FRDA_ECOLI
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 03-AUG-2022, entry version 212.
DE RecName: Full=Fumarate reductase flavoprotein subunit;
DE EC=1.3.5.4;
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; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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 = a quinol + fumarate;
CC Xref=Rhea:RHEA:40523, ChEBI:CHEBI:24646, ChEBI:CHEBI:29806,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:132124; EC=1.3.5.4;
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=1.3.5.4;
CC Evidence={ECO:0000305|PubMed:10373108};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Note=Binds 1 FAD covalently per subunit (PubMed:24374335,
CC PubMed:26644464, PubMed:10373108). 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}.
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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_STEB01000014.1.
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 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; -.
DR AlphaFoldDB; P00363; -.
DR SMR; P00363; -.
DR BioGRID; 4260883; 174.
DR ComplexPortal; CPX-1967; Plasma membrane fumarate reductase complex.
DR DIP; DIP-9681N; -.
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; P00363; -.
DR PRIDE; P00363; -.
DR EnsemblBacteria; AAC77114; AAC77114; b4154.
DR EnsemblBacteria; BAE78158; BAE78158; BAE78158.
DR GeneID; 66671932; -.
DR GeneID; 948667; -.
DR KEGG; ecj:JW4115; -.
DR KEGG; eco:b4154; -.
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 PhylomeDB; P00363; -.
DR BioCyc; EcoCyc:FUM-FLAVO; -.
DR BioCyc; MetaCyc:FUM-FLAVO; -.
DR BRENDA; 1.3.5.4; 2026.
DR SABIO-RK; P00363; -.
DR EvolutionaryTrace; P00363; -.
DR PRO; PR:P00363; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045284; C:plasma membrane fumarate reductase complex; IDA:EcoCyc.
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:0102040; F:fumarate reductase (menaquinone); IEA:UniProtKB-EC.
DR GO; GO:0000104; F:succinate dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0009061; P:anaerobic respiration; IMP:EcoCyc.
DR GO; GO:0044780; P:bacterial-type flagellum assembly; IMP:EcoCyc.
DR GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IMP:EcoCyc.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0006113; P:fermentation; IMP:EcoCyc.
DR Gene3D; 3.50.50.60; -; 1.
DR Gene3D; 3.90.700.10; -; 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; IPR005884; Fum_red_fp.
DR InterPro; IPR030664; SdhA/FrdA/AprA.
DR InterPro; IPR011280; Succ_DH/Fum_Rdt_flav_su.
DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR InterPro; IPR014006; Succ_Dhase_FrdA_Gneg.
DR PANTHER; PTHR11632; PTHR11632; 1.
DR PANTHER; PTHR11632:SF53; PTHR11632:SF53; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR Pfam; PF02910; Succ_DH_flav_C; 1.
DR SUPFAM; SSF46977; SSF46977; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF56425; SSF56425; 1.
DR TIGRFAMs; TIGR01176; fum_red_Fp; 1.
DR TIGRFAMs; TIGR01812; sdhA_frdA_Gneg; 1.
DR PROSITE; PS00504; FRD_SDH_FAD_BINDING; 1.
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 583..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 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 332..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"
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
