HGGL1_MAIZE
ID HGGL1_MAIZE Reviewed; 566 AA.
AC P49235;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase 1, chloroplastic;
DE EC=3.2.1.182;
DE AltName: Full=Beta-D-glucoside glucohydrolase;
DE AltName: Full=Beta-glucosidase 1;
DE Short=ZmGlu1;
DE EC=3.2.1.21;
DE Flags: Precursor;
GN Name=GLU1;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Inbred line K55; TISSUE=Shoot;
RA Esen A., Shahid M.;
RL Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. MUTIN; TISSUE=Coleoptile;
RX PubMed=8235622; DOI=10.1126/science.8235622;
RA Brzobohaty B., Moore I., Kristoffersen P., Bako L., Campos N., Schell J.,
RA Palme K.;
RT "Release of active cytokinin by a beta-glucosidase localized to the maize
RT root meristem.";
RL Science 262:1051-1054(1993).
RN [3]
RP PROTEIN SEQUENCE OF 55-74, FUNCTION, SUBUNIT, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=cv. Inbred line K55;
RX PubMed=16668611; DOI=10.1104/pp.98.1.174;
RA Esen A.;
RT "Purification and partial characterization of Maize (Zea Mays L.) beta-
RT glucosidase.";
RL Plant Physiol. 98:174-182(1992).
RN [4]
RP PROTEIN SEQUENCE OF 55-69; 165-174; 207-213 AND 217-235.
RC TISSUE=Coleoptile;
RX AGRICOLA=IND20551642; DOI=10.1007/BF00224104;
RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., Pernollet J.-C.,
RA Zivy M., de Vienne D.;
RT "The maize two dimensional gel protein database: towards an integrated
RT genome analysis program.";
RL Theor. Appl. Genet. 93:997-1005(1996).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX DOI=10.1016/0168-9452(94)90162-7;
RA Babcock G.D., Esen A.;
RT "Substrate specificity of maize beta-glucosidase.";
RL Plant Sci. 101:31-39(1994).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBUNIT, SUBSTRATE
RP SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10099619;
RX DOI=10.1002/(sici)1097-0290(19990520)63:4<392::aid-bit2>3.0.co;2-m;
RA Cicek M., Esen A.;
RT "Expression of soluble and catalytically active plant (monocot) beta-
RT glucosidases in E. coli.";
RL Biotechnol. Bioeng. 63:392-400(1999).
RN [7]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10497081; DOI=10.1006/prep.1999.1108;
RA Zouhar J., Nanak E., Brzobohaty B.;
RT "Expression, single-step purification, and matrix-assisted refolding of a
RT maize cytokinin glucoside-specific beta-glucosidase.";
RL Protein Expr. Purif. 17:153-162(1999).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 55-566 IN COMPLEX WITH SUBSTRATES
RP AND THE INHIBITOR PARA-HYDROXY-S-MANDELONITRILE BETA-GLUCOSIDE, MUTAGENESIS
RP OF GLU-245, AND ACTIVITY REGULATION.
RX PubMed=11106394; DOI=10.1073/pnas.97.25.13555;
RA Czjzek M., Cicek M., Zamboni V., Bevan D.R., Henrissat B., Esen A.;
RT "The mechanism of substrate (aglycone) specificity in beta -glucosidases is
RT revealed by crystal structures of mutant maize beta -glucosidase-DIMBOA,
RT -DIMBOAGlc, and -dhurrin complexes.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:13555-13560(2000).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 55-566 IN COMPLEX WITH THE
RP INHIBITOR P-NITROPHENYL BETA-D-THIOGLUCOSIDE, ACTIVITY REGULATION,
RP HOMODIMER, AND DISULFIDE BOND.
RX PubMed=11171077; DOI=10.1042/0264-6021:3540037;
RA Czjzek M., Cicek M., Zamboni V., Burmeister W.P., Bevan D.R., Henrissat B.,
RA Esen A.;
RT "Crystal structure of a monocotyledon (maize ZMGlu1) beta-glucosidase and a
RT model of its complex with p-nitrophenyl beta-D-thioglucoside.";
RL Biochem. J. 354:37-46(2001).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 60-566, MUTAGENESIS OF GLU-245;
RP PHE-252; MET-317; GLU-460 AND ILE-463, SUBUNIT, AND DISULFIDE BOND.
RX PubMed=11706179; DOI=10.1104/pp.010712;
RA Zouhar J., Vevodova J., Marek J., Damborsky J., Su X.-D., Brzobohaty B.;
RT "Insights into the functional architecture of the catalytic center of a
RT maize beta-glucosidase Zm-p60.1.";
RL Plant Physiol. 127:973-985(2001).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 55-566 IN COMPLEX WITH SUBSTRATE,
RP AND DISULFIDE BOND.
RX PubMed=12684498; DOI=10.1074/jbc.m301978200;
RA Verdoucq L., Czjzek M., Moriniere J., Bevan D.R., Esen A.;
RT "Mutational and structural analysis of aglycone specificity in maize and
RT sorghum beta-glucosidases.";
RL J. Biol. Chem. 278:25055-25062(2003).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 55-566 IN COMPLEX WITH SUBSTRATES
RP AND THE INHIBITOR GLUCOTETRAZOLE, MUTAGENESIS OF GLU-245,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND DISULFIDE BOND.
RX PubMed=15148317; DOI=10.1074/jbc.m402918200;
RA Verdoucq L., Moriniere J., Bevan D.R., Esen A., Vasella A., Henrissat B.,
RA Czjzek M.;
RT "Structural determinants of substrate specificity in family 1 beta-
RT glucosidases: novel insights from the crystal structure of sorghum
RT dhurrinase-1, a plant beta-glucosidase with strict specificity, in complex
RT with its natural substrate.";
RL J. Biol. Chem. 279:31796-31803(2004).
CC -!- FUNCTION: Is implicated in many functions such as ABA metabolism,
CC hydrolysis of conjugated gibberellins, conversion of storage forms of
CC cytokinins to active forms. Also acts in defense of young plant parts
CC against pests via the production of hydroxamic acids from hydroxamic
CC acid glucosides. Enzymatic activity is highly correlated with plant
CC growth. The preferred substrate is DIMBOA-beta-D-glucoside. Hydrolyzes
CC the chromogenic substrate 6-bromo-2-naphthyl-beta-D-glucoside (6BNGlc)
CC and various artificial aryl beta-glucosides. No activity with
CC cellobiose, arbutin, gentiobiose, linamarin or dhurrin as substrates.
CC {ECO:0000269|PubMed:10099619, ECO:0000269|PubMed:16668611,
CC ECO:0000269|Ref.5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues
CC with release of beta-D-glucose.; EC=3.2.1.21;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=DIMBOA beta-D-glucoside + H2O = D-glucose + DIMBOA;
CC Xref=Rhea:RHEA:33975, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:18048, ChEBI:CHEBI:37573; EC=3.2.1.182;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=DIBOA beta-D-glucoside + H2O = D-glucose + DIBOA;
CC Xref=Rhea:RHEA:33979, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:63558, ChEBI:CHEBI:63670; EC=3.2.1.182;
CC -!- ACTIVITY REGULATION: Reversibly inhibited by micromolar concentrations
CC of Hg(2+) or Ag(+), but irreversibly inhibited by alkylation in
CC presence of urea. Competitive inhibition by p-nitrophenyl beta-D-
CC thioglucoside (pNPTGlc), glucotetrazole, and para-hydroxy-S-
CC mandelonitrile beta-glucoside (dhurrin). {ECO:0000269|PubMed:11106394,
CC ECO:0000269|PubMed:11171077}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.14 mM for 4-methylumbelliferyl beta-D-glucopyranoside (MUG)
CC {ECO:0000269|PubMed:10099619, ECO:0000269|PubMed:10497081,
CC ECO:0000269|PubMed:15148317, ECO:0000269|PubMed:16668611,
CC ECO:0000269|Ref.5};
CC KM=0.64 mM for p-nitrophenyl beta-D-glucopyranoside (PNPG)
CC {ECO:0000269|PubMed:10099619, ECO:0000269|PubMed:10497081,
CC ECO:0000269|PubMed:15148317, ECO:0000269|PubMed:16668611,
CC ECO:0000269|Ref.5};
CC KM=0.41 mM for p-nitrophenyl beta-D-glucopyranoside (PNPG) (with
CC recombinant enzyme) {ECO:0000269|PubMed:10099619,
CC ECO:0000269|PubMed:10497081, ECO:0000269|PubMed:15148317,
CC ECO:0000269|PubMed:16668611, ECO:0000269|Ref.5};
CC KM=98 uM for DIMBOA-beta-D-glucoside {ECO:0000269|PubMed:10099619,
CC ECO:0000269|PubMed:10497081, ECO:0000269|PubMed:15148317,
CC ECO:0000269|PubMed:16668611, ECO:0000269|Ref.5};
CC KM=0.251 mM for n-octyl-beta-D-glucopyranoside
CC {ECO:0000269|PubMed:10099619, ECO:0000269|PubMed:10497081,
CC ECO:0000269|PubMed:15148317, ECO:0000269|PubMed:16668611,
CC ECO:0000269|Ref.5};
CC KM=0.394 mM for p-nitrophenyl beta-D-xyloside
CC {ECO:0000269|PubMed:10099619, ECO:0000269|PubMed:10497081,
CC ECO:0000269|PubMed:15148317, ECO:0000269|PubMed:16668611,
CC ECO:0000269|Ref.5};
CC KM=0.648 mM for p-nitrophenyl beta-D-fucopyranoside
CC {ECO:0000269|PubMed:10099619, ECO:0000269|PubMed:10497081,
CC ECO:0000269|PubMed:15148317, ECO:0000269|PubMed:16668611,
CC ECO:0000269|Ref.5};
CC KM=0.674 mM for p-nitrophenyl beta-D-cellobioside
CC {ECO:0000269|PubMed:10099619, ECO:0000269|PubMed:10497081,
CC ECO:0000269|PubMed:15148317, ECO:0000269|PubMed:16668611,
CC ECO:0000269|Ref.5};
CC KM=0.769 mM for p-nitrophenyl beta-D-mannopyranoside
CC {ECO:0000269|PubMed:10099619, ECO:0000269|PubMed:10497081,
CC ECO:0000269|PubMed:15148317, ECO:0000269|PubMed:16668611,
CC ECO:0000269|Ref.5};
CC KM=1.64 mM for o-nitrophenyl beta-D-glucopyranoside
CC {ECO:0000269|PubMed:10099619, ECO:0000269|PubMed:10497081,
CC ECO:0000269|PubMed:15148317, ECO:0000269|PubMed:16668611,
CC ECO:0000269|Ref.5};
CC KM=1.42 mM for o-nitrophenyl beta-D-glucopyranoside (with recombinant
CC enzyme) {ECO:0000269|PubMed:10099619, ECO:0000269|PubMed:10497081,
CC ECO:0000269|PubMed:15148317, ECO:0000269|PubMed:16668611,
CC ECO:0000269|Ref.5};
CC KM=4.32 mM for p-nitrophenyl beta-D-galactopyranoside
CC {ECO:0000269|PubMed:10099619, ECO:0000269|PubMed:10497081,
CC ECO:0000269|PubMed:15148317, ECO:0000269|PubMed:16668611,
CC ECO:0000269|Ref.5};
CC Vmax=225.4 umol/h/ug enzyme with p-nitrophenyl beta-D-glucopyranoside
CC as substrate (with recombinant enzyme) {ECO:0000269|PubMed:10099619,
CC ECO:0000269|PubMed:10497081, ECO:0000269|PubMed:15148317,
CC ECO:0000269|PubMed:16668611, ECO:0000269|Ref.5};
CC Vmax=282.7 umol/h/ug enzyme with o-nitrophenyl beta-D-glucopyranoside
CC as substrate (with recombinant enzyme) {ECO:0000269|PubMed:10099619,
CC ECO:0000269|PubMed:10497081, ECO:0000269|PubMed:15148317,
CC ECO:0000269|PubMed:16668611, ECO:0000269|Ref.5};
CC pH dependence:
CC Optimum pH is 5.8. {ECO:0000269|PubMed:10099619,
CC ECO:0000269|PubMed:10497081, ECO:0000269|PubMed:15148317,
CC ECO:0000269|PubMed:16668611, ECO:0000269|Ref.5};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius. Loses activity when is
CC heated at 55 degrees Celsius. {ECO:0000269|PubMed:10099619,
CC ECO:0000269|PubMed:10497081, ECO:0000269|PubMed:15148317,
CC ECO:0000269|PubMed:16668611, ECO:0000269|Ref.5};
CC -!- SUBUNIT: Homo- and heterodimer. {ECO:0000269|PubMed:10099619,
CC ECO:0000269|PubMed:11106394, ECO:0000269|PubMed:11171077,
CC ECO:0000269|PubMed:11706179, ECO:0000269|PubMed:15148317,
CC ECO:0000269|PubMed:16668611}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- TISSUE SPECIFICITY: Expressed in all seedling parts. Most abundant in
CC the coleoptile. {ECO:0000269|PubMed:10099619}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
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DR EMBL; U25157; AAA65946.1; -; mRNA.
DR EMBL; X74217; CAA52293.1; -; mRNA.
DR PIR; A48860; A48860.
DR RefSeq; NP_001105454.1; NM_001111984.1.
DR PDB; 1E1E; X-ray; 2.50 A; A/B=55-566.
DR PDB; 1E1F; X-ray; 2.60 A; A/B=55-566.
DR PDB; 1E4L; X-ray; 2.20 A; A/B=55-566.
DR PDB; 1E4N; X-ray; 2.10 A; A/B=55-566.
DR PDB; 1E55; X-ray; 2.00 A; A/B=55-566.
DR PDB; 1E56; X-ray; 2.10 A; A/B=55-566.
DR PDB; 1H49; X-ray; 1.90 A; A/B=55-566.
DR PDB; 1HXJ; X-ray; 2.05 A; A/B=60-566.
DR PDB; 1V08; X-ray; 1.90 A; A/B=55-566.
DR PDBsum; 1E1E; -.
DR PDBsum; 1E1F; -.
DR PDBsum; 1E4L; -.
DR PDBsum; 1E4N; -.
DR PDBsum; 1E55; -.
DR PDBsum; 1E56; -.
DR PDBsum; 1H49; -.
DR PDBsum; 1HXJ; -.
DR PDBsum; 1V08; -.
DR AlphaFoldDB; P49235; -.
DR SMR; P49235; -.
DR STRING; 4577.GRMZM2G016890_P01; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR PaxDb; P49235; -.
DR PRIDE; P49235; -.
DR ProMEX; P49235; -.
DR EnsemblPlants; Zm00001eb411380_T001; Zm00001eb411380_P001; Zm00001eb411380.
DR GeneID; 542414; -.
DR Gramene; Zm00001eb411380_T001; Zm00001eb411380_P001; Zm00001eb411380.
DR MaizeGDB; 13870; -.
DR eggNOG; KOG0626; Eukaryota.
DR OMA; WFAGFTE; -.
DR OrthoDB; 408001at2759; -.
DR BioCyc; MetaCyc:MON-10621; -.
DR BRENDA; 3.2.1.182; 6752.
DR BRENDA; 3.2.1.21; 6752.
DR SABIO-RK; P49235; -.
DR EvolutionaryTrace; P49235; -.
DR Proteomes; UP000007305; Chromosome 10.
DR ExpressionAtlas; P49235; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0008422; F:beta-glucosidase activity; IDA:UniProtKB.
DR GO; GO:0016162; F:cellulose 1,4-beta-cellobiosidase activity; IDA:UniProtKB.
DR GO; GO:0102726; F:DIMBOA glucoside beta-D-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0015928; F:fucosidase activity; IDA:UniProtKB.
DR GO; GO:0015925; F:galactosidase activity; IDA:UniProtKB.
DR GO; GO:0015923; F:mannosidase activity; IDA:UniProtKB.
DR GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0097599; F:xylanase activity; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0009736; P:cytokinin-activated signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR001360; Glyco_hydro_1.
DR InterPro; IPR018120; Glyco_hydro_1_AS.
DR InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10353; PTHR10353; 1.
DR Pfam; PF00232; Glyco_hydro_1; 1.
DR PRINTS; PR00131; GLHYDRLASE1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
DR PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Cytokinin signaling pathway;
KW Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..54
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:16668611, ECO:0000269|Ref.4"
FT CHAIN 55..566
FT /note="4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-
FT benzoxazin-2-yl glucoside beta-D-glucosidase 1,
FT chloroplastic"
FT /id="PRO_0000011763"
FT REGION 17..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..361
FT /note="Dimerization"
FT REGION 394..405
FT /note="Dimerization"
FT REGION 450..453
FT /note="Dimerization"
FT COMPBIAS 24..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 245
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q7XKV4"
FT ACT_SITE 460
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q7XKV4"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11106394,
FT ECO:0000269|PubMed:12684498, ECO:0007744|PDB:1E56,
FT ECO:0007744|PDB:1H49"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11106394,
FT ECO:0007744|PDB:1E56"
FT BINDING 244
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11106394,
FT ECO:0007744|PDB:1E56"
FT BINDING 387
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11106394,
FT ECO:0007744|PDB:1E56"
FT BINDING 511
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11106394,
FT ECO:0000269|PubMed:12684498, ECO:0007744|PDB:1E55,
FT ECO:0007744|PDB:1E56, ECO:0007744|PDB:1H49"
FT BINDING 518..519
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11106394,
FT ECO:0000269|PubMed:12684498, ECO:0007744|PDB:1E55,
FT ECO:0007744|PDB:1E56, ECO:0007744|PDB:1H49"
FT BINDING 527
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11106394,
FT ECO:0007744|PDB:1E56"
FT DISULFID 264..270
FT /evidence="ECO:0000269|PubMed:11171077,
FT ECO:0000269|PubMed:11706179, ECO:0000269|PubMed:15148317"
FT MUTAGEN 245
FT /note="E->D,Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11106394,
FT ECO:0000269|PubMed:11706179, ECO:0000269|PubMed:15148317"
FT MUTAGEN 252
FT /note="F->I,W,Y: Reduced substrate affinity."
FT /evidence="ECO:0000269|PubMed:11706179"
FT MUTAGEN 264
FT /note="C->A,D,R,S: Loss of activity due to impaired
FT dimerization."
FT MUTAGEN 270
FT /note="C->A,D,R,S: Loss of activity due to impaired
FT dimerization."
FT MUTAGEN 317
FT /note="M->F,I,V: No effect."
FT /evidence="ECO:0000269|PubMed:11706179"
FT MUTAGEN 460
FT /note="E->D: Loss of activity and impaired dimerization."
FT /evidence="ECO:0000269|PubMed:11706179"
FT MUTAGEN 460
FT /note="E->Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11706179"
FT MUTAGEN 463
FT /note="I->D: Loss of activity due to impaired
FT dimerization."
FT /evidence="ECO:0000269|PubMed:11706179"
FT CONFLICT 477
FT /note="A -> D (in Ref. 2; CAA52293)"
FT /evidence="ECO:0000305"
FT CONFLICT 551
FT /note="E -> Q (in Ref. 2; CAA52293)"
FT /evidence="ECO:0000305"
FT CONFLICT 554
FT /note="T -> A (in Ref. 2; CAA52293)"
FT /evidence="ECO:0000305"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:1H49"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:1H49"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:1H49"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:1H49"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:1E1E"
FT HELIX 106..113
FT /evidence="ECO:0007829|PDB:1H49"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:1H49"
FT HELIX 130..143
FT /evidence="ECO:0007829|PDB:1H49"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:1H49"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:1H49"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:1H49"
FT HELIX 170..185
FT /evidence="ECO:0007829|PDB:1H49"
FT STRAND 189..197
FT /evidence="ECO:0007829|PDB:1H49"
FT HELIX 201..207
FT /evidence="ECO:0007829|PDB:1H49"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:1H49"
FT HELIX 217..233
FT /evidence="ECO:0007829|PDB:1H49"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:1H49"
FT STRAND 239..244
FT /evidence="ECO:0007829|PDB:1H49"
FT HELIX 246..253
FT /evidence="ECO:0007829|PDB:1H49"
FT STRAND 268..272
FT /evidence="ECO:0007829|PDB:1H49"
FT TURN 277..279
FT /evidence="ECO:0007829|PDB:1H49"
FT HELIX 280..302
FT /evidence="ECO:0007829|PDB:1H49"
FT STRAND 309..325
FT /evidence="ECO:0007829|PDB:1H49"
FT HELIX 326..339
FT /evidence="ECO:0007829|PDB:1H49"
FT HELIX 341..349
FT /evidence="ECO:0007829|PDB:1H49"
FT HELIX 354..360
FT /evidence="ECO:0007829|PDB:1H49"
FT HELIX 361..363
FT /evidence="ECO:0007829|PDB:1H49"
FT HELIX 369..375
FT /evidence="ECO:0007829|PDB:1H49"
FT STRAND 380..394
FT /evidence="ECO:0007829|PDB:1H49"
FT HELIX 406..410
FT /evidence="ECO:0007829|PDB:1H49"
FT STRAND 412..417
FT /evidence="ECO:0007829|PDB:1H49"
FT STRAND 423..425
FT /evidence="ECO:0007829|PDB:1H49"
FT STRAND 429..432
FT /evidence="ECO:0007829|PDB:1H49"
FT HELIX 438..449
FT /evidence="ECO:0007829|PDB:1H49"
FT STRAND 456..460
FT /evidence="ECO:0007829|PDB:1H49"
FT STRAND 469..471
FT /evidence="ECO:0007829|PDB:1H49"
FT HELIX 475..479
FT /evidence="ECO:0007829|PDB:1H49"
FT HELIX 482..500
FT /evidence="ECO:0007829|PDB:1H49"
FT STRAND 505..511
FT /evidence="ECO:0007829|PDB:1H49"
FT HELIX 519..521
FT /evidence="ECO:0007829|PDB:1H49"
FT STRAND 524..526
FT /evidence="ECO:0007829|PDB:1H49"
FT STRAND 529..533
FT /evidence="ECO:0007829|PDB:1H49"
FT TURN 534..537
FT /evidence="ECO:0007829|PDB:1H49"
FT STRAND 538..542
FT /evidence="ECO:0007829|PDB:1H49"
FT HELIX 544..554
FT /evidence="ECO:0007829|PDB:1H49"
SQ SEQUENCE 566 AA; 64237 MW; 4EA241258AE3641B CRC64;
MAPLLAAAMN HAAAHPGLRS HLVGPNNESF SRHHLPSSSP QSSKRRCNLS FTTRSARVGS
QNGVQMLSPS EIPQRDWFPS DFTFGAATSA YQIEGAWNED GKGESNWDHF CHNHPERILD
GSNSDIGANS YHMYKTDVRL LKEMGMDAYR FSISWPRILP KGTKEGGINP DGIKYYRNLI
NLLLENGIEP YVTIFHWDVP QALEEKYGGF LDKSHKSIVE DYTYFAKVCF DNFGDKVKNW
LTFNEPQTFT SFSYGTGVFA PGRCSPGLDC AYPTGNSLVE PYTAGHNILL AHAEAVDLYN
KHYKRDDTRI GLAFDVMGRV PYGTSFLDKQ AEERSWDINL GWFLEPVVRG DYPFSMRSLA
RERLPFFKDE QKEKLAGSYN MLGLNYYTSR FSKNIDISPN YSPVLNTDDA YASQEVNGPD
GKPIGPPMGN PWIYMYPEGL KDLLMIMKNK YGNPPIYITE NGIGDVDTKE TPLPMEAALN
DYKRLDYIQR HIATLKESID LGSNVQGYFA WSLLDNFEWF AGFTERYGIV YVDRNNNCTR
YMKESAKWLK EFNTAKKPSK KILTPA
