GAOA_GIBZA
ID GAOA_GIBZA Reviewed; 680 AA.
AC P0CS93; O43098; Q01745; Q4HVH6;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2012, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Galactose oxidase;
DE Short=GAO;
DE Short=GO;
DE Short=GOase;
DE EC=1.1.3.9;
DE Flags: Precursor;
GN Name=GAOA;
OS Gibberella zeae (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=5518;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=ATCC 46032 / CBS 110244 / NRRL 2903;
RX PubMed=1569070; DOI=10.1016/s0021-9258(18)42419-2;
RA McPherson M.J., Ogel Z.B., Stevens C.E., Yadav K.D.S., Keen J.N.,
RA Knowles P.F.;
RT "Galactose oxidase of Dactylium dendroides. Gene cloning and sequence
RT analysis.";
RL J. Biol. Chem. 267:8146-8152(1992).
RN [2]
RP PROTEIN SEQUENCE OF 25-33 AND 42-50, AND PROPEPTIDE CLEAVAGE.
RC STRAIN=ATCC 46032 / CBS 110244 / NRRL 2903;
RX DOI=10.1021/ja993385y;
RA Rogers M.S., Baron A.J., McPherson M.J., Knowles P.F., Dooley D.M.;
RT "Galactose oxidase pro-sequence cleavage and cofactor assembly are self-
RT processing reactions.";
RL J. Am. Chem. Soc. 122:990-991(2000).
RN [3]
RP PROTEIN SEQUENCE OF 42-47, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS
RP OF ARG-371 AND PHE-505.
RX PubMed=15239055; DOI=10.1002/cbic.200300810;
RA Deacon S.E., Mahmoud K., Spooner R.K., Firbank S.J., Knowles P.F.,
RA Phillips S.E., McPherson M.J.;
RT "Enhanced fructose oxidase activity in a galactose oxidase variant.";
RL ChemBioChem 5:972-979(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 98-142.
RC STRAIN=DSM 4527 / 183;
RX DOI=10.1016/S0723-2020(97)80055-0;
RA Niessen M.L., Vogel R.F.;
RT "Specific identification of Fusarium graminearum by PCR with gaoA targeted
RT primers.";
RL Syst. Appl. Microbiol. 20:111-123(1997).
RN [5]
RP FUNCTION.
RX PubMed=13641238; DOI=10.1016/s0021-9258(18)70223-8;
RA Cooper J.A., Smith W., Bacila M., Medina H.;
RT "Galactose oxidase from Polyporus circinatus, Fr.";
RL J. Biol. Chem. 234:445-448(1959).
RN [6]
RP SUBSTRATE SPECIFICITY.
RX PubMed=13863403;
RA Avigad G., Amaral D., Asensio C., Horecker B.L.;
RT "The D-galactose oxidase of Polyporus circinatus.";
RL J. Biol. Chem. 237:2736-2743(1962).
RN [7]
RP TAXONOMY.
RX DOI=10.1016/0006-291X(63)90251-1;
RA Nobles M.K., Madhosingh C.;
RT "Dactylium dendroides (Bull.) Fr. misnamed as Polyporus circinatus Fr.";
RL Biochem. Biophys. Res. Commun. 12:146-147(1963).
RN [8]
RP ACTIVITY REGULATION, AND COPPER-BINDING.
RX PubMed=14012475;
RA Amaral D., Bernstein L., Morse D., Horecker B.L.;
RT "Galactose oxidase of Polyporus circinatus: a copper enzyme.";
RL J. Biol. Chem. 238:2281-2284(1963).
RN [9]
RP FUNCTION, AND SUBUNIT.
RX PubMed=4441089; DOI=10.1016/0003-9861(74)90271-9;
RA Kosman D.J., Ettinger M.J., Weiner R.E., Massaro E.J.;
RT "The molecular properties of the copper enzyme galactose oxidase.";
RL Arch. Biochem. Biophys. 165:456-467(1974).
RN [10]
RP TAXONOMY.
RX AGRICOLA=IND20498749;
RA Ogel Z.B., Brayford D., McPherson M.J.;
RT "Cellulose-triggered sporulation in the galactose oxidase producing fungus
RT Cladobotryum (Dactylium) dendroides NRRL 2903 and its re-identification as
RT a species of Fusarium.";
RL Mycol. Res. 98:474-480(1994).
RN [11]
RP REACTION MECHANISM.
RX PubMed=11401560; DOI=10.1021/bi010303l;
RA Whittaker M.M., Whittaker J.W.;
RT "Catalytic reaction profile for alcohol oxidation by galactose oxidase.";
RL Biochemistry 40:7140-7148(2001).
RN [12]
RP PROTEIN MATURATION.
RX PubMed=12672814; DOI=10.1074/jbc.m300112200;
RA Whittaker M.M., Whittaker J.W.;
RT "Cu(I)-dependent biogenesis of the galactose oxidase redox cofactor.";
RL J. Biol. Chem. 278:22090-22101(2003).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 42-680 IN COMPLEX WITH COPPER
RP IONS.
RX PubMed=2002850; DOI=10.1038/350087a0;
RA Ito N., Phillips S.E.V., Stevens C.E., Ogel Z.B., McPherson M.J.,
RA Keen J.N., Yadav K.D.S., Knowles P.F.;
RT "Novel thioether bond revealed by a 1.7 A crystal structure of galactose
RT oxidase.";
RL Nature 350:87-90(1991).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 42-680 OF MUTANTS GLY-269 AND
RP HIS-331 IN COMPLEX WITH COPPER IONS, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=7929198; DOI=10.1016/s0021-9258(17)31504-1;
RA Baron A.J., Stevens C., Wilmot C., Seneviratne K.D., Blakeley V.,
RA Dooley D.M., Phillips S.E., Knowles P.F., McPherson M.J.;
RT "Structure and mechanism of galactose oxidase. The free radical site.";
RL J. Biol. Chem. 269:25095-25105(1994).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 42-680 OF MUTANT PHE-536 IN
RP COMPLEX WITH COPPER IONS, ACTIVE SITE, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX DOI=10.1007/s007750050139;
RA Reynolds M.P., Baron A.J., Wilmot C.M., Vinecombe E., Stevens C.,
RA Phillips S.E.V., Knowles P.F., McPherson M.J.;
RT "Structure and mechanism of galactose oxidase: catalytic role of tyrosine
RT 495.";
RL J. Biol. Inorg. Chem. 2:327-335(1997).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 25-680.
RX PubMed=11698678; DOI=10.1073/pnas.231463798;
RA Firbank S.J., Rogers M.S., Wilmot C.M., Dooley D.M., Halcrow M.A.,
RA Knowles P.F., McPherson M.J., Phillips S.E.;
RT "Crystal structure of the precursor of galactose oxidase: an unusual self-
RT processing enzyme.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12932-12937(2001).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 42-680 OF MUTANT SER-424 IN
RP COMPLEX WITH COPPER IONS, MASS SPECTROMETRY, MUTAGENESIS OF CYS-424;
RP TYR-477 AND VAL-535, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 46032 / CBS 110244 / NRRL 2903;
RX PubMed=15047910; DOI=10.1093/protein/gzh018;
RA Wilkinson D., Akumanyi N., Hurtado-Guerrero R., Dawkes H., Knowles P.F.,
RA Phillips S.E.V., McPherson M.J.;
RT "Structural and kinetic studies of a series of mutants of galactose oxidase
RT identified by directed evolution.";
RL Protein Eng. Des. Sel. 17:141-148(2004).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 42-680 OF MUTANTS GLY-331; HIS-331
RP AND PHE-331 IN COMPLEX WITH COPPER IONS, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17385891; DOI=10.1021/bi062139d;
RA Rogers M.S., Tyler E.M., Akyumani N., Kurtis C.R., Spooner R.K.,
RA Deacon S.E., Tamber S., Firbank S.J., Mahmoud K., Knowles P.F.,
RA Phillips S.E.V., McPherson M.J., Dooley D.M.;
RT "The stacking tryptophan of galactose oxidase: a second-coordination sphere
RT residue that has profound effects on tyrosyl radical behavior and enzyme
RT catalysis.";
RL Biochemistry 46:4606-4618(2007).
CC -!- FUNCTION: Catalyzes the sterospecific oxidation of primary alcohols to
CC the corresponding aldehydes. The biologically relevant substrate of the
CC enzyme is not known as the enzyme exhibits broad substrate specificity
CC from small alcohols through sugars to oligo- and polysaccharides.
CC {ECO:0000269|PubMed:13641238, ECO:0000269|PubMed:4441089}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-galactose + O2 = D-galacto-hexodialdose + H2O2;
CC Xref=Rhea:RHEA:24160, ChEBI:CHEBI:4139, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16222, ChEBI:CHEBI:16240; EC=1.1.3.9;
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Note=Binds 1 Cu(2+) ion per subunit.;
CC -!- ACTIVITY REGULATION: Inhibited by diethyldithiocarbamate.
CC {ECO:0000269|PubMed:14012475}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=56 mM for 1-methyl-alpha-D-galactopyranoside
CC {ECO:0000269|PubMed:15047910, ECO:0000269|PubMed:15239055,
CC ECO:0000269|PubMed:17385891, ECO:0000269|PubMed:7929198,
CC ECO:0000269|Ref.15};
CC KM=57 mM for 2-methylene-1,3-propanediol
CC {ECO:0000269|PubMed:15047910, ECO:0000269|PubMed:15239055,
CC ECO:0000269|PubMed:17385891, ECO:0000269|PubMed:7929198,
CC ECO:0000269|Ref.15};
CC KM=68 mM for D-galactose {ECO:0000269|PubMed:15047910,
CC ECO:0000269|PubMed:15239055, ECO:0000269|PubMed:17385891,
CC ECO:0000269|PubMed:7929198, ECO:0000269|Ref.15};
CC KM=2.5 M for D-fructose {ECO:0000269|PubMed:15047910,
CC ECO:0000269|PubMed:15239055, ECO:0000269|PubMed:17385891,
CC ECO:0000269|PubMed:7929198, ECO:0000269|Ref.15};
CC pH dependence:
CC Optimum pH is 7. Active from pH 5.7 to 9.4.
CC {ECO:0000269|PubMed:15047910, ECO:0000269|PubMed:15239055,
CC ECO:0000269|PubMed:17385891, ECO:0000269|PubMed:7929198,
CC ECO:0000269|Ref.15};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15047910,
CC ECO:0000269|PubMed:17385891, ECO:0000269|PubMed:2002850,
CC ECO:0000269|PubMed:4441089, ECO:0000269|PubMed:7929198,
CC ECO:0000269|Ref.15}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: Galactose oxidase contains a protein-derived free radical
CC cofactor. In the active state, Tyr-313, which is cross-linked to Cys-
CC 269 via a thioether bond, is oxidized to a radical and acts with Cu(2+)
CC as a two-electron acceptor in the oxidation reaction. The cross-link is
CC believed to modulate the redox potential of the tyrosyl radical, which
CC is further stabilized by a stacking interaction with Trp-331 in the
CC active site. The post-translational formation of the cross-link is
CC closely linked to the propeptide cleavage event, and both are copper-
CC dependent, autocatalytic processes. The propeptide may act as an
CC intramolecular chaperone, facilitating thioester bond formation and
CC copper binding by positioning of active-site residues, including copper
CC ligands.
CC -!- MASS SPECTROMETRY: Mass=68520; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:15047910};
CC -!- CAUTION: Was originally thought to originate from Polyporus circinatus
CC then later from Dactylium dendroides and is now known to be originating
CC from Gibberella (Fusarium). {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Worthington enzyme manual;
CC URL="https://www.worthington-biochem.com/GAO/";
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DR EMBL; M86819; AAA16228.1; -; Unassigned_DNA.
DR EMBL; AH005781; AAB94635.1; -; Genomic_DNA.
DR PDB; 1GOF; X-ray; 1.70 A; A=42-680.
DR PDB; 1GOG; X-ray; 1.90 A; A=42-680.
DR PDB; 1GOH; X-ray; 2.20 A; A=42-680.
DR PDB; 1K3I; X-ray; 1.40 A; A=25-680.
DR PDB; 1T2X; X-ray; 2.30 A; A=42-680.
DR PDB; 2EIB; X-ray; 2.10 A; A=42-680.
DR PDB; 2EIC; X-ray; 2.80 A; A=42-680.
DR PDB; 2EID; X-ray; 2.20 A; A=42-680.
DR PDB; 2EIE; X-ray; 1.80 A; A=42-680.
DR PDB; 2JKX; X-ray; 1.84 A; A=42-680.
DR PDB; 2VZ1; X-ray; 1.91 A; A=42-680.
DR PDB; 2VZ3; X-ray; 1.90 A; A=42-680.
DR PDB; 2WQ8; X-ray; 2.19 A; A=42-680.
DR PDB; 6XLR; X-ray; 1.23 A; A=42-680.
DR PDB; 6XLS; X-ray; 1.80 A; A=42-680.
DR PDB; 6XLT; X-ray; 1.48 A; A=42-680.
DR PDBsum; 1GOF; -.
DR PDBsum; 1GOG; -.
DR PDBsum; 1GOH; -.
DR PDBsum; 1K3I; -.
DR PDBsum; 1T2X; -.
DR PDBsum; 2EIB; -.
DR PDBsum; 2EIC; -.
DR PDBsum; 2EID; -.
DR PDBsum; 2EIE; -.
DR PDBsum; 2JKX; -.
DR PDBsum; 2VZ1; -.
DR PDBsum; 2VZ3; -.
DR PDBsum; 2WQ8; -.
DR PDBsum; 6XLR; -.
DR PDBsum; 6XLS; -.
DR PDBsum; 6XLT; -.
DR AlphaFoldDB; P0CS93; -.
DR SMR; P0CS93; -.
DR CAZy; AA5; Auxiliary Activities 5.
DR CAZy; CBM32; Carbohydrate-Binding Module Family 32.
DR BioCyc; MetaCyc:MON-15357; -.
DR BRENDA; 1.1.3.9; 2428.
DR SABIO-RK; P0CS93; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0045480; F:galactose oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd02851; E_set_GO_C; 1.
DR CDD; cd00057; FA58C; 1.
DR Gene3D; 2.130.10.80; -; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR011043; Gal_Oxase/kelch_b-propeller.
DR InterPro; IPR037293; Gal_Oxidase_central_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR015202; GO-like_E_set.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR006652; Kelch_1.
DR Pfam; PF09118; DUF1929; 1.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF01344; Kelch_1; 1.
DR SMART; SM00231; FA58C; 1.
DR SMART; SM00612; Kelch; 3.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF50965; SSF50965; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS50022; FA58C_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Copper; Direct protein sequencing; Disulfide bond;
KW Kelch repeat; Metal-binding; Oxidoreductase; Repeat; Secreted; Signal;
KW Thioether bond.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|Ref.2"
FT PROPEP 25..41
FT /evidence="ECO:0000269|PubMed:15239055, ECO:0000269|Ref.2"
FT /id="PRO_0000285407"
FT CHAIN 42..680
FT /note="Galactose oxidase"
FT /id="PRO_0000016610"
FT DOMAIN 42..189
FT /note="F5/8 type C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT REPEAT 223..268
FT /note="Kelch 1"
FT REPEAT 279..321
FT /note="Kelch 2"
FT REPEAT 323..372
FT /note="Kelch 3"
FT REPEAT 436..490
FT /note="Kelch 4"
FT REPEAT 492..544
FT /note="Kelch 5"
FT ACT_SITE 536
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|Ref.15"
FT BINDING 313
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT BINDING 536
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT BINDING 537
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT BINDING 622
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT DISULFID 59..68
FT DISULFID 556..559
FT CROSSLNK 269..313
FT /note="3'-(S-cysteinyl)-tyrosine (Cys-Tyr)"
FT MUTAGEN 269
FT /note="C->G: Reduces catalytic activity more than 10000-
FT fold."
FT MUTAGEN 331
FT /note="W->F: Reduces catalytic efficiency 50-fold and
FT substrate affinity 36-fold."
FT MUTAGEN 331
FT /note="W->G: Reduces substrate affinity 20-fold and
FT catalytic activity more than 6000-fold."
FT MUTAGEN 331
FT /note="W->H: Reduces catalytic efficiency 1000-fold."
FT MUTAGEN 371
FT /note="R->A: Reduces catalytic efficiency 250-fold and
FT substrate affinity 22-fold for D-galactose, but improves
FT catalytic efficiency 1.8-fold towards D-fructose."
FT /evidence="ECO:0000269|PubMed:15239055"
FT MUTAGEN 371
FT /note="R->K: Reduces catalytic efficiency 45-fold and
FT substrate affinity 8.7-fold for D-galactose, but improves
FT catalytic efficiency 8-fold towards D-fructose."
FT /evidence="ECO:0000269|PubMed:15239055"
FT MUTAGEN 424
FT /note="C->A: Reduces catalytic efficiency 1.5- to 2-fold
FT towards D-galactose and 1-methyl-alpha-D-
FT galactopyranoside."
FT /evidence="ECO:0000269|PubMed:15047910"
FT MUTAGEN 424
FT /note="C->S: Improves catalytic efficiency 3- to 4-fold
FT towards D-galactose and 1-methyl-alpha-D-galactopyranoside,
FT mainly by increasing the affinity for the substrates.
FT Improves catalytic efficiency 5.3-fold towards D-galactose;
FT when associated with H-477. Improves catalytic efficiency
FT 4.9-fold towards 1-methyl-alpha-D-galactopyranoside; when
FT associated with A-535. Improves catalytic activity 4.7-fold
FT towards D-galactose, but only 1.8-fold towards 1-methyl-
FT alpha-D-galactopyranoside; when associated with A-477."
FT /evidence="ECO:0000269|PubMed:15047910"
FT MUTAGEN 477
FT /note="Y->A: No effect. Improves catalytic efficiency 2- to
FT 3-fold towards D-galactose and 1-methyl-alpha-D-
FT galactopyranoside; when associated with A-535. Improves
FT catalytic activity 4.7-fold towards D-galactose, but only
FT 1.8-fold towards 1-methyl-alpha-D-galactopyranoside; when
FT associated with S-424."
FT /evidence="ECO:0000269|PubMed:15047910"
FT MUTAGEN 477
FT /note="Y->H: No effect. Improves catalytic efficiency 5.3-
FT fold towards D-galactose; when associated with S-424."
FT /evidence="ECO:0000269|PubMed:15047910"
FT MUTAGEN 505
FT /note="F->A: Reduces catalytic efficiency 166-fold and
FT substrate affinity 9-fold."
FT /evidence="ECO:0000269|PubMed:15239055"
FT MUTAGEN 535
FT /note="V->A: Improves catalytic efficiency 1.3- to 1.8-
FT fold. Improves catalytic efficiency 2- to 3-fold towards D-
FT galactose and 1-methyl-alpha-D-galactopyranoside; when
FT associated with A-477. Improves catalytic efficiency 4.9-
FT fold towards 1-methyl-alpha-D-galactopyranoside; when
FT associated with S-424."
FT /evidence="ECO:0000269|PubMed:15047910"
FT MUTAGEN 536
FT /note="Y->F: Reduces catalytic efficiency 1000-fold, but
FT does not reduce substrate affinity."
FT CONFLICT 111
FT /note="M -> I (in Ref. 4; AAB94635)"
FT /evidence="ECO:0000305"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:1K3I"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:6XLR"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:6XLR"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:6XLR"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:6XLR"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:6XLR"
FT STRAND 94..112
FT /evidence="ECO:0007829|PDB:6XLR"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:6XLR"
FT STRAND 125..135
FT /evidence="ECO:0007829|PDB:6XLR"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:6XLR"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:6XLR"
FT STRAND 153..169
FT /evidence="ECO:0007829|PDB:6XLR"
FT STRAND 180..188
FT /evidence="ECO:0007829|PDB:6XLR"
FT STRAND 201..207
FT /evidence="ECO:0007829|PDB:6XLR"
FT STRAND 213..217
FT /evidence="ECO:0007829|PDB:6XLR"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:6XLR"
FT STRAND 224..227
FT /evidence="ECO:0007829|PDB:6XLR"
FT STRAND 229..233
FT /evidence="ECO:0007829|PDB:6XLR"
FT STRAND 243..248
FT /evidence="ECO:0007829|PDB:6XLR"
FT TURN 250..252
FT /evidence="ECO:0007829|PDB:6XLR"
FT STRAND 255..260
FT /evidence="ECO:0007829|PDB:6XLR"
FT STRAND 271..274
FT /evidence="ECO:0007829|PDB:6XLR"
FT STRAND 278..283
FT /evidence="ECO:0007829|PDB:6XLR"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:1K3I"
FT STRAND 291..295
FT /evidence="ECO:0007829|PDB:6XLR"
FT TURN 296..299
FT /evidence="ECO:0007829|PDB:6XLR"
FT STRAND 300..303
FT /evidence="ECO:0007829|PDB:6XLR"
FT STRAND 315..318
FT /evidence="ECO:0007829|PDB:6XLR"
FT STRAND 324..327
FT /evidence="ECO:0007829|PDB:6XLR"
FT STRAND 330..333
FT /evidence="ECO:0007829|PDB:6XLR"
FT STRAND 340..344
FT /evidence="ECO:0007829|PDB:6XLR"
FT TURN 345..348
FT /evidence="ECO:0007829|PDB:6XLR"
FT STRAND 349..353
FT /evidence="ECO:0007829|PDB:6XLR"
FT HELIX 359..361
FT /evidence="ECO:0007829|PDB:6XLR"
FT TURN 366..368
FT /evidence="ECO:0007829|PDB:6XLR"
FT HELIX 369..372
FT /evidence="ECO:0007829|PDB:6XLR"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:6XLR"
FT HELIX 382..384
FT /evidence="ECO:0007829|PDB:6XLR"
FT STRAND 386..388
FT /evidence="ECO:0007829|PDB:6XLR"
FT STRAND 391..399
FT /evidence="ECO:0007829|PDB:6XLR"
FT STRAND 405..411
FT /evidence="ECO:0007829|PDB:6XLR"
FT STRAND 426..431
FT /evidence="ECO:0007829|PDB:6XLR"
FT TURN 432..435
FT /evidence="ECO:0007829|PDB:6XLR"
FT STRAND 436..440
FT /evidence="ECO:0007829|PDB:6XLR"
FT STRAND 443..448
FT /evidence="ECO:0007829|PDB:6XLR"
FT STRAND 455..459
FT /evidence="ECO:0007829|PDB:6XLR"
FT STRAND 468..471
FT /evidence="ECO:0007829|PDB:6XLR"
FT STRAND 480..482
FT /evidence="ECO:0007829|PDB:1GOH"
FT STRAND 484..487
FT /evidence="ECO:0007829|PDB:6XLR"
FT STRAND 493..496
FT /evidence="ECO:0007829|PDB:6XLR"
FT STRAND 499..501
FT /evidence="ECO:0007829|PDB:6XLR"
FT STRAND 515..518
FT /evidence="ECO:0007829|PDB:6XLR"
FT TURN 519..522
FT /evidence="ECO:0007829|PDB:6XLR"
FT STRAND 523..526
FT /evidence="ECO:0007829|PDB:6XLR"
FT STRAND 538..542
FT /evidence="ECO:0007829|PDB:6XLR"
FT STRAND 548..552
FT /evidence="ECO:0007829|PDB:6XLR"
FT STRAND 565..570
FT /evidence="ECO:0007829|PDB:6XLR"
FT HELIX 572..574
FT /evidence="ECO:0007829|PDB:6XLR"
FT STRAND 579..581
FT /evidence="ECO:0007829|PDB:6XLR"
FT STRAND 587..591
FT /evidence="ECO:0007829|PDB:6XLR"
FT STRAND 593..596
FT /evidence="ECO:0007829|PDB:6XLR"
FT STRAND 600..607
FT /evidence="ECO:0007829|PDB:6XLR"
FT STRAND 610..616
FT /evidence="ECO:0007829|PDB:6XLR"
FT STRAND 619..621
FT /evidence="ECO:0007829|PDB:6XLR"
FT STRAND 630..632
FT /evidence="ECO:0007829|PDB:6XLR"
FT STRAND 636..639
FT /evidence="ECO:0007829|PDB:6XLR"
FT STRAND 642..646
FT /evidence="ECO:0007829|PDB:6XLR"
FT TURN 651..653
FT /evidence="ECO:0007829|PDB:6XLR"
FT STRAND 656..664
FT /evidence="ECO:0007829|PDB:6XLR"
FT STRAND 674..679
FT /evidence="ECO:0007829|PDB:6XLR"
SQ SEQUENCE 680 AA; 72823 MW; 2F97C561B63E46E9 CRC64;
MKHLLTLALC FSSINAVAVT VPHKAVGTGI PEGSLQFLSL RASAPIGSAI SRNNWAVTCD
SAQSGNECNK AIDGNKDTFW HTFYGANGDP KPPHTYTIDM KTTQNVNGLS MLPRQDGNQN
GWIGRHEVYL SSDGTNWGSP VASGSWFADS TTKYSNFETR PARYVRLVAI TEANGQPWTS
IAEINVFQAS SYTAPQPGLG RWGPTIDLPI VPAAAAIEPT SGRVLMWSSY RNDAFGGSPG
GITLTSSWDP STGIVSDRTV TVTKHDMFCP GISMDGNGQI VVTGGNDAKK TSLYDSSSDS
WIPGPDMQVA RGYQSSATMS DGRVFTIGGS WSGGVFEKNG EVYSPSSKTW TSLPNAKVNP
MLTADKQGLY RSDNHAWLFG WKKGSVFQAG PSTAMNWYYT SGSGDVKSAG KRQSNRGVAP
DAMCGNAVMY DAVKGKILTF GGSPDYQDSD ATTNAHIITL GEPGTSPNTV FASNGLYFAR
TFHTSVVLPD GSTFITGGQR RGIPFEDSTP VFTPEIYVPE QDTFYKQNPN SIVRVYHSIS
LLLPDGRVFN GGGGLCGDCT TNHFDAQIFT PNYLYNSNGN LATRPKITRT STQSVKVGGR
ITISTDSSIS KASLIRYGTA THTVNTDQRR IPLTLTNNGG NSYSFQVPSD SGVALPGYWM
LFVMNSAGVP SVASTIRVTQ
