BGL07_ORYSJ
ID BGL07_ORYSJ Reviewed; 504 AA.
AC Q75I93; Q10EB0; Q10EB1; Q10EB2; Q42975; Q75I92;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Beta-glucosidase 7 {ECO:0000305};
DE Short=Os3bglu7 {ECO:0000303|PubMed:17196101};
DE EC=3.2.1.21 {ECO:0000269|PubMed:14692878};
DE Flags: Precursor;
GN Name=BGLU7 {ECO:0000305}; Synonyms=BGLU1 {ECO:0000303|PubMed:14692878};
GN OrderedLocusNames=Os03g0703000 {ECO:0000312|EMBL:BAF12927.1},
GN LOC_Os03g49600 {ECO:0000312|EMBL:ABF98423.1}; ORFNames=OSJNBa0004L11.16;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Nipponbare; TISSUE=Root;
RA Esen A., Opassiri R., Ketudat Cairns J.R., Akiyama T.;
RT "Oryza sativa beta-glucosidase mRNA.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16109971; DOI=10.1101/gr.3869505;
RG The rice chromosome 3 sequencing consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=14692878; DOI=10.1042/bj20031485;
RA Opassiri R., Hua Y., Wara-Aswapati O., Akiyama T., Svasti J., Esen A.,
RA Ketudat Cairns J.R.;
RT "Beta-glucosidase, exo-beta-glucanase and pyridoxine transglucosylase
RT activities of rice BGlu1.";
RL Biochem. J. 379:125-131(2004).
RN [8]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=17196101; DOI=10.1186/1471-2229-6-33;
RA Opassiri R., Pomthong B., Onkoksoong T., Akiyama T., Esen A.,
RA Ketudat Cairns J.R.;
RT "Analysis of rice glycosyl hydrolase family 1 and expression of Os4bglu12
RT beta-glucosidase.";
RL BMC Plant Biol. 6:33-33(2006).
RN [9]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=19766588; DOI=10.1016/j.abb.2009.09.004;
RA Kuntothom T., Luang S., Harvey A.J., Fincher G.B., Opassiri R., Hrmova M.,
RA Ketudat Cairns J.R.;
RT "Rice family GH1 glycoside hydrolases with beta-D-glucosidase and beta-D-
RT mannosidase activities.";
RL Arch. Biochem. Biophys. 491:85-95(2009).
RN [10]
RP MUTAGENESIS OF ASN-273.
RX PubMed=22341501; DOI=10.1016/j.carres.2012.01.010;
RA Sansenya S., Maneesan J., Cairns J.R.;
RT "Exchanging a single amino acid residue generates or weakens a +2
RT cellooligosaccharide binding subsite in rice beta-glucosidases.";
RL Carbohydr. Res. 351:130-133(2012).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 29-504 IN COMPLEX WITH SUBSTRATE
RP ANALOG, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND MUTAGENESIS
RP OF ILE-207; ASN-218; ASN-273 AND LEU-470.
RX PubMed=18308333; DOI=10.1016/j.jmb.2008.01.076;
RA Chuenchor W., Pengthaisong S., Robinson R.C., Yuvaniyama J., Oonanant W.,
RA Bevan D.R., Esen A., Chen C.J., Opassiri R., Svasti J., Cairns J.R.;
RT "Structural insights into rice BGlu1 beta-glucosidase oligosaccharide
RT hydrolysis and transglycosylation.";
RL J. Mol. Biol. 377:1200-1215(2008).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.37 ANGSTROMS) OF 29-504 IN COMPLEX WITH SUBSTRATE
RP ANALOG.
RX PubMed=20884352; DOI=10.1016/j.jsb.2010.09.021;
RA Chuenchor W., Pengthaisong S., Robinson R.C., Yuvaniyama J., Svasti J.,
RA Cairns J.R.;
RT "The structural basis of oligosaccharide binding by rice BGlu1 beta-
RT glucosidase.";
RL J. Struct. Biol. 173:169-179(2011).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) OF 29-504 IN COMPLEX WITH SUBSTRATE
RP ANALOG, AND ACTIVE SITE.
RX PubMed=25252199; DOI=10.1002/pro.2556;
RA Pengthaisong S., Ketudat Cairns J.R.;
RT "Effects of active site cleft residues on oligosaccharide binding,
RT hydrolysis, and glycosynthase activities of rice BGlu1 and its mutants.";
RL Protein Sci. 23:1738-1752(2014).
CC -!- FUNCTION: Hydrolyzes p-nitrophenyl beta-D-glucoside, p-nitrophenyl
CC beta-D-mannoside, p-nitrophenyl beta-D-galactoside, p-nitrophenyl beta-
CC D-xyloside, p-nitrophenyl beta-D-fucoside, p-nitrophenyl beta-L-
CC arabinoside, oligosaccharides, pyridoxine beta-D-glucoside and the
CC cyanogenic glucosides amygdalin, prunasin and dhurrin. Possesses
CC pyridoxine transglucosylation activity. {ECO:0000269|PubMed:14692878,
CC ECO:0000269|PubMed:18308333, ECO:0000269|PubMed:19766588}.
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:14692878};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.2 mM for p-nitrophenyl beta-D-glucoside (at pH 5.0)
CC {ECO:0000269|PubMed:14692878, ECO:0000269|PubMed:18308333,
CC ECO:0000269|PubMed:19766588};
CC KM=0.23 mM for p-nitrophenyl beta-D-fucoside (at pH 5.0)
CC {ECO:0000269|PubMed:14692878, ECO:0000269|PubMed:18308333,
CC ECO:0000269|PubMed:19766588};
CC KM=3.2 mM for p-nitrophenyl beta-D-galactoside (at pH 5.0)
CC {ECO:0000269|PubMed:14692878, ECO:0000269|PubMed:18308333,
CC ECO:0000269|PubMed:19766588};
CC KM=1.3 mM for p-nitrophenyl beta-D-mannoside (at pH 5.0)
CC {ECO:0000269|PubMed:14692878, ECO:0000269|PubMed:18308333,
CC ECO:0000269|PubMed:19766588};
CC KM=1.3 mM for p-nitrophenyl beta-D-xyloside (at pH 5.0)
CC {ECO:0000269|PubMed:14692878, ECO:0000269|PubMed:18308333,
CC ECO:0000269|PubMed:19766588};
CC KM=1.2 mM for p-nitrophenyl beta-L-arabinoside (at pH 5.0)
CC {ECO:0000269|PubMed:14692878, ECO:0000269|PubMed:18308333,
CC ECO:0000269|PubMed:19766588};
CC KM=0.78 mM for p-nitrophenyl beta-D-cellobioside (at pH 5.0)
CC {ECO:0000269|PubMed:14692878, ECO:0000269|PubMed:18308333,
CC ECO:0000269|PubMed:19766588};
CC KM=22 mM for cellobiose (at pH 5.0) {ECO:0000269|PubMed:14692878,
CC ECO:0000269|PubMed:18308333, ECO:0000269|PubMed:19766588};
CC KM=0.22 mM for cellotriose (at pH 5.0) {ECO:0000269|PubMed:14692878,
CC ECO:0000269|PubMed:18308333, ECO:0000269|PubMed:19766588};
CC KM=0.28 mM for cellotetraose (at pH 5.0)
CC {ECO:0000269|PubMed:14692878, ECO:0000269|PubMed:18308333,
CC ECO:0000269|PubMed:19766588};
CC KM=0.24 mM for cellopentaose (at pH 5.0)
CC {ECO:0000269|PubMed:14692878, ECO:0000269|PubMed:18308333,
CC ECO:0000269|PubMed:19766588};
CC KM=0.22 mM for cellohexaose (at pH 5.0) {ECO:0000269|PubMed:14692878,
CC ECO:0000269|PubMed:18308333, ECO:0000269|PubMed:19766588};
CC KM=2.05 mM for laminaribiose (at pH 5.0)
CC {ECO:0000269|PubMed:14692878, ECO:0000269|PubMed:18308333,
CC ECO:0000269|PubMed:19766588};
CC KM=1.92 mM for laminaritriose (at pH 5.0)
CC {ECO:0000269|PubMed:14692878, ECO:0000269|PubMed:18308333,
CC ECO:0000269|PubMed:19766588};
CC KM=13.9 mM for sophorose (at pH 5.0) {ECO:0000269|PubMed:14692878,
CC ECO:0000269|PubMed:18308333, ECO:0000269|PubMed:19766588};
CC KM=38.3 mM for gentiobiose (at pH 5.0) {ECO:0000269|PubMed:14692878,
CC ECO:0000269|PubMed:18308333, ECO:0000269|PubMed:19766588};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18308333}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAS07255.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=ABF98424.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=ABF98425.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=ABF98426.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U28047; AAA84906.3; -; mRNA.
DR EMBL; AC091670; AAX95519.1; -; Genomic_DNA.
DR EMBL; AC133334; AAS07254.1; -; Genomic_DNA.
DR EMBL; AC133334; AAS07255.1; ALT_SEQ; Genomic_DNA.
DR EMBL; DP000009; ABF98423.1; -; Genomic_DNA.
DR EMBL; DP000009; ABF98424.1; ALT_SEQ; Genomic_DNA.
DR EMBL; DP000009; ABF98425.1; ALT_SEQ; Genomic_DNA.
DR EMBL; DP000009; ABF98426.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008209; BAF12927.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS85953.1; -; Genomic_DNA.
DR EMBL; AK100165; BAG94472.1; -; mRNA.
DR PIR; T03296; T03296.
DR RefSeq; XP_015630897.1; XM_015775411.1.
DR PDB; 2RGL; X-ray; 2.20 A; A/B=29-504.
DR PDB; 2RGM; X-ray; 1.55 A; A/B=29-504.
DR PDB; 3AHT; X-ray; 2.80 A; A/B=29-504.
DR PDB; 3AHV; X-ray; 1.75 A; A/B=29-504.
DR PDB; 3F4V; X-ray; 1.65 A; A/B=29-504.
DR PDB; 3F5J; X-ray; 1.95 A; A/B=29-504.
DR PDB; 3F5K; X-ray; 1.80 A; A/B=29-504.
DR PDB; 3F5L; X-ray; 1.37 A; A/B=29-504.
DR PDB; 3SCN; X-ray; 2.20 A; A/B=29-504.
DR PDB; 3SCO; X-ray; 1.95 A; A/B=29-504.
DR PDB; 3SCP; X-ray; 2.10 A; A/B=29-504.
DR PDB; 3SCQ; X-ray; 2.10 A; A/B=29-504.
DR PDB; 3SCR; X-ray; 1.80 A; A/B=29-504.
DR PDB; 3SCS; X-ray; 1.85 A; A/B=29-504.
DR PDB; 3SCT; X-ray; 1.60 A; A/B=29-504.
DR PDB; 3SCU; X-ray; 1.58 A; A/B=29-504.
DR PDB; 3SCV; X-ray; 2.11 A; A/B=29-504.
DR PDB; 3SCW; X-ray; 1.90 A; A/B=29-504.
DR PDB; 4QLJ; X-ray; 1.95 A; A/B=29-504.
DR PDB; 4QLK; X-ray; 1.83 A; A/B=29-504.
DR PDB; 4QLL; X-ray; 1.85 A; A/B=29-504.
DR PDB; 7BZM; X-ray; 2.30 A; A/B=29-504.
DR PDBsum; 2RGL; -.
DR PDBsum; 2RGM; -.
DR PDBsum; 3AHT; -.
DR PDBsum; 3AHV; -.
DR PDBsum; 3F4V; -.
DR PDBsum; 3F5J; -.
DR PDBsum; 3F5K; -.
DR PDBsum; 3F5L; -.
DR PDBsum; 3SCN; -.
DR PDBsum; 3SCO; -.
DR PDBsum; 3SCP; -.
DR PDBsum; 3SCQ; -.
DR PDBsum; 3SCR; -.
DR PDBsum; 3SCS; -.
DR PDBsum; 3SCT; -.
DR PDBsum; 3SCU; -.
DR PDBsum; 3SCV; -.
DR PDBsum; 3SCW; -.
DR PDBsum; 4QLJ; -.
DR PDBsum; 4QLK; -.
DR PDBsum; 4QLL; -.
DR PDBsum; 7BZM; -.
DR AlphaFoldDB; Q75I93; -.
DR SMR; Q75I93; -.
DR BioGRID; 802878; 1.
DR STRING; 4530.OS03T0703000-01; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR PaxDb; Q75I93; -.
DR PRIDE; Q75I93; -.
DR EnsemblPlants; Os03t0703000-01; Os03t0703000-01; Os03g0703000.
DR GeneID; 4333841; -.
DR Gramene; Os03t0703000-01; Os03t0703000-01; Os03g0703000.
DR KEGG; osa:4333841; -.
DR eggNOG; KOG0626; Eukaryota.
DR HOGENOM; CLU_001859_1_0_1; -.
DR InParanoid; Q75I93; -.
DR OMA; PWCASIL; -.
DR OrthoDB; 408001at2759; -.
DR BRENDA; 3.2.1.21; 4460.
DR PlantReactome; R-OSA-1119284; Coumarin biosynthesis (via 2-coumarate).
DR SABIO-RK; Q75I93; -.
DR EvolutionaryTrace; Q75I93; -.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR ExpressionAtlas; Q75I93; baseline and differential.
DR Genevisible; Q75I93; OS.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0047668; F:amygdalin beta-glucosidase activity; IDA:UniProtKB.
DR GO; GO:0033907; F:beta-D-fucosidase activity; IDA:UniProtKB.
DR GO; GO:0004565; F:beta-galactosidase activity; IDA:UniProtKB.
DR GO; GO:0080083; F:beta-gentiobiose beta-glucosidase activity; IDA:UniProtKB.
DR GO; GO:0008422; F:beta-glucosidase activity; IDA:UniProtKB.
DR GO; GO:0047701; F:beta-L-arabinosidase activity; IDA:UniProtKB.
DR GO; GO:0004567; F:beta-mannosidase activity; IDA:UniProtKB.
DR GO; GO:0080079; F:cellobiose glucosidase activity; IDA:UniProtKB.
DR GO; GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0050224; F:prunasin beta-glucosidase activity; IDA:UniProtKB.
DR GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR InterPro; IPR001360; Glyco_hydro_1.
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.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Glycosidase; Hydrolase;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..504
FT /note="Beta-glucosidase 7"
FT /id="PRO_0000383461"
FT ACT_SITE 204
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:25252199"
FT ACT_SITE 414
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:25252199"
FT BINDING 57
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:18308333,
FT ECO:0000269|PubMed:20884352, ECO:0000269|PubMed:25252199,
FT ECO:0007744|PDB:2RGM, ECO:0007744|PDB:3AHT,
FT ECO:0007744|PDB:3F5J, ECO:0007744|PDB:3F5K,
FT ECO:0007744|PDB:3F5L, ECO:0007744|PDB:4QLK"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20884352,
FT ECO:0000269|PubMed:25252199, ECO:0007744|PDB:3AHT,
FT ECO:0007744|PDB:3F5J, ECO:0007744|PDB:3F5K,
FT ECO:0007744|PDB:3F5L, ECO:0007744|PDB:4QLK"
FT BINDING 203
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:18308333,
FT ECO:0000269|PubMed:20884352, ECO:0000269|PubMed:25252199,
FT ECO:0007744|PDB:2RGM, ECO:0007744|PDB:3F5K,
FT ECO:0007744|PDB:3F5L, ECO:0007744|PDB:4QLK"
FT BINDING 343
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:18308333,
FT ECO:0000269|PubMed:20884352, ECO:0000269|PubMed:25252199,
FT ECO:0007744|PDB:2RGM, ECO:0007744|PDB:3AHT,
FT ECO:0007744|PDB:3F5K, ECO:0007744|PDB:3F5L,
FT ECO:0007744|PDB:4QLK"
FT BINDING 461
FT /ligand="substrate"
FT /evidence="ECO:0000305, ECO:0007744|PDB:3SCW"
FT BINDING 468..469
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:18308333,
FT ECO:0000269|PubMed:20884352, ECO:0000269|PubMed:25252199,
FT ECO:0007744|PDB:2RGM, ECO:0007744|PDB:3AHT,
FT ECO:0007744|PDB:3F5J, ECO:0007744|PDB:3F5K,
FT ECO:0007744|PDB:3F5L, ECO:0007744|PDB:4QLK"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 223..226
FT /evidence="ECO:0000250"
FT MUTAGEN 207
FT /note="I->V: Increases KM for substrate about 5-fold.
FT Increases kcat/Km values 9 to 24-fold depending on the
FT substrate."
FT /evidence="ECO:0000269|PubMed:18308333,
FT ECO:0000269|PubMed:22341501"
FT MUTAGEN 218
FT /note="N->H: Decreases KM for substrate about 2-fold."
FT /evidence="ECO:0000269|PubMed:18308333"
FT MUTAGEN 273
FT /note="N->V: Increases KM for substrate about 5-fold."
FT /evidence="ECO:0000269|PubMed:18308333"
FT MUTAGEN 470
FT /note="L->R: No effect on KM."
FT /evidence="ECO:0000269|PubMed:18308333"
FT CONFLICT 52
FT /note="A -> V (in Ref. 1; AAA84906)"
FT /evidence="ECO:0000305"
FT TURN 34..37
FT /evidence="ECO:0007829|PDB:3F5L"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:3F5L"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:3F5L"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:3F5L"
FT HELIX 71..76
FT /evidence="ECO:0007829|PDB:3F5L"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:3F5L"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:3F5L"
FT HELIX 94..107
FT /evidence="ECO:0007829|PDB:3F5L"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:3F5L"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:3F5L"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:3F5L"
FT HELIX 132..147
FT /evidence="ECO:0007829|PDB:3F5L"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:3F5L"
FT HELIX 163..169
FT /evidence="ECO:0007829|PDB:3F5L"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:3F5L"
FT HELIX 177..192
FT /evidence="ECO:0007829|PDB:3F5L"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:3F5L"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:3F5L"
FT HELIX 205..213
FT /evidence="ECO:0007829|PDB:3F5L"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:4QLL"
FT TURN 232..234
FT /evidence="ECO:0007829|PDB:3F5L"
FT HELIX 235..257
FT /evidence="ECO:0007829|PDB:3F5L"
FT HELIX 259..262
FT /evidence="ECO:0007829|PDB:3F5L"
FT STRAND 265..271
FT /evidence="ECO:0007829|PDB:3F5L"
FT STRAND 274..281
FT /evidence="ECO:0007829|PDB:3F5L"
FT HELIX 282..295
FT /evidence="ECO:0007829|PDB:3F5L"
FT HELIX 297..305
FT /evidence="ECO:0007829|PDB:3F5L"
FT HELIX 310..316
FT /evidence="ECO:0007829|PDB:3F5L"
FT HELIX 317..319
FT /evidence="ECO:0007829|PDB:3F5L"
FT HELIX 325..331
FT /evidence="ECO:0007829|PDB:3F5L"
FT STRAND 336..341
FT /evidence="ECO:0007829|PDB:3F5L"
FT STRAND 345..349
FT /evidence="ECO:0007829|PDB:3F5L"
FT HELIX 361..364
FT /evidence="ECO:0007829|PDB:3F5L"
FT STRAND 368..373
FT /evidence="ECO:0007829|PDB:3F5L"
FT STRAND 376..379
FT /evidence="ECO:0007829|PDB:3F5L"
FT HELIX 392..404
FT /evidence="ECO:0007829|PDB:3F5L"
FT STRAND 410..414
FT /evidence="ECO:0007829|PDB:3F5L"
FT STRAND 419..422
FT /evidence="ECO:0007829|PDB:3F5L"
FT HELIX 425..429
FT /evidence="ECO:0007829|PDB:3F5L"
FT HELIX 432..450
FT /evidence="ECO:0007829|PDB:3F5L"
FT STRAND 455..461
FT /evidence="ECO:0007829|PDB:3F5L"
FT HELIX 469..474
FT /evidence="ECO:0007829|PDB:3F5L"
FT STRAND 479..482
FT /evidence="ECO:0007829|PDB:3F5L"
FT TURN 484..486
FT /evidence="ECO:0007829|PDB:3F5L"
FT STRAND 489..491
FT /evidence="ECO:0007829|PDB:3F5L"
FT HELIX 493..501
FT /evidence="ECO:0007829|PDB:3F5L"
SQ SEQUENCE 504 AA; 56872 MW; 4C36D2A5AF452CE9 CRC64;
MAARRANCAL VLVLALALLA ARDAGAAAVP KPNWLGGLSR AAFPKRFVFG TATSAYQVEG
MAASGGRGPS IWDAFAHTPG NVAGNQNGDV ATDQYHRYKE DVNLMKSLNF DAYRFSISWS
RIFPDGEGRV NQEGVAYYNN LINYLLQKGI TPYVNLYHYD LPLALEKKYG GWLNAKMADL
FTEYADFCFK TFGNRVKHWF TFNEPRIVAL LGYDQGTNPP KRCTKCAAGG NSATEPYIVA
HNFLLSHAAA VARYRTKYQA AQQGKVGIVL DFNWYEALSN STEDQAAAQR ARDFHIGWYL
DPLINGHYPQ IMQDLVKDRL PKFTPEQARL VKGSADYIGI NQYTASYMKG QQLMQQTPTS
YSADWQVTYV FAKNGKPIGP QANSNWLYIV PWGMYGCVNY IKQKYGNPTV VITENGMDQP
ANLSRDQYLR DTTRVHFYRS YLTQLKKAID EGANVAGYFA WSLLDNFEWL SGYTSKFGIV
YVDFNTLERH PKASAYWFRD MLKH
