U76G1_STERE
ID U76G1_STERE Reviewed; 458 AA.
AC Q6VAB4;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=UDP-glycosyltransferase 76G1 {ECO:0000303|PubMed:15610349};
DE EC=2.4.1.- {ECO:0000269|PubMed:15610349, ECO:0000269|PubMed:31182573, ECO:0000269|PubMed:31324778};
GN Name=UGT76G1 {ECO:0000303|PubMed:15610349};
OS Stevia rebaudiana (Stevia) (Eupatorium rebaudianum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC Heliantheae alliance; Eupatorieae; Stevia.
OX NCBI_TaxID=55670;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Leaf;
RX PubMed=15610349; DOI=10.1111/j.1365-313x.2004.02275.x;
RA Richman A., Swanson A., Humphrey T., Chapman R., McGarvey B., Pocs R.,
RA Brandle J.;
RT "Functional genomics uncovers three glucosyltransferases involved in the
RT synthesis of the major sweet glucosides of Stevia rebaudiana.";
RL Plant J. 41:56-67(2005).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=27378621; DOI=10.1016/j.jbiotec.2016.06.034;
RA Dewitte G., Walmagh M., Diricks M., Lepak A., Gutmann A., Nidetzky B.,
RA Desmet T.;
RT "Screening of recombinant glycosyltransferases reveals the broad acceptor
RT specificity of stevia UGT-76G1.";
RL J. Biotechnol. 233:49-55(2016).
RN [3]
RP INDUCTION.
RX PubMed=28215607; DOI=10.1016/j.phytochem.2017.02.002;
RA Yoneda Y., Nakashima H., Miyasaka J., Ohdoi K., Shimizu H.;
RT "Impact of blue, red, and far-red light treatments on gene expression and
RT steviol glycoside accumulation in Stevia rebaudiana.";
RL Phytochemistry 137:57-65(2017).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOTECHNOLOGY.
RX PubMed=30569490; DOI=10.1111/pbi.13035;
RA Kim M.J., Zheng J., Liao M.H., Jang I.C.;
RT "Overexpression of SrUGT76G1 in Stevia alters major steviol glycosides
RT composition towards improved quality.";
RL Plant Biotechnol. J. 17:1037-1047(2019).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.69 ANGSTROMS) IN COMPLEX WITH UDP-GLUCOSE;
RP RUBUSOSIDE AND REBAUDIOSIDE A, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE, SUBUNIT, AND MUTAGENESIS OF
RP HIS-25.
RX PubMed=31324778; DOI=10.1038/s41467-019-11154-4;
RA Yang T., Zhang J., Ke D., Yang W., Tang M., Jiang J., Cheng G., Li J.,
RA Cheng W., Wei Y., Li Q., Naismith J.H., Zhu X.;
RT "Hydrophobic recognition allows the glycosyltransferase UGT76G1 to catalyze
RT its substrate in two orientations.";
RL Nat. Commun. 10:3214-3214(2019).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH UDP-GLUCOSE,
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE,
RP SUBUNIT, AND MUTAGENESIS OF HIS-25; LEU-126; MET-145; THR-146; SER-147;
RP ASN-151; HIS-155; LEU-200; LEU-204; MET-207 AND LEU-379.
RX PubMed=31182573; DOI=10.1073/pnas.1902104116;
RA Lee S.G., Salomon E., Yu O., Jez J.M.;
RT "Molecular basis for branched steviol glucoside biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 116:13131-13136(2019).
CC -!- FUNCTION: Involved in the biosynthesis of steviol glycosides in leaves
CC (PubMed:15610349, PubMed:30569490, PubMed:31324778, PubMed:31182573).
CC Converts the di-glycoside steviolbioside to the tri-glycoside
CC rebaudioside B (PubMed:15610349, PubMed:31324778). Converts the tri-
CC glycoside stevioside to the tetra-glycoside rebaudioside A
CC (PubMed:15610349, PubMed:27378621, PubMed:30569490, PubMed:31324778,
CC PubMed:31182573). Converts the tetra-glycoside rebaudioside E to the
CC penta-glycoside rebaudioside D (PubMed:31324778). Converts the penta-
CC glycoside rebaudioside D to the hexa-glycoside rebaudioside M
CC (PubMed:31324778). Can glucosylate rubusoside and rebaudioside A in
CC vitro (PubMed:31324778). {ECO:0000269|PubMed:15610349,
CC ECO:0000269|PubMed:27378621, ECO:0000269|PubMed:30569490,
CC ECO:0000269|PubMed:31182573, ECO:0000269|PubMed:31324778}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=steviolbioside + UDP-alpha-D-glucose = H(+) + rebaudioside B +
CC UDP; Xref=Rhea:RHEA:61752, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:58885, ChEBI:CHEBI:145009, ChEBI:CHEBI:145013;
CC Evidence={ECO:0000269|PubMed:15610349, ECO:0000269|PubMed:31324778};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61753;
CC Evidence={ECO:0000269|PubMed:15610349};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=stevioside + UDP-alpha-D-glucose = H(+) + rebaudioside A +
CC UDP; Xref=Rhea:RHEA:61756, ChEBI:CHEBI:9271, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:145012;
CC Evidence={ECO:0000269|PubMed:15610349, ECO:0000269|PubMed:27378621,
CC ECO:0000269|PubMed:30569490, ECO:0000269|PubMed:31182573,
CC ECO:0000269|PubMed:31324778};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61757;
CC Evidence={ECO:0000269|PubMed:15610349};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=rebaudioside E + UDP-alpha-D-glucose = H(+) + rebaudioside D +
CC UDP; Xref=Rhea:RHEA:61772, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:58885, ChEBI:CHEBI:145018, ChEBI:CHEBI:145022;
CC Evidence={ECO:0000269|PubMed:31324778};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61773;
CC Evidence={ECO:0000269|PubMed:31324778};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=rebaudioside D + UDP-alpha-D-glucose = H(+) + rebaudioside M +
CC UDP; Xref=Rhea:RHEA:61776, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:58885, ChEBI:CHEBI:145019, ChEBI:CHEBI:145022;
CC Evidence={ECO:0000269|PubMed:31324778};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61777;
CC Evidence={ECO:0000269|PubMed:31324778};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.6 uM for UDP-glucose {ECO:0000269|PubMed:31324778};
CC KM=440 uM for UDP-glucose {ECO:0000269|PubMed:27378621};
CC KM=4.5 uM for steviolbioside {ECO:0000269|PubMed:31324778};
CC KM=103.2 uM for steviolbioside {ECO:0000269|PubMed:15610349};
CC KM=25.5 uM for stevioside {ECO:0000269|PubMed:31324778};
CC KM=230 uM for stevioside {ECO:0000269|PubMed:27378621};
CC KM=291.7 uM for stevioside {ECO:0000269|PubMed:15610349};
CC KM=360 uM for stevioside {ECO:0000269|PubMed:31182573};
CC KM=9.2 uM for rebaudioside E {ECO:0000269|PubMed:31324778};
CC KM=54.4 uM for rubusoside {ECO:0000269|PubMed:31324778};
CC KM=94.2 uM for rebaudioside D {ECO:0000269|PubMed:31324778};
CC KM=243.4 uM for rebaudioside A {ECO:0000269|PubMed:31324778};
CC Vmax=11.1 umol/min/mg enzyme toward UDP-glucose
CC {ECO:0000269|PubMed:27378621};
CC Vmax=9.3 umol/min/mg enzyme toward stevioside
CC {ECO:0000269|PubMed:27378621};
CC Note=kcat is 4.1 min(-1) with UDP-glucose as substrate
CC (PubMed:31324778). kcat is 32.5 min(-1) with UDP-glucose as substrate
CC (PubMed:31182573). kcat is 4.8 min(-1) with steviolbioside as
CC substrate (PubMed:31324778). kcat is 21.3 min(-1) with stevioside as
CC substrate (PubMed:31324778). kcat is 33.8 min(-1) with stevioside as
CC substrate (PubMed:31182573). kcat is 41.8 min(-1) with rebaudioside E
CC as substrate (PubMed:31324778). kcat is 5.9 min(-1) with rubusoside
CC as substrate (PubMed:31324778). kcat is 3.3 min(-1) with rebaudioside
CC D as substrate (PubMed:31324778). kcat is 0.12 min(-1) with
CC rebaudioside A as substrate (PubMed:31324778).
CC {ECO:0000269|PubMed:31182573, ECO:0000269|PubMed:31324778};
CC pH dependence:
CC Optimum pH is 7.0-8.5 with stevioside as substrate (at 40 degrees
CC Celsius). {ECO:0000269|PubMed:27378621};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius with stevioside as
CC substrate (at pH 7.0). {ECO:0000269|PubMed:27378621};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:31182573,
CC ECO:0000269|PubMed:31324778}.
CC -!- INDUCTION: Induced by blue light and red:far-red light in a ratio of
CC 1.22. {ECO:0000269|PubMed:28215607}.
CC -!- BIOTECHNOLOGY: Overexpression of UGT76G1 in Stevia leaves increases the
CC rebaudioside A/stevioside ratio more than 5-fold without compromising
CC plant development or changes in total steviol glycoside content
CC (PubMed:30569490). Rebaudioside A has the advantage to be sweeter and
CC have less bitter aftertaste than stevioside (PubMed:30569490).
CC {ECO:0000269|PubMed:30569490}.
CC -!- MISCELLANEOUS: Leaves of the 'sweet herb' Stevia rebaudiana contain a
CC mix of steviol glycosides, compounds that are unique in the plant world
CC because of their intense sweetness and high concentration in leaf
CC tissue (Probable). Stevia leaves have been used as natural sweeteners
CC in South America for centuries (Probable). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {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; AY345974; AAR06912.1; -; mRNA.
DR PDB; 6INF; X-ray; 1.69 A; A=1-458.
DR PDB; 6ING; X-ray; 1.70 A; A=1-458.
DR PDB; 6INH; X-ray; 2.10 A; A=1-458.
DR PDB; 6INI; X-ray; 1.70 A; A=1-458.
DR PDB; 6KVI; X-ray; 2.60 A; A=1-458.
DR PDB; 6KVJ; X-ray; 2.50 A; A=1-458.
DR PDB; 6KVK; X-ray; 2.40 A; A=1-458.
DR PDB; 6KVL; X-ray; 2.00 A; A=1-458.
DR PDB; 6O86; X-ray; 1.80 A; A=1-458.
DR PDB; 6O87; X-ray; 1.75 A; A=1-458.
DR PDB; 6O88; X-ray; 1.99 A; A=1-458.
DR PDBsum; 6INF; -.
DR PDBsum; 6ING; -.
DR PDBsum; 6INH; -.
DR PDBsum; 6INI; -.
DR PDBsum; 6KVI; -.
DR PDBsum; 6KVJ; -.
DR PDBsum; 6KVK; -.
DR PDBsum; 6KVL; -.
DR PDBsum; 6O86; -.
DR PDBsum; 6O87; -.
DR PDBsum; 6O88; -.
DR AlphaFoldDB; Q6VAB4; -.
DR SMR; Q6VAB4; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR PRIDE; Q6VAB4; -.
DR BioCyc; MetaCyc:MON-17485; -.
DR GO; GO:0035251; F:UDP-glucosyltransferase activity; IDA:UniProtKB.
DR CDD; cd03784; GT1_Gtf-like; 1.
DR InterPro; IPR002213; UDP_glucos_trans.
DR Pfam; PF00201; UDPGT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Transferase.
FT CHAIN 1..458
FT /note="UDP-glycosyltransferase 76G1"
FT /id="PRO_0000434465"
FT ACT_SITE 25
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:31182573,
FT ECO:0000269|PubMed:31324778"
FT ACT_SITE 124
FT /note="Charge relay"
FT /evidence="ECO:0000269|PubMed:31182573,
FT ECO:0000269|PubMed:31324778"
FT BINDING 25
FT /ligand="rebaudioside A"
FT /ligand_id="ChEBI:CHEBI:145012"
FT /evidence="ECO:0000269|PubMed:31324778,
FT ECO:0007744|PDB:6INI"
FT BINDING 25
FT /ligand="rubusoside"
FT /ligand_id="ChEBI:CHEBI:145021"
FT /evidence="ECO:0000269|PubMed:31324778,
FT ECO:0007744|PDB:6INH"
FT BINDING 27
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000269|PubMed:31182573,
FT ECO:0000269|PubMed:31324778, ECO:0007744|PDB:6INF,
FT ECO:0007744|PDB:6O86"
FT BINDING 146..147
FT /ligand="rebaudioside A"
FT /ligand_id="ChEBI:CHEBI:145012"
FT /evidence="ECO:0000269|PubMed:31182573,
FT ECO:0000269|PubMed:31324778, ECO:0007744|PDB:6INI,
FT ECO:0007744|PDB:6O88"
FT BINDING 155
FT /ligand="rebaudioside A"
FT /ligand_id="ChEBI:CHEBI:145012"
FT /evidence="ECO:0000269|PubMed:31182573,
FT ECO:0000269|PubMed:31324778, ECO:0007744|PDB:6INI,
FT ECO:0007744|PDB:6O88"
FT BINDING 283
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000269|PubMed:31182573,
FT ECO:0000269|PubMed:31324778, ECO:0007744|PDB:6INF,
FT ECO:0007744|PDB:6O86"
FT BINDING 338..339
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000269|PubMed:31182573,
FT ECO:0000269|PubMed:31324778, ECO:0007744|PDB:6INF,
FT ECO:0007744|PDB:6O86"
FT BINDING 356..364
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000269|PubMed:31182573,
FT ECO:0000269|PubMed:31324778, ECO:0007744|PDB:6INF,
FT ECO:0007744|PDB:6O86"
FT BINDING 359
FT /ligand="rebaudioside A"
FT /ligand_id="ChEBI:CHEBI:145012"
FT /evidence="ECO:0000269|PubMed:31182573,
FT ECO:0000269|PubMed:31324778, ECO:0007744|PDB:6INI,
FT ECO:0007744|PDB:6O88"
FT BINDING 380..381
FT /ligand="rebaudioside A"
FT /ligand_id="ChEBI:CHEBI:145012"
FT /evidence="ECO:0000269|PubMed:31182573,
FT ECO:0000269|PubMed:31324778, ECO:0007744|PDB:6INI,
FT ECO:0007744|PDB:6KVL, ECO:0007744|PDB:6O88"
FT MUTAGEN 25
FT /note="H->A,N: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:31182573,
FT ECO:0000269|PubMed:31324778"
FT MUTAGEN 126
FT /note="L->I: Reduces catalytic efficiency 780-fold for
FT stevioside."
FT /evidence="ECO:0000269|PubMed:31182573"
FT MUTAGEN 145
FT /note="M->F: Reduces catalytic efficiency 19-fold for
FT stevioside."
FT /evidence="ECO:0000269|PubMed:31182573"
FT MUTAGEN 145
FT /note="M->W: Reduces catalytic efficiency 780-fold for
FT stevioside."
FT /evidence="ECO:0000269|PubMed:31182573"
FT MUTAGEN 146
FT /note="T->A: Reduces catalytic efficiency 78-fold for
FT stevioside."
FT /evidence="ECO:0000269|PubMed:31182573"
FT MUTAGEN 147
FT /note="S->A: Reduces catalytic efficiency 173-fold for
FT stevioside."
FT /evidence="ECO:0000269|PubMed:31182573"
FT MUTAGEN 147
FT /note="S->N: Reduces catalytic efficiency 142-fold for
FT stevioside."
FT /evidence="ECO:0000269|PubMed:31182573"
FT MUTAGEN 147
FT /note="S->T: Reduces catalytic efficiency 142-fold for
FT stevioside."
FT /evidence="ECO:0000269|PubMed:31182573"
FT MUTAGEN 151
FT /note="N->A: Reduces catalytic efficiency 16-fold for
FT stevioside."
FT /evidence="ECO:0000269|PubMed:31182573"
FT MUTAGEN 151
FT /note="N->Q: Reduces catalytic efficiency 4-fold for
FT stevioside."
FT /evidence="ECO:0000269|PubMed:31182573"
FT MUTAGEN 155
FT /note="H->A: Reduces catalytic efficiency 3.5-fold for
FT stevioside."
FT /evidence="ECO:0000269|PubMed:31182573"
FT MUTAGEN 155
FT /note="H->R: Reduces catalytic efficiency 29-fold for
FT stevioside."
FT /evidence="ECO:0000269|PubMed:31182573"
FT MUTAGEN 155
FT /note="H->W: Reduces catalytic efficiency 25-fold for
FT stevioside."
FT /evidence="ECO:0000269|PubMed:31182573"
FT MUTAGEN 200
FT /note="L->I: Reduces catalytic efficiency 4-fold for
FT stevioside."
FT /evidence="ECO:0000269|PubMed:31182573"
FT MUTAGEN 204
FT /note="L->I: Reduces catalytic efficiency 2.6-fold for
FT stevioside."
FT /evidence="ECO:0000269|PubMed:31182573"
FT MUTAGEN 207
FT /note="M->F: Reduces catalytic efficiency 3.6-fold for
FT stevioside."
FT /evidence="ECO:0000269|PubMed:31182573"
FT MUTAGEN 207
FT /note="M->W: Reduces catalytic efficiency 13-fold for
FT stevioside."
FT /evidence="ECO:0000269|PubMed:31182573"
FT MUTAGEN 379
FT /note="L->I: Reduces catalytic efficiency 2.5-fold for
FT stevioside."
FT /evidence="ECO:0000269|PubMed:31182573"
FT STRAND 13..18
FT /evidence="ECO:0007829|PDB:6INF"
FT HELIX 23..38
FT /evidence="ECO:0007829|PDB:6INF"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:6INF"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:6INF"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:6INF"
FT TURN 74..78
FT /evidence="ECO:0007829|PDB:6INF"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:6INF"
FT HELIX 85..88
FT /evidence="ECO:0007829|PDB:6INF"
FT HELIX 89..96
FT /evidence="ECO:0007829|PDB:6INF"
FT HELIX 98..110
FT /evidence="ECO:0007829|PDB:6INF"
FT STRAND 117..124
FT /evidence="ECO:0007829|PDB:6INF"
FT HELIX 130..136
FT /evidence="ECO:0007829|PDB:6INF"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:6INF"
FT HELIX 149..156
FT /evidence="ECO:0007829|PDB:6INF"
FT HELIX 158..163
FT /evidence="ECO:0007829|PDB:6INF"
FT TURN 164..167
FT /evidence="ECO:0007829|PDB:6INI"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:6KVK"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:6INF"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:6INF"
FT HELIX 187..193
FT /evidence="ECO:0007829|PDB:6INF"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:6INF"
FT HELIX 197..212
FT /evidence="ECO:0007829|PDB:6INF"
FT STRAND 217..221
FT /evidence="ECO:0007829|PDB:6INF"
FT TURN 223..225
FT /evidence="ECO:0007829|PDB:6INF"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:6INF"
FT HELIX 230..236
FT /evidence="ECO:0007829|PDB:6INF"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:6INF"
FT HELIX 246..249
FT /evidence="ECO:0007829|PDB:6INF"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:6INF"
FT HELIX 263..268
FT /evidence="ECO:0007829|PDB:6INF"
FT STRAND 276..280
FT /evidence="ECO:0007829|PDB:6INF"
FT TURN 282..284
FT /evidence="ECO:0007829|PDB:6O87"
FT HELIX 289..302
FT /evidence="ECO:0007829|PDB:6INF"
FT STRAND 305..309
FT /evidence="ECO:0007829|PDB:6INF"
FT STRAND 314..317
FT /evidence="ECO:0007829|PDB:6KVK"
FT STRAND 318..321
FT /evidence="ECO:0007829|PDB:6INF"
FT TURN 326..332
FT /evidence="ECO:0007829|PDB:6ING"
FT STRAND 333..337
FT /evidence="ECO:0007829|PDB:6INF"
FT HELIX 341..345
FT /evidence="ECO:0007829|PDB:6INF"
FT STRAND 350..355
FT /evidence="ECO:0007829|PDB:6INF"
FT HELIX 359..368
FT /evidence="ECO:0007829|PDB:6INF"
FT STRAND 372..374
FT /evidence="ECO:0007829|PDB:6INF"
FT HELIX 381..390
FT /evidence="ECO:0007829|PDB:6INF"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:6INF"
FT HELIX 404..415
FT /evidence="ECO:0007829|PDB:6INF"
FT HELIX 418..420
FT /evidence="ECO:0007829|PDB:6INF"
FT HELIX 421..438
FT /evidence="ECO:0007829|PDB:6INF"
FT HELIX 443..457
FT /evidence="ECO:0007829|PDB:6INF"
SQ SEQUENCE 458 AA; 52029 MW; 3EDC979553F143F3 CRC64;
MENKTETTVR RRRRIILFPV PFQGHINPIL QLANVLYSKG FSITIFHTNF NKPKTSNYPH
FTFRFILDND PQDERISNLP THGPLAGMRI PIINEHGADE LRRELELLML ASEEDEEVSC
LITDALWYFA QSVADSLNLR RLVLMTSSLF NFHAHVSLPQ FDELGYLDPD DKTRLEEQAS
GFPMLKVKDI KSAYSNWQIL KEILGKMIKQ TKASSGVIWN SFKELEESEL ETVIREIPAP
SFLIPLPKHL TASSSSLLDH DRTVFQWLDQ QPPSSVLYVS FGSTSEVDEK DFLEIARGLV
DSKQSFLWVV RPGFVKGSTW VEPLPDGFLG ERGRIVKWVP QQEVLAHGAI GAFWTHSGWN
STLESVCEGV PMIFSDFGLD QPLNARYMSD VLKVGVYLEN GWERGEIANA IRRVMVDEEG
EYIRQNARVL KQKADVSLMK GGSSYESLES LVSYISSL