ID FUMC_ECOLI Reviewed; 467 AA. AC P05042; P76891; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 13-AUG-1987, sequence version 1. DT 27-MAR-2024, entry version 201. DE RecName: Full=Fumarate hydratase class II {ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000303|PubMed:3282546}; DE Short=Fumarase C {ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000303|PubMed:3541901}; DE EC=4.2.1.2 {ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000269|PubMed:1917897, ECO:0000269|PubMed:3282546}; DE AltName: Full=Aerobic fumarase {ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000303|PubMed:7592392}; DE AltName: Full=Iron-independent fumarase {ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000303|PubMed:3282546}; GN Name=fumC {ECO:0000255|HAMAP-Rule:MF_00743, GN ECO:0000303|PubMed:3541901}; OrderedLocusNames=b1611, JW1603; 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=3541901; DOI=10.1042/bj2370547; RA Woods S.A., Miles J.S., Roberts R.E., Guest J.R.; RT "Structural and functional relationships between fumarase and aspartase. RT Nucleotide sequences of the fumarase (fumC) and aspartase (aspA) genes of RT Escherichia coli K12."; RL Biochem. J. 237:547-557(1986). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=9097039; DOI=10.1093/dnares/3.6.363; RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., RA Wada C., Yamamoto Y., Horiuchi T.; RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to RT the 28.0-40.1 min region on the linkage map."; RL DNA Res. 3:363-377(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 1-89. RX PubMed=6328431; DOI=10.1093/nar/12.8.3631; RA Miles J.S., Guest J.R.; RT "Complete nucleotide sequence of the fumarase gene fumA, of Escherichia RT coli."; RL Nucleic Acids Res. 12:3631-3642(1984). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-89. RX PubMed=3005475; DOI=10.1099/00221287-131-11-2971; RA Guest J.R., Miles J.S., Roberts R.E., Woods S.A.; RT "The fumarase genes of Escherichia coli: location of the fumB gene and RT discovery of a new gene (fumC)."; RL J. Gen. Microbiol. 131:2971-2984(1985). RN [7] RP PROTEIN SEQUENCE OF 1-20, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL RP PROPERTIES, ACTIVITY REGULATION, AND SUBUNIT. RX PubMed=1917897; DOI=10.1093/oxfordjournals.jbchem.a123448; RA Ueda Y., Yumoto N., Tokushige M., Fukui K., Ohya-Nishiguchi H.; RT "Purification and characterization of two types of fumarase from RT Escherichia coli."; RL J. Biochem. 109:728-733(1991). RN [8] RP PROTEIN SEQUENCE OF 1-15, FUNCTION, AND SUBUNIT. RX PubMed=8496960; DOI=10.1006/jmbi.1993.1264; RA Weaver T.M., Levitt D.G., Banaszak L.J.; RT "Purification and crystallization of fumarase C from Escherichia coli."; RL J. Mol. Biol. 231:141-144(1993). RN [9] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, AND RP SUBUNIT. RX PubMed=3282546; DOI=10.1016/0167-4838(88)90050-7; RA Woods S.A., Shwartzbach S.D., Guest J.R.; RT "Two biochemically distinct classes of fumarase in Escherichia coli."; RL Biochim. Biophys. Acta 954:14-26(1988). RN [10] RP FUNCTION, AND INDUCTION. RX PubMed=7592392; DOI=10.1128/jb.177.21.6255-6262.1995; RA Park S.J., Gunsalus R.P.; RT "Oxygen, iron, carbon, and superoxide control of the fumarase fumA and fumC RT genes of Escherichia coli: role of the arcA, fnr, and soxR gene products."; RL J. Bacteriol. 177:6255-6262(1995). RN [11] 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 [12] RP MUTAGENESIS OF ARG-126; LYS-127 AND HIS-129. RX PubMed=14990798; DOI=10.1073/pnas.0307524101; RA Rose I.A., Weaver T.M.; RT "The role of the allosteric B site in the fumarase reaction."; RL Proc. Natl. Acad. Sci. U.S.A. 101:3393-3397(2004). RN [13] RP DISRUPTION PHENOTYPE. RX PubMed=17222132; DOI=10.1111/j.1462-2920.2006.01143.x; RA Domka J., Lee J., Bansal T., Wood T.K.; RT "Temporal gene-expression in Escherichia coli K-12 biofilms."; RL Environ. Microbiol. 9:332-346(2007). RN [14] RP REACTION MECHANISM. RX PubMed=22551392; DOI=10.1021/bi300430j; RA Puthan Veetil V., Fibriansah G., Raj H., Thunnissen A.M., Poelarends G.J.; RT "Aspartase/fumarase superfamily: a common catalytic strategy involving RT general base-catalyzed formation of a highly stabilized aci-carboxylate RT intermediate."; RL Biochemistry 51:4237-4243(2012). RN [15] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND RP SUBSTRATE ANALOGS, AND SUBUNIT. RX PubMed=8909293; DOI=10.1021/bi9614702; RA Weaver T., Banaszak L.; RT "Crystallographic studies of the catalytic and a second site in fumarase C RT from Escherichia coli."; RL Biochemistry 35:13955-13965(1996). RN [16] RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF MUTANTS ASN-129 AND ASN-188 IN RP COMPLEX WITH SUBSTRATE AND SUBSTRATE ANALOGS, MUTAGENESIS OF HIS-129 AND RP HIS-188, ACTIVE SITE, AND SUBUNIT. RX PubMed=9098893; DOI=10.1002/pro.5560060410; RA Weaver T., Lees M., Banaszak L.; RT "Mutations of fumarase that distinguish between the active site and a RT nearby dicarboxylic acid binding site."; RL Protein Sci. 6:834-842(1997). RN [17] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF MUTANT GLN-315 IN COMPLEX WITH RP SUBSTRATE AND SUBSTRATE ANALOGS, MUTAGENESIS OF GLU-315, BIOPHYSICOCHEMICAL RP PROPERTIES, AND SUBUNIT. RX PubMed=12021453; DOI=10.1110/ps.0201502; RA Estevez M., Skarda J., Spencer J., Banaszak L., Weaver T.M.; RT "X-ray crystallographic and kinetic correlation of a clinically observed RT human fumarase mutation."; RL Protein Sci. 11:1552-1557(2002). RN [18] RP X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS). RX PubMed=16204892; DOI=10.1107/s0907444905024194; RA Weaver T.; RT "Structure of free fumarase C from Escherichia coli."; RL Acta Crystallogr. D 61:1395-1401(2005). CC -!- FUNCTION: Involved in the TCA cycle. FumC seems to be a backup enzyme CC for FumA under conditions of iron limitation and oxidative stress CC (PubMed:7592392). Catalyzes the stereospecific interconversion of CC fumarate to L-malate (PubMed:1917897, PubMed:3282546). CC {ECO:0000269|PubMed:1917897, ECO:0000269|PubMed:3282546, CC ECO:0000269|PubMed:7592392, ECO:0000305|PubMed:8496960}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(S)-malate = fumarate + H2O; Xref=Rhea:RHEA:12460, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15589, ChEBI:CHEBI:29806; EC=4.2.1.2; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00743, CC ECO:0000269|PubMed:1917897, ECO:0000269|PubMed:3282546}; CC -!- ACTIVITY REGULATION: Inhibited by ATP, citrate and S-2,3- CC dicarboxyaziridine. {ECO:0000269|PubMed:1917897}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=50 uM for L-malate (at pH 7.3 and 30 degrees Celsius) CC {ECO:0000269|PubMed:1917897}; CC KM=207 uM for fumarate (at pH 7.9) {ECO:0000269|PubMed:12021453}; CC KM=390 uM for fumarate {ECO:0000269|PubMed:3282546}; CC KM=857 uM for S-malate (at pH 7.9) {ECO:0000269|PubMed:12021453}; CC KM=2.94 mM for S-malate {ECO:0000269|PubMed:3282546}; CC Vmax=1 umol/min/mg enzyme for fumarate {ECO:0000269|PubMed:3282546}; CC Vmax=1 umol/min/mg enzyme for S-malate {ECO:0000269|PubMed:3282546}; CC Vmax=344.8 umol/min/mg enzyme for fumarate (at pH 7.9) CC {ECO:0000269|PubMed:12021453}; CC Vmax=176.8 umol/min/mg enzyme for S-malate (at pH 7.9) CC {ECO:0000269|PubMed:12021453}; CC Note=kcat is 1149 sec(-1) for fumarate (at pH 7.9). kcat is 595.2 CC sec(-1) for S-malate (at pH 7.9). {ECO:0000269|PubMed:12021453}; CC pH dependence: CC Optimum pH is 8. {ECO:0000269|PubMed:1917897}; CC Temperature dependence: CC Thermostable. {ECO:0000269|PubMed:3282546}; CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate CC from fumarate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00743, CC ECO:0000305}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00743, CC ECO:0000269|PubMed:12021453, ECO:0000269|PubMed:1917897, CC ECO:0000269|PubMed:3282546, ECO:0000269|PubMed:8496960, CC ECO:0000269|PubMed:8909293, ECO:0000269|PubMed:9098893}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00743, CC ECO:0000305}. CC -!- INDUCTION: Under conditions of iron limitation and oxidative stress. CC {ECO:0000269|PubMed:3282546, ECO:0000269|PubMed:7592392}. CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show an increase of CC biofilm formation. {ECO:0000269|PubMed:17222132}. CC -!- MISCELLANEOUS: There are 2 substrate-binding sites: the catalytic A CC site, and the non-catalytic B site that may play a role in the transfer CC of substrate or product between the active site and the solvent. CC Alternatively, the B site may bind allosteric effectors. CC {ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000305|PubMed:14990798, CC ECO:0000305|PubMed:9098893}. CC -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family. Fumarase CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00743, 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; X04065; CAA27698.1; -; Genomic_DNA. DR EMBL; U00096; AAC74683.1; -; Genomic_DNA. DR EMBL; AP009048; BAA15349.1; -; Genomic_DNA. DR EMBL; X00522; CAA25205.1; -; Genomic_DNA. DR PIR; S07138; UFEC. DR RefSeq; NP_416128.1; NC_000913.3. DR RefSeq; WP_001099085.1; NZ_SSZK01000001.1. DR PDB; 1FUO; X-ray; 1.98 A; A/B=1-467. DR PDB; 1FUP; X-ray; 2.30 A; A/B=1-467. DR PDB; 1FUQ; X-ray; 2.00 A; A/B=1-467. DR PDB; 1FUR; X-ray; 1.95 A; A/B=1-467. DR PDB; 1KQ7; X-ray; 2.60 A; A/B=1-467. DR PDB; 1YFE; X-ray; 2.19 A; A=1-467. DR PDB; 2FUS; X-ray; 2.20 A; A/B=1-467. DR PDB; 6NZ9; X-ray; 1.53 A; A/B=1-467. DR PDB; 6NZA; X-ray; 1.41 A; A/B=1-467. DR PDB; 6NZB; X-ray; 1.37 A; A/B=1-467. DR PDB; 6NZC; X-ray; 1.40 A; A/B=1-467. DR PDB; 6OS7; X-ray; 1.36 A; A/B=1-467. DR PDB; 6P3C; X-ray; 1.46 A; A/B=1-467. DR PDB; 8SBS; X-ray; 1.91 A; A=1-467. DR PDBsum; 1FUO; -. DR PDBsum; 1FUP; -. DR PDBsum; 1FUQ; -. DR PDBsum; 1FUR; -. DR PDBsum; 1KQ7; -. DR PDBsum; 1YFE; -. DR PDBsum; 2FUS; -. DR PDBsum; 6NZ9; -. DR PDBsum; 6NZA; -. DR PDBsum; 6NZB; -. DR PDBsum; 6NZC; -. DR PDBsum; 6OS7; -. DR PDBsum; 6P3C; -. DR PDBsum; 8SBS; -. DR AlphaFoldDB; P05042; -. DR SMR; P05042; -. DR BioGRID; 4263123; 11. DR DIP; DIP-9719N; -. DR IntAct; P05042; 14. DR STRING; 511145.b1611; -. DR DrugBank; DB03452; 3-Trimethylsilylsuccinic Acid. DR DrugBank; DB04272; Citric acid. DR DrugBank; DB03499; D-Malic acid. DR DrugBank; DB02749; Pyromellitic Acid. DR jPOST; P05042; -. DR PaxDb; 511145-b1611; -. DR EnsemblBacteria; AAC74683; AAC74683; b1611. DR GeneID; 946147; -. DR KEGG; ecj:JW1603; -. DR KEGG; eco:b1611; -. DR PATRIC; fig|1411691.4.peg.651; -. DR EchoBASE; EB0353; -. DR eggNOG; COG0114; Bacteria. DR HOGENOM; CLU_021594_4_1_6; -. DR InParanoid; P05042; -. DR OMA; AKWRAQT; -. DR OrthoDB; 9802809at2; -. DR PhylomeDB; P05042; -. DR BioCyc; EcoCyc:FUMC-MONOMER; -. DR BioCyc; MetaCyc:FUMC-MONOMER; -. DR BRENDA; 4.2.1.2; 2026. DR SABIO-RK; P05042; -. DR UniPathway; UPA00223; UER01007. DR EvolutionaryTrace; P05042; -. DR PRO; PR:P05042; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0045239; C:tricarboxylic acid cycle enzyme complex; IEA:InterPro. DR GO; GO:0004333; F:fumarate hydratase activity; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc. DR GO; GO:0006106; P:fumarate metabolic process; IBA:GO_Central. DR GO; GO:0006108; P:malate metabolic process; IBA:GO_Central. DR GO; GO:0006979; P:response to oxidative stress; IEP:EcoCyc. DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central. DR CDD; cd01362; Fumarase_classII; 1. DR Gene3D; 1.10.40.30; Fumarase/aspartase (C-terminal domain); 1. DR Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 1. DR Gene3D; 1.10.275.10; Fumarase/aspartase (N-terminal domain); 1. DR HAMAP; MF_00743; FumaraseC; 1. DR InterPro; IPR005677; Fum_hydII. DR InterPro; IPR024083; Fumarase/histidase_N. DR InterPro; IPR018951; Fumarase_C_C. DR InterPro; IPR020557; Fumarate_lyase_CS. DR InterPro; IPR000362; Fumarate_lyase_fam. DR InterPro; IPR022761; Fumarate_lyase_N. DR InterPro; IPR008948; L-Aspartase-like. DR NCBIfam; TIGR00979; fumC_II; 1. DR PANTHER; PTHR11444; ASPARTATEAMMONIA/ARGININOSUCCINATE/ADENYLOSUCCINATE LYASE; 1. DR PANTHER; PTHR11444:SF1; FUMARATE HYDRATASE, MITOCHONDRIAL; 1. DR Pfam; PF10415; FumaraseC_C; 1. DR Pfam; PF00206; Lyase_1; 1. DR PRINTS; PR00149; FUMRATELYASE. DR SUPFAM; SSF48557; L-aspartase-like; 1. DR PROSITE; PS00163; FUMARATE_LYASES; 1. PE 1: Evidence at protein level; KW 3D-structure; Allosteric enzyme; Cytoplasm; Direct protein sequencing; KW Lyase; Reference proteome; Tricarboxylic acid cycle. FT CHAIN 1..467 FT /note="Fumarate hydratase class II" FT /id="PRO_0000161275" FT ACT_SITE 188 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743, FT ECO:0000269|PubMed:9098893" FT ACT_SITE 318 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743" FT BINDING 98..100 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743, FT ECO:0000305|PubMed:12021453, ECO:0000305|PubMed:8909293, FT ECO:0000305|PubMed:9098893, ECO:0007744|PDB:1FUO, FT ECO:0007744|PDB:1FUP, ECO:0007744|PDB:1FUQ, FT ECO:0007744|PDB:1KQ7, ECO:0007744|PDB:2FUS" FT BINDING 126 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:8909293, FT ECO:0000269|PubMed:9098893, ECO:0007744|PDB:1FUO, FT ECO:0007744|PDB:1FUP, ECO:0007744|PDB:1FUQ, FT ECO:0007744|PDB:1FUR" FT BINDING 129..132 FT /ligand="substrate" FT /note="in site B" FT /evidence="ECO:0000269|PubMed:12021453, FT ECO:0000269|PubMed:8909293, ECO:0000269|PubMed:9098893, FT ECO:0007744|PDB:1FUO, ECO:0007744|PDB:1FUP, FT ECO:0007744|PDB:1FUQ, ECO:0007744|PDB:1FUR, FT ECO:0007744|PDB:1KQ7" FT BINDING 139..141 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743, FT ECO:0000269|PubMed:12021453, ECO:0000269|PubMed:8909293, FT ECO:0000269|PubMed:9098893, ECO:0007744|PDB:1FUO, FT ECO:0007744|PDB:1FUP, ECO:0007744|PDB:1FUQ, FT ECO:0007744|PDB:1KQ7, ECO:0007744|PDB:2FUS" FT BINDING 187 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743" FT BINDING 319 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743" FT BINDING 324..326 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743" FT SITE 331 FT /note="Important for catalytic activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00743, FT ECO:0000305|PubMed:8909293" FT MUTAGEN 126 FT /note="R->A: 10-fold decrease of fumarase activity." FT /evidence="ECO:0000269|PubMed:14990798" FT MUTAGEN 127 FT /note="K->D: No effect." FT /evidence="ECO:0000269|PubMed:14990798" FT MUTAGEN 129 FT /note="H->N: No effect on fumarase activity and essentially FT same conformation compared to the wild-type, but appears to FT dramatically reduce binding of ligands at the B-site." FT /evidence="ECO:0000269|PubMed:14990798, FT ECO:0000269|PubMed:9098893" FT MUTAGEN 188 FT /note="H->N: 200-fold decrease of fumarase activity." FT /evidence="ECO:0000269|PubMed:9098893" FT MUTAGEN 315 FT /note="E->Q: There is essentially no effect on the affinity FT values for both S-malate and fumarate. In contrast, the FT catalytic efficiency values have been lowered by 10-fold in FT both directions." FT /evidence="ECO:0000269|PubMed:12021453" FT STRAND 4..9 FT /evidence="ECO:0007829|PDB:6OS7" FT STRAND 12..17 FT /evidence="ECO:0007829|PDB:6OS7" FT HELIX 24..32 FT /evidence="ECO:0007829|PDB:6OS7" FT HELIX 42..61 FT /evidence="ECO:0007829|PDB:6OS7" FT HELIX 67..81 FT /evidence="ECO:0007829|PDB:6OS7" FT TURN 82..85 FT /evidence="ECO:0007829|PDB:1FUR" FT HELIX 86..88 FT /evidence="ECO:0007829|PDB:6OS7" FT STRAND 92..95 FT /evidence="ECO:0007829|PDB:6OS7" FT HELIX 100..117 FT /evidence="ECO:0007829|PDB:6OS7" FT HELIX 130..134 FT /evidence="ECO:0007829|PDB:6OS7" FT TURN 135..137 FT /evidence="ECO:0007829|PDB:6OS7" FT HELIX 140..158 FT /evidence="ECO:0007829|PDB:6OS7" FT HELIX 160..177 FT /evidence="ECO:0007829|PDB:6OS7" FT TURN 178..180 FT /evidence="ECO:0007829|PDB:6OS7" FT STRAND 182..187 FT /evidence="ECO:0007829|PDB:6OS7" FT STRAND 190..196 FT /evidence="ECO:0007829|PDB:6OS7" FT HELIX 197..222 FT /evidence="ECO:0007829|PDB:6OS7" FT TURN 230..232 FT /evidence="ECO:0007829|PDB:6OS7" FT HELIX 242..254 FT /evidence="ECO:0007829|PDB:6OS7" FT HELIX 264..269 FT /evidence="ECO:0007829|PDB:6OS7" FT HELIX 272..298 FT /evidence="ECO:0007829|PDB:6OS7" FT STRAND 302..305 FT /evidence="ECO:0007829|PDB:6OS7" FT STRAND 308..310 FT /evidence="ECO:0007829|PDB:6OS7" FT STRAND 319..321 FT /evidence="ECO:0007829|PDB:6NZB" FT HELIX 328..351 FT /evidence="ECO:0007829|PDB:6OS7" FT HELIX 362..386 FT /evidence="ECO:0007829|PDB:6OS7" FT HELIX 388..390 FT /evidence="ECO:0007829|PDB:6OS7" FT HELIX 395..404 FT /evidence="ECO:0007829|PDB:6OS7" FT HELIX 407..412 FT /evidence="ECO:0007829|PDB:6OS7" FT HELIX 413..416 FT /evidence="ECO:0007829|PDB:6OS7" FT HELIX 418..431 FT /evidence="ECO:0007829|PDB:6OS7" FT HELIX 435..442 FT /evidence="ECO:0007829|PDB:6OS7" FT HELIX 447..453 FT /evidence="ECO:0007829|PDB:6OS7" FT HELIX 456..458 FT /evidence="ECO:0007829|PDB:6OS7" SQ SEQUENCE 467 AA; 50489 MW; 3D67E3C0F0FDF40B CRC64; MNTVRSEKDS MGAIDVPADK LWGAQTQRSL EHFRISTEKM PTSLIHALAL TKRAAAKVNE DLGLLSEEKA SAIRQAADEV LAGQHDDEFP LAIWQTGSGT QSNMNMNEVL ANRASELLGG VRGMERKVHP NDDVNKSQSS NDVFPTAMHV AALLALRKQL IPQLKTLTQT LNEKSRAFAD IVKIGRTHLQ DATPLTLGQE ISGWVAMLEH NLKHIEYSLP HVAELALGGT AVGTGLNTHP EYARRVADEL AVITCAPFVT APNKFEALAT CDALVQAHGA LKGLAASLMK IANDVRWLAS GPRCGIGEIS IPENEPGSSI MPGKVNPTQC EALTMLCCQV MGNDVAINMG GASGNFELNV FRPMVIHNFL QSVRLLADGM ESFNKHCAVG IEPNRERINQ LLNESLMLVT ALNTHIGYDK AAEIAKKAHK EGLTLKAAAL ALGYLSEAEF DSWVRPEQMV GSMKAGR //