FUMC_ECOLI
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 03-AUG-2022, entry version 194.
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, ECO:0000303|PubMed:3541901};
GN OrderedLocusNames=b1611, JW1603;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; 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}.
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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 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 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; P05042; -.
DR PRIDE; P05042; -.
DR EnsemblBacteria; AAC74683; AAC74683; b1611.
DR EnsemblBacteria; BAA15349; BAA15349; BAA15349.
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; HDSMGEV; -.
DR PhylomeDB; P05042; -.
DR BioCyc; EcoCyc:FUMC-MON; -.
DR BioCyc; MetaCyc:FUMC-MON; -.
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; 1.10.275.10; -; 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 PANTHER; PTHR11444; PTHR11444; 1.
DR Pfam; PF10415; FumaraseC_C; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; SSF48557; 1.
DR TIGRFAMs; TIGR00979; fumC_II; 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
