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 27-MAR-2024, entry version 150. 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 {ECO:0000269|PubMed:10099619, ECO:0000269|Ref.5}; DE AltName: Full=Beta-D-glucoside glucohydrolase; DE AltName: Full=Beta-glucosidase 1; DE Short=ZmGlu1; DE EC=3.2.1.21 {ECO:0000269|PubMed:10099619, ECO:0000269|Ref.5}; 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.127.3.973; 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 Evidence={ECO:0000269|PubMed:10099619, ECO:0000269|Ref.5}; 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 Evidence={ECO:0000269|PubMed:10099619, ECO:0000269|Ref.5}; 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 Evidence={ECO:0000269|PubMed:10099619, ECO:0000269|Ref.5}; 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}. 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; 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.P49235; -. DR CAZy; GH1; Glycoside Hydrolase Family 1. DR PaxDb; 4577-GRMZM2G016890_P01; -. DR ProMEX; P49235; -. DR EnsemblPlants; Zm00001eb411380_T001; Zm00001eb411380_P001; Zm00001eb411380. DR Gramene; Zm00001eb411380_T001; Zm00001eb411380_P001; Zm00001eb411380. DR MaizeGDB; 13870; -. DR eggNOG; KOG0626; Eukaryota. DR InParanoid; P49235; -. DR OMA; ADICYHN; -. DR OrthoDB; 334393at2759; -. DR BioCyc; MetaCyc:MONOMER-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 Gene3D; 3.20.20.80; Glycosidases; 1. 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:SF326; 4-HYDROXY-7-METHOXY-3-OXO-3,4-DIHYDRO-2H-1,4-BENZOXAZIN-2-YL GLUCOSIDE BETA-D-GLUCOSIDASE 2, CHLOROPLASTIC; 1. DR PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1. DR Pfam; PF00232; Glyco_hydro_1; 1. DR PRINTS; PR00131; GLHYDRLASE1. DR SUPFAM; SSF51445; (Trans)glycosidases; 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="a beta-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22798" FT /evidence="ECO:0000305|PubMed:11106394, FT ECO:0000305|PubMed:12684498, ECO:0007744|PDB:1E56, FT ECO:0007744|PDB:1H49" FT BINDING 196 FT /ligand="a beta-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22798" FT /evidence="ECO:0000305|PubMed:11106394, FT ECO:0007744|PDB:1E56" FT BINDING 244..245 FT /ligand="a beta-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22798" FT /evidence="ECO:0000305|PubMed:11106394, FT ECO:0007744|PDB:1E56" FT BINDING 387 FT /ligand="a beta-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22798" FT /evidence="ECO:0000305|PubMed:11106394, FT ECO:0007744|PDB:1E56" FT BINDING 460 FT /ligand="a beta-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22798" FT /evidence="ECO:0000250|UniProtKB:Q9SPP9" FT BINDING 511 FT /ligand="a beta-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22798" FT /evidence="ECO:0000305|PubMed:11106394, FT ECO:0000305|PubMed:12684498, ECO:0007744|PDB:1E55, FT ECO:0007744|PDB:1E56, ECO:0007744|PDB:1H49" FT BINDING 518..519 FT /ligand="a beta-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22798" FT /evidence="ECO:0000305|PubMed:11106394, FT ECO:0000305|PubMed:12684498, ECO:0007744|PDB:1E55, FT ECO:0007744|PDB:1E56, ECO:0007744|PDB:1H49" FT BINDING 527 FT /ligand="a beta-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22798" FT /evidence="ECO:0000305|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 //