER01005. DR EvolutionaryTrace; P0AC41; -. DR PHI-base; PHI:7964; -. DR PRO; PR:P0AC41; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0016020; C:membrane; NAS:ComplexPortal. DR GO; GO:0005886; C:plasma membrane; IDA:EcoliWiki. DR GO; GO:0045282; C:plasma membrane succinate dehydrogenase complex; IDA:EcoliWiki. DR GO; GO:0045281; C:succinate dehydrogenase complex; IPI:ComplexPortal. DR GO; GO:0009055; F:electron transfer activity; IDA:EcoCyc. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:EcoliWiki. DR GO; GO:0102040; F:fumarate reductase (menaquinone); IEA:UniProtKB-EC. DR GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC. DR GO; GO:0000104; F:succinate dehydrogenase activity; IMP:EcoliWiki. DR GO; GO:0019646; P:aerobic electron transport chain; NAS:ComplexPortal. DR GO; GO:0009060; P:aerobic respiration; IGI:EcoliWiki. DR GO; GO:0009061; P:anaerobic respiration; IBA:GO_Central. DR GO; GO:0006099; P:tricarboxylic acid cycle; IGI:EcoliWiki. DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1. DR Gene3D; 1.20.58.100; Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal domain; 1. DR Gene3D; 4.10.80.40; succinate dehydrogenase protein domain; 1. DR Gene3D; 3.90.700.10; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1. DR InterPro; IPR003953; FAD-binding_2. DR InterPro; IPR036188; FAD/NAD-bd_sf. DR InterPro; IPR003952; FRD_SDH_FAD_BS. DR InterPro; IPR037099; Fum_R/Succ_DH_flav-like_C_sf. DR InterPro; IPR015939; Fum_Rdtase/Succ_DH_flav-like_C. DR InterPro; IPR030664; SdhA/FrdA/AprA. DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf. DR InterPro; IPR011281; Succ_DH_flav_su_fwd. DR InterPro; IPR014006; Succ_Dhase_FrdA_Gneg. DR NCBIfam; TIGR01816; sdhA_forward; 1. DR NCBIfam; TIGR01812; sdhA_frdA_Gneg; 1. DR PANTHER; PTHR11632; SUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT; 1. DR PANTHER; PTHR11632:SF51; SUCCINATE DEHYDROGENASE [UBIQUINONE] FLAVOPROTEIN SUBUNIT, MITOCHONDRIAL; 1. DR Pfam; PF00890; FAD_binding_2; 1. DR Pfam; PF02910; Succ_DH_flav_C; 1. DR PIRSF; PIRSF000171; SDHA_APRA_LASPO; 1. DR PRINTS; PR00368; FADPNR. DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1. DR SUPFAM; SSF46977; Succinate dehydrogenase/fumarate reductase flavoprotein C-terminal domain; 1. DR SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1. DR PROSITE; PS00504; FRD_SDH_FAD_BINDING; 1. DR SWISS-2DPAGE; P0AC41; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cell inner membrane; Cell membrane; KW Direct protein sequencing; Electron transport; FAD; Flavoprotein; Membrane; KW Oxidoreductase; Reference proteome; Transport; Tricarboxylic acid cycle. FT CHAIN 1..588 FT /note="Succinate dehydrogenase flavoprotein subunit" FT /id="PRO_0000158652" FT ACT_SITE 286 FT /note="Proton acceptor" FT /evidence="ECO:0000269|PubMed:19710024" FT BINDING 14..19 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:12560550, FT ECO:0000269|PubMed:16407191, ECO:0000269|PubMed:19710024" FT BINDING 37..52 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:12560550, FT ECO:0000269|PubMed:16407191, ECO:0000269|PubMed:19710024" FT BINDING 221 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:12560550, FT ECO:0000269|PubMed:16407191, ECO:0000269|PubMed:19710024" FT BINDING 242 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:19710024" FT BINDING 254 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:19710024" FT BINDING 354 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:19710024" FT BINDING 388 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:12560550, FT ECO:0000269|PubMed:16407191, ECO:0000269|PubMed:19710024" FT BINDING 399 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:19710024" FT BINDING 404..405 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:12560550, FT ECO:0000269|PubMed:16407191, ECO:0000269|PubMed:19710024" FT MOD_RES 45 FT /note="Tele-8alpha-FAD histidine" FT /evidence="ECO:0000269|PubMed:12560550, FT ECO:0000269|PubMed:16407191, ECO:0000269|PubMed:19710024" FT MOD_RES 267 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:18723842" FT MUTAGEN 186 FT /note="E->M: Allows recovery of protein cross-linked to FT SdhE, SdhA is flavinylated." FT /evidence="ECO:0000269|PubMed:26644464" FT MUTAGEN 187 FT /note="T->M: No recovery of protein cross-linked to SdhE, FT SdhA is flavinylated." FT /evidence="ECO:0000269|PubMed:26644464" FT CONFLICT 20..22 FT /note="MRA -> IAR (in Ref. 1; AAA23895/CAA25487)" FT /evidence="ECO:0000305" FT STRAND 5..13 FT /evidence="ECO:0007829|PDB:6C12" FT HELIX 17..28 FT /evidence="ECO:0007829|PDB:6C12" FT STRAND 33..39 FT /evidence="ECO:0007829|PDB:6C12" FT HELIX 41..43 FT /evidence="ECO:0007829|PDB:6C12" FT HELIX 45..48 FT /evidence="ECO:0007829|PDB:6C12" FT STRAND 59..61 FT /evidence="ECO:0007829|PDB:2WDQ" FT HELIX 65..75 FT /evidence="ECO:0007829|PDB:6C12" FT TURN 76..78 FT /evidence="ECO:0007829|PDB:6C12" FT HELIX 82..100 FT /evidence="ECO:0007829|PDB:6C12" FT TURN 101..103 FT /evidence="ECO:0007829|PDB:2ACZ" FT STRAND 112..114 FT /evidence="ECO:0007829|PDB:2WDQ" FT STRAND 119..121 FT /evidence="ECO:0007829|PDB:1NEK" FT TURN 125..127 FT /evidence="ECO:0007829|PDB:2WDQ" FT STRAND 129..135 FT /evidence="ECO:0007829|PDB:1NEK" FT HELIX 141..155 FT /evidence="ECO:0007829|PDB:6C12" FT STRAND 159..162 FT /evidence="ECO:0007829|PDB:6C12" FT STRAND 164..171 FT /evidence="ECO:0007829|PDB:6C12" FT STRAND 177..184 FT /evidence="ECO:0007829|PDB:6C12" FT TURN 185..187 FT /evidence="ECO:0007829|PDB:6C12" FT STRAND 190..200 FT /evidence="ECO:0007829|PDB:6C12" FT HELIX 206..208 FT /evidence="ECO:0007829|PDB:6C12" FT STRAND 209..214 FT /evidence="ECO:0007829|PDB:6C12" FT HELIX 221..228 FT /evidence="ECO:0007829|PDB:6C12" FT STRAND 233..235 FT /evidence="ECO:0007829|PDB:7JZ2" FT STRAND 239..246 FT /evidence="ECO:0007829|PDB:6C12" FT TURN 247..249 FT /evidence="ECO:0007829|PDB:6C12" FT HELIX 256..259 FT /evidence="ECO:0007829|PDB:6C12" FT STRAND 263..265 FT /evidence="ECO:0007829|PDB:6C12" FT HELIX 273..276 FT /evidence="ECO:0007829|PDB:6C12" FT TURN 278..280 FT /evidence="ECO:0007829|PDB:6C12" FT HELIX 281..283 FT /evidence="ECO:0007829|PDB:6C12" FT HELIX 286..298 FT /evidence="ECO:0007829|PDB:6C12" FT STRAND 305..307 FT /evidence="ECO:0007829|PDB:1NEK" FT STRAND 309..314 FT /evidence="ECO:0007829|PDB:6C12" FT HELIX 316..318 FT /evidence="ECO:0007829|PDB:6C12" FT HELIX 320..326 FT /evidence="ECO:0007829|PDB:6C12" FT HELIX 328..337 FT /evidence="ECO:0007829|PDB:6C12" FT TURN 342..344 FT /evidence="ECO:0007829|PDB:6C12" FT STRAND 347..356 FT /evidence="ECO:0007829|PDB:6C12" FT STRAND 359..362 FT /evidence="ECO:0007829|PDB:6C12" FT STRAND 367..371 FT /evidence="ECO:0007829|PDB:6C12" FT STRAND 373..375 FT /evidence="ECO:0007829|PDB:1NEK" FT STRAND 377..385 FT /evidence="ECO:0007829|PDB:6C12" FT HELIX 387..389 FT /evidence="ECO:0007829|PDB:2WDQ" FT STRAND 393..395 FT /evidence="ECO:0007829|PDB:2WDQ" FT HELIX 403..417 FT /evidence="ECO:0007829|PDB:6C12" FT HELIX 419..426 FT /evidence="ECO:0007829|PDB:6C12" FT HELIX 434..439 FT /evidence="ECO:0007829|PDB:6C12" FT HELIX 442..448 FT /evidence="ECO:0007829|PDB:6C12" FT STRAND 451..454 FT /evidence="ECO:0007829|PDB:6C12" FT HELIX 456..471 FT /evidence="ECO:0007829|PDB:6C12" FT STRAND 472..475 FT /evidence="ECO:0007829|PDB:1NEK" FT HELIX 477..494 FT /evidence="ECO:0007829|PDB:6C12" FT STRAND 504..506 FT /evidence="ECO:0007829|PDB:2WU2" FT HELIX 508..532 FT /evidence="ECO:0007829|PDB:6C12" FT STRAND 535..537 FT /evidence="ECO:0007829|PDB:7JZ2" FT STRAND 542..545 FT /evidence="ECO:0007829|PDB:6C12" FT HELIX 550..553 FT /evidence="ECO:0007829|PDB:6C12" FT STRAND 554..560 FT /evidence="ECO:0007829|PDB:6C12" FT TURN 561..564 FT /evidence="ECO:0007829|PDB:6C12" FT STRAND 565..569 FT /evidence="ECO:0007829|PDB:6C12" FT STRAND 576..578 FT /evidence="ECO:0007829|PDB:6C12" SQ SEQUENCE 588 AA; 64422 MW; 837F9A63991B6CE8 CRC64; MKLPVREFDA VVIGAGGAGM RAALQISQSG QTCALLSKVF PTRSHTVSAQ GGITVALGNT HEDNWEWHMY DTVKGSDYIG DQDAIEYMCK TGPEAILELE HMGLPFSRLD DGRIYQRPFG GQSKNFGGEQ AARTAAAADR TGHALLHTLY QQNLKNHTTI FSEWYALDLV KNQDGAVVGC TALCIETGEV VYFKARATVL ATGGAGRIYQ STTNAHINTG DGVGMAIRAG VPVQDMEMWQ FHPTGIAGAG VLVTEGCRGE GGYLLNKHGE RFMERYAPNA KDLAGRDVVA RSIMIEIREG RGCDGPWGPH AKLKLDHLGK EVLESRLPGI LELSRTFAHV DPVKEPIPVI PTCHYMMGGI PTKVTGQALT VNEKGEDVVV PGLFAVGEIA CVSVHGANRL GGNSLLDLVV FGRAAGLHLQ ESIAEQGALR DASESDVEAS LDRLNRWNNN RNGEDPVAIR KALQECMQHN FSVFREGDAM AKGLEQLKVI RERLKNARLD DTSSEFNTQR VECLELDNLM ETAYATAVSA NFRTESRGAH SRFDFPDRDD ENWLCHSLYL PESESMTRRS VNMEPKLRPA FPPKIRTY //