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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}.
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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
 
 
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