ID FRDA_ECOLI Reviewed; 602 AA. AC P00363; Q2M6E8; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 02-SEP-2026, entry version 229. DE RecName: Full=Fumarate reductase flavoprotein subunit; DE EC=1.3.5.1 {ECO:0000269|PubMed:11850430}; DE AltName: Full=Quinol-fumarate reductase flavoprotein subunit {ECO:0000303|PubMed:11850430}; DE Short=QFR flavoprotein subunit {ECO:0000303|PubMed:11850430}; GN Name=frdA; OrderedLocusNames=b4154, JW4115; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=K12; RX PubMed=7037404; DOI=10.1111/j.1432-1033.1982.tb06462.x; RA Cole S.T.; RT "Nucleotide sequence coding for the flavoprotein subunit of the fumarate RT reductase of Escherichia coli."; RL Eur. J. Biochem. 122:479-484(1982). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=7610040; DOI=10.1093/nar/23.12.2105; RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.; RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region RT from 92.8 through 100 minutes."; RL Nucleic Acids Res. 23:2105-2119(1995). 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 PROTEIN SEQUENCE OF 170-185, COFACTOR, SUBUNIT, AND MUTAGENESIS OF LYS-131; RP MET-177; GLU-178; GLY-207 AND SER-240. 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 [6] RP COFACTOR, AND MUTAGENESIS OF HIS-45; LYS-131; MET-177; GLU-178; GLY-207; RP HIS-233; SER-240; CYS-248 AND ARG-249. RX PubMed=2668268; DOI=10.1016/s0021-9258(18)80039-4; RA Blaut M., Whittaker K., Valdovinos A., Ackrell B.A., Gunsalus R.P., RA Cecchini G.; RT "Fumarate reductase mutants of Escherichia coli that lack covalently bound RT flavin."; RL J. Biol. Chem. 264:13599-13604(1989). RN [7] RP ACTIVE SITE, AND MUTAGENESIS OF HIS-233; CYS-248 AND ARG-249. RX PubMed=1856194; DOI=10.1016/s0021-9258(18)92737-7; RA Schroeder I., Gunsalus R.P., Ackrell B.A.C., Cochran B., Cecchini G.; RT "Identification of active site residues of Escherichia coli fumarate RT reductase by site-directed mutagenesis."; RL J. Biol. Chem. 266:13572-13579(1991). 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. RX PubMed=20484676; DOI=10.1073/pnas.1000956107; RA Moebius K., Arias-Cartin R., Breckau D., Haennig A.L., Riedmann K., RA Biedendieck R., Schroeder S., Becher D., Magalon A., Moser J., Jahn M., RA Jahn D.; RT "Heme biosynthesis is coupled to electron transport chains for energy RT generation."; RL Proc. Natl. Acad. Sci. U.S.A. 107:10436-10441(2010). RN [10] 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 [11] RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) IN COMPLEX WITH FAD AND SUBSTRATE RP ANALOG, COFACTOR, ACTIVITY REGULATION, SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=10373108; DOI=10.1126/science.284.5422.1961; RA Iverson T.M., Luna-Chavez C., Cecchini G., Rees D.C.; RT "Structure of the Escherichia coli fumarate reductase respiratory RT complex."; RL Science 284:1961-1966(1999). RN [12] {ECO:0007744|PDB:1KF6, ECO:0007744|PDB:1KFY, ECO:0007744|PDB:1L0V} RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH FAD; SUBSTRATE RP ANALOGS AND INHIBITORS, CATALYTIC ACTIVITY, AND SUBUNIT. RX PubMed=11850430; DOI=10.1074/jbc.m200815200; RA Iverson T.M., Luna-Chavez C., Croal L.R., Cecchini G., Rees D.C.; RT "Crystallographic studies of the Escherichia coli quinol-fumarate reductase RT with inhibitors bound to the quinol-binding site."; RL J. Biol. Chem. 277:16124-16130(2002). CC -!- FUNCTION: Two distinct, membrane-bound, FAD-containing enzymes are CC responsible for the catalysis of fumarate and succinate CC interconversion; fumarate reductase is used during anaerobic growth, CC and succinate dehydrogenase is used during aerobic growth. The QFR CC enzyme complex binds 2 quinones in or near the membrane; 1 near the CC [3Fe-4S] cluster (QP is proximal to the [3Fe-4S] cluster, on the CC cytoplasmic side of the membrane) while QD (the distal cluster) is on CC the other side of the membrane. It is not clear if both of the quinol- CC binding sites are functionally relevant (PubMed:10373108, CC PubMed:11850430). {ECO:0000269|PubMed:10373108, CC ECO:0000269|PubMed:11850430, ECO:0000269|PubMed:24374335}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a quinone + succinate = fumarate + a quinol; 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:0000269|PubMed:11850430}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a menaquinone + succinate = a menaquinol + fumarate; CC Xref=Rhea:RHEA:27834, Rhea:RHEA-COMP:9537, Rhea:RHEA-COMP:9539, CC ChEBI:CHEBI:16374, ChEBI:CHEBI:18151, ChEBI:CHEBI:29806, CC ChEBI:CHEBI:30031; EC=1.3.5.1; CC Evidence={ECO:0000305|PubMed:10373108}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Note=Binds 1 FAD covalently per subunit (PubMed:10373108, CC PubMed:24374335, PubMed:26644464). Flavinylated by SdhE, about 5% CC flavinylation occurs in the absence of SdhE (PubMed:24374335, CC PubMed:26644464). {ECO:0000269|PubMed:10373108, CC ECO:0000269|PubMed:24374335, ECO:0000269|PubMed:26644464}; CC -!- ACTIVITY REGULATION: Inhibited by oxaloacetate, a substrate analog. CC {ECO:0000269|PubMed:10373108}. CC -!- SUBUNIT: Part of an enzyme complex containing four subunits: a CC flavoprotein (FrdA), an iron-sulfur protein (FrdB), and two hydrophobic CC anchor proteins (FrdC and FrdD) (PubMed:10373108, PubMed:11850430). Can CC be cross-linked to SdhE (PubMed:26644464). Purified from membrane CC fractions associated with protoporphyrinogen IX dehydrogenase (hemG) CC (PubMed:20484676). {ECO:0000269|PubMed:10373108, CC ECO:0000269|PubMed:11850430, ECO:0000269|PubMed:20484676, CC ECO:0000269|PubMed:26644464, ECO:0000305|PubMed:26644464}. CC -!- INTERACTION: CC P00363; P0AC47: frdB; NbExp=4; IntAct=EBI-550480, EBI-906724; CC P00363; P0ACB4: hemG; NbExp=2; IntAct=EBI-550480, EBI-1115706; CC P00363; P76111: ydcZ; NbExp=2; IntAct=EBI-550480, EBI-550492; CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305|PubMed:10373108, CC ECO:0000305|PubMed:20484676}; Peripheral membrane protein CC {ECO:0000305|PubMed:10373108}; Cytoplasmic side CC {ECO:0000305|PubMed:10373108}. CC -!- DISRUPTION PHENOTYPE: No anaerobic growth on glycerol fumarate medium. CC {ECO:0000269|PubMed:24374335}. 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; J01611; AAA23437.1; -; Genomic_DNA. DR EMBL; U14003; AAA97053.1; -; Genomic_DNA. DR EMBL; U00096; AAC77114.1; -; Genomic_DNA. DR EMBL; AP009048; BAE78158.1; -; Genomic_DNA. DR PIR; A00376; RDECFF. DR RefSeq; NP_418578.1; NC_000913.3. DR RefSeq; WP_001192973.1; NZ_CP009789.1. DR PDB; 1KF6; X-ray; 2.70 A; A/M=1-602. DR PDB; 1KFY; X-ray; 3.60 A; A/M=1-602. DR PDB; 1L0V; X-ray; 3.30 A; A/M=1-602. DR PDB; 2B76; X-ray; 3.30 A; A/M=1-602. DR PDB; 3CIR; X-ray; 3.65 A; A/M=1-602. DR PDB; 3P4P; X-ray; 2.80 A; A/M=1-577. DR PDB; 3P4Q; X-ray; 3.35 A; A/M=1-577. DR PDB; 3P4R; X-ray; 3.05 A; A/M=1-577. DR PDB; 3P4S; X-ray; 3.10 A; A/M=1-577. DR PDB; 4KX6; X-ray; 2.95 A; A/M=1-577. DR PDB; 5VPN; X-ray; 4.22 A; A/E=1-585. DR PDB; 6AWF; X-ray; 3.35 A; A/E=1-602. DR PDB; 6B58; X-ray; 2.61 A; A/C=1-577. DR AlphaFoldDB; P00363; -. DR MDposit; P00363; -. DR MDRepo; P00363; -. DR SMR; P00363; -. DR BioGRID; 4260883; 178. DR BioGRID; 852959; 1. DR ComplexPortal; CPX-1967; Plasma membrane fumarate reductase complex. DR DIP; DIP-9681N; -. DR FunCoup; P00363; 403. DR IntAct; P00363; 15. DR STRING; 511145.b4154; -. DR DrugBank; DB07490; 2-[1-(4-CHLORO-PHENYL)-ETHYL]-4,6-DINITRO-PHENOL. DR DrugBank; DB07918; 2-heptyl-4-hydroxyquinoline N-oxide. DR DrugBank; DB00730; Thiabendazole. DR jPOST; P00363; -. DR PaxDb; 511145-b4154; -. DR EnsemblBacteria; AAC77114; AAC77114; b4154. DR GeneID; 93777668; -. DR GeneID; 948667; -. DR KEGG; ecj:JW4115; -. DR KEGG; eco:b4154; -. DR KEGG; ecoc:C3026_22455; -. DR PATRIC; fig|1411691.4.peg.2544; -. DR EchoBASE; EB0326; -. DR eggNOG; COG1053; Bacteria. DR HOGENOM; CLU_014312_6_2_6; -. DR InParanoid; P00363; -. DR OMA; PTAHHFM; -. DR OrthoDB; 9806724at2; -. DR PhylomeDB; P00363; -. DR BioCyc; EcoCyc:FUM-FLAVO; -. DR BioCyc; MetaCyc:FUM-FLAVO; -. DR BRENDA; 1.3.5.1; 2026. DR SABIO-RK; P00363; -. DR EvolutionaryTrace; P00363; -. DR PRO; PR:P00363; -. DR Proteomes; UP000000625; Chromosome. DR AbasyAtlas; P00363; -. DR GO; GO:0005829; C:cytosol; IDA:EcoCyc. DR GO; GO:0045283; C:fumarate reductase complex; IDA:EcoCyc. DR GO; GO:0016020; C:membrane; IDA:ComplexPortal. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0009055; F:electron transfer activity; IDA:EcoCyc. DR GO; GO:0071949; F:FAD binding; IDA:EcoCyc. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central. DR GO; GO:0008177; F:succinate dehydrogenase (quinone) activity; EXP:UniProtKB. DR GO; GO:0000104; F:succinate dehydrogenase activity; IBA:GO_Central. DR GO; GO:0019645; P:anaerobic electron transport chain; NAS:ComplexPortal. DR GO; GO:0009061; P:anaerobic respiration; IMP:EcoCyc. DR GO; GO:0044780; P:bacterial-type flagellum assembly; IMP:EcoCyc. DR GO; GO:0006974; P:DNA damage response; IEP:EcoliWiki. DR FunFam; 3.50.50.60:FF:000017; Fumarate reductase flavoprotein subunit; 1. DR FunFam; 3.90.700.10:FF:000003; Fumarate reductase flavoprotein subunit; 1. DR FunFam; 4.10.80.40:FF:000003; Fumarate reductase flavoprotein subunit; 1. DR FunFam; 1.20.58.100:FF:000001; Succinate dehydrogenase flavoprotein subunit (SdhA); 1. 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-dep_OxRdtase_2_FAD-bd. 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; IPR005884; Fum_red_fp. DR InterPro; IPR030664; SdhA/FrdA/AprA. DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf. DR InterPro; IPR014006; Succ_Dhase_FrdA_Gneg. DR NCBIfam; TIGR01176; fum_red_Fp; 1. DR NCBIfam; NF006686; PRK09231.1; 1. DR NCBIfam; TIGR01812; sdhA_frdA_Gneg; 1. DR PANTHER; PTHR11632:SF82; FUMARATE REDUCTASE FLAVOPROTEIN SUBUNIT; 1. DR PANTHER; PTHR11632; SUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT; 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 PRINTS; PR00411; PNDRDTASEI. 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 PDBsum; 1KF6; -. DR PDBsum; 1KFY; -. DR PDBsum; 1L0V; -. DR PDBsum; 2B76; -. DR PDBsum; 3CIR; -. DR PDBsum; 3P4P; -. DR PDBsum; 3P4Q; -. DR PDBsum; 3P4R; -. DR PDBsum; 3P4S; -. DR PDBsum; 4KX6; -. DR PDBsum; 5VPN; -. DR PDBsum; 6AWF; -. DR PDBsum; 6B58; -. PE 1: Evidence at protein level; KW 3D-structure; Cell inner membrane; Cell membrane; KW Direct protein sequencing; Electron transport; FAD; Flavoprotein; Membrane; KW Nucleotide-binding; Oxidoreductase; Reference proteome; Transport. FT INIT_MET 1 FT /note="Removed" FT CHAIN 2..602 FT /note="Fumarate reductase flavoprotein subunit" FT /id="PRO_0000158660" FT REGION 581..602 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 587..602 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 233 FT /evidence="ECO:0000305|PubMed:1856194" FT ACT_SITE 249 FT /evidence="ECO:0000305|PubMed:1856194" FT BINDING 12..16 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007744|PDB:1KF6, ECO:0007744|PDB:1KFY, FT ECO:0007744|PDB:1L0V" FT BINDING 36..38 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007744|PDB:1KF6, ECO:0007744|PDB:1KFY, FT ECO:0007744|PDB:1L0V" FT BINDING 44..52 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007744|PDB:1KF6, ECO:0007744|PDB:1KFY, FT ECO:0007744|PDB:1L0V" FT BINDING 156..158 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007744|PDB:1KF6, ECO:0007744|PDB:1KFY, FT ECO:0007744|PDB:1L0V" FT BINDING 192..193 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007744|PDB:1KF6" FT BINDING 212 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007744|PDB:1KF6, ECO:0007744|PDB:1KFY, FT ECO:0007744|PDB:1L0V" FT BINDING 356..357 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007744|PDB:2B76, ECO:0007744|PDB:3CIR" FT BINDING 380 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007744|PDB:1KF6, ECO:0007744|PDB:1KFY, FT ECO:0007744|PDB:1L0V" FT BINDING 391..397 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007744|PDB:1KF6, ECO:0007744|PDB:1KFY, FT ECO:0007744|PDB:1L0V" FT MOD_RES 45 FT /note="Tele-8alpha-FAD histidine" FT /evidence="ECO:0000269|PubMed:10373108, FT ECO:0007744|PDB:1L0V" FT MUTAGEN 45 FT /note="H->R: Inactivates enzyme." FT /evidence="ECO:0000269|PubMed:2668268" FT MUTAGEN 45 FT /note="H->S,C,Y: Decreased ability (greater than 70%) to FT reduce fumarate." FT /evidence="ECO:0000269|PubMed:2668268" FT MUTAGEN 131 FT /note="K->M: Increased cross-linking to SdhE, FrdA is FT slightly less flavinylated." FT /evidence="ECO:0000269|PubMed:26644464" FT MUTAGEN 177 FT /note="M->A: No longer forms cross-link to SdhE, FrdA is FT still flavinylated." FT /evidence="ECO:0000269|PubMed:26644464" FT MUTAGEN 178 FT /note="E->A: Decreased cross-linking to SdhE, FrdA is still FT flavinylated." FT /evidence="ECO:0000269|PubMed:26644464" FT MUTAGEN 207 FT /note="G->M: Increased cross-linking to SdhE, FrdA is FT flavinylated." FT /evidence="ECO:0000269|PubMed:26644464" FT MUTAGEN 233 FT /note="H->S: Severely affects succinate oxidation, FT decreases fumarate oxidation by 75%." FT /evidence="ECO:0000269|PubMed:1856194" FT MUTAGEN 240 FT /note="S->M: Increased cross-linking to SdhE, FrdA is FT flavinylated." FT /evidence="ECO:0000269|PubMed:26644464" FT MUTAGEN 248 FT /note="C->S,A: Does not inactivate enzyme." FT /evidence="ECO:0000269|PubMed:1856194" FT MUTAGEN 249 FT /note="R->H,L: Inactivates enzyme." FT /evidence="ECO:0000269|PubMed:1856194" FT CONFLICT 386 FT /note="L -> P (in Ref. 1; AAA23437)" FT /evidence="ECO:0000305" FT STRAND 2..5 FT /evidence="ECO:0007829|PDB:6B58" FT STRAND 7..11 FT /evidence="ECO:0007829|PDB:6B58" FT HELIX 15..27 FT /evidence="ECO:0007829|PDB:6B58" FT STRAND 33..39 FT /evidence="ECO:0007829|PDB:6B58" FT HELIX 41..43 FT /evidence="ECO:0007829|PDB:6B58" FT HELIX 45..48 FT /evidence="ECO:0007829|PDB:6B58" FT STRAND 58..60 FT /evidence="ECO:0007829|PDB:3P4P" FT HELIX 63..73 FT /evidence="ECO:0007829|PDB:6B58" FT TURN 74..76 FT /evidence="ECO:0007829|PDB:6B58" FT HELIX 80..99 FT /evidence="ECO:0007829|PDB:6B58" FT STRAND 110..112 FT /evidence="ECO:0007829|PDB:1KF6" FT STRAND 128..130 FT /evidence="ECO:0007829|PDB:1L0V" FT HELIX 132..145 FT /evidence="ECO:0007829|PDB:6B58" FT STRAND 150..154 FT /evidence="ECO:0007829|PDB:6B58" FT STRAND 156..175 FT /evidence="ECO:0007829|PDB:6B58" FT TURN 176..178 FT /evidence="ECO:0007829|PDB:6B58" FT STRAND 181..185 FT /evidence="ECO:0007829|PDB:6B58" FT STRAND 187..191 FT /evidence="ECO:0007829|PDB:6B58" FT HELIX 197..199 FT /evidence="ECO:0007829|PDB:6B58" FT STRAND 200..205 FT /evidence="ECO:0007829|PDB:6B58" FT HELIX 212..219 FT /evidence="ECO:0007829|PDB:6B58" FT STRAND 224..226 FT /evidence="ECO:0007829|PDB:6B58" FT STRAND 230..236 FT /evidence="ECO:0007829|PDB:6B58" FT TURN 238..240 FT /evidence="ECO:0007829|PDB:6B58" FT HELIX 247..250 FT /evidence="ECO:0007829|PDB:6B58" FT STRAND 254..256 FT /evidence="ECO:0007829|PDB:6B58" FT HELIX 263..266 FT /evidence="ECO:0007829|PDB:6B58" FT TURN 267..269 FT /evidence="ECO:0007829|PDB:1KF6" FT HELIX 272..274 FT /evidence="ECO:0007829|PDB:6B58" FT HELIX 283..285 FT /evidence="ECO:0007829|PDB:6B58" FT HELIX 288..300 FT /evidence="ECO:0007829|PDB:6B58" FT STRAND 304..307 FT /evidence="ECO:0007829|PDB:6B58" FT STRAND 310..316 FT /evidence="ECO:0007829|PDB:6B58" FT TURN 318..320 FT /evidence="ECO:0007829|PDB:6B58" FT HELIX 322..327 FT /evidence="ECO:0007829|PDB:6B58" FT HELIX 331..339 FT /evidence="ECO:0007829|PDB:6B58" FT TURN 344..346 FT /evidence="ECO:0007829|PDB:6B58" FT STRAND 349..358 FT /evidence="ECO:0007829|PDB:6B58" FT STRAND 361..363 FT /evidence="ECO:0007829|PDB:6B58" FT STRAND 371..373 FT /evidence="ECO:0007829|PDB:6B58" FT STRAND 375..377 FT /evidence="ECO:0007829|PDB:6B58" FT HELIX 379..381 FT /evidence="ECO:0007829|PDB:6B58" FT STRAND 385..387 FT /evidence="ECO:0007829|PDB:6B58" FT HELIX 395..415 FT /evidence="ECO:0007829|PDB:6B58" FT HELIX 423..440 FT /evidence="ECO:0007829|PDB:6B58" FT HELIX 449..463 FT /evidence="ECO:0007829|PDB:6B58" FT STRAND 464..468 FT /evidence="ECO:0007829|PDB:6B58" FT HELIX 470..487 FT /evidence="ECO:0007829|PDB:6B58" FT STRAND 497..499 FT /evidence="ECO:0007829|PDB:3P4P" FT HELIX 501..525 FT /evidence="ECO:0007829|PDB:6B58" FT STRAND 533..535 FT /evidence="ECO:0007829|PDB:6B58" FT STRAND 540..542 FT /evidence="ECO:0007829|PDB:6B58" FT TURN 545..547 FT /evidence="ECO:0007829|PDB:6B58" FT STRAND 550..556 FT /evidence="ECO:0007829|PDB:6B58" FT STRAND 562..567 FT /evidence="ECO:0007829|PDB:6B58" FT HELIX 569..571 FT /evidence="ECO:0007829|PDB:4KX6" SQ SEQUENCE 602 AA; 65972 MW; 3306D7FF6E198AE9 CRC64; MQTFQADLAI VGAGGAGLRA AIAAAQANPN AKIALISKVY PMRSHTVAAE GGSAAVAQDH DSFEYHFHDT VAGGDWLCEQ DVVDYFVHHC PTEMTQLELW GCPWSRRPDG SVNVRRFGGM KIERTWFAAD KTGFHMLHTL FQTSLQFPQI QRFDEHFVLD ILVDDGHVRG LVAMNMMEGT LVQIRANAVV MATGGAGRVY RYNTNGGIVT GDGMGMALSH GVPLRDMEFV QYHPTGLPGS GILMTEGCRG EGGILVNKNG YRYLQDYGMG PETPLGEPKN KYMELGPRDK VSQAFWHEWR KGNTISTPRG DVVYLDLRHL GEKKLHERLP FICELAKAYV GVDPVKEPIP VRPTAHYTMG GIETDQNCET RIKGLFAVGE CSSVGLHGAN RLGSNSLAEL VVFGRLAGEQ ATERAATAGN GNEAAIEAQA AGVEQRLKDL VNQDGGENWA KIRDEMGLAM EEGCGIYRTP ELMQKTIDKL AELQERFKRV RITDTSSVFN TDLLYTIELG HGLNVAECMA HSAMARKESR GAHQRLDEGC TERDDVNFLK HTLAFRDADG TTRLEYSDVK ITTLPPAKRV YGGEADAADK AEAANKKEKA NG //