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BX9_MAIZE
ID   BX9_MAIZE               Reviewed;         462 AA.
AC   B4G072; Q8W2B6;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=DIMBOA UDP-glucosyltransferase BX9;
DE            EC=2.4.1.202 {ECO:0000269|PubMed:11851909, ECO:0000269|PubMed:16666853};
DE   AltName: Full=2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one 2-D-glucosyltransferase BX9;
DE   AltName: Full=Protein BENZOXAZINLESS 9;
GN   Name=BX9;
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 [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION,
RP   CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DEVELOPMENTAL STAGE, AND
RP   TISSUE SPECIFICITY.
RC   STRAIN=cv. CI31A;
RX   PubMed=11851909; DOI=10.1046/j.1365-313x.2001.01161.x;
RA   von Rad U., Huttl R., Lottspeich F., Gierl A., Frey M.;
RT   "Two glucosyltransferases are involved in detoxification of benzoxazinoids
RT   in maize.";
RL   Plant J. 28:633-642(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. B73;
RA   Yu Y., Currie J., Lomeli R., Angelova A., Collura K., Wissotski M.,
RA   Campos D., Kudrna D., Golser W., Ashely E., Haller K., Descour A.,
RA   Fernandes J., Zuccolo A., Soderlund C., Walbot V.;
RT   "Maize full-length cDNA project.";
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
RC   STRAIN=cv. CI31A;
RX   PubMed=16666853; DOI=10.1104/pp.90.3.1071;
RA   Bailey B.A., Larson R.L.;
RT   "Hydroxamic acid glucosyltransferases from maize seedlings.";
RL   Plant Physiol. 90:1071-1076(1989).
CC   -!- FUNCTION: Glucosyltransferase involved in the last step of
CC       benzoxazinoid glucoside biosynthesis. Catalyzes the glucosylation of
CC       hydroxamic acids utilizing UDP-glucose as glucose doner, reducing the
CC       toxicity of these natural insecticides for storage. Can use DIMBOA and
CC       DIBOA as substrates, HMBOA (2-hydroxy-7-methoxy-2H-1,4-benzoxazin-
CC       3(4H)-one) and HBOA (2-hydroxy-2H-1,4-benzoxazin-3(4H)-one) with a
CC       lower efficiency, but not indole acetic acid or quercitin.
CC       {ECO:0000269|PubMed:11851909}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=DIMBOA + UDP-alpha-D-glucose = DIMBOA beta-D-glucoside + H(+)
CC         + UDP; Xref=Rhea:RHEA:15541, ChEBI:CHEBI:15378, ChEBI:CHEBI:18048,
CC         ChEBI:CHEBI:37573, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885;
CC         EC=2.4.1.202; Evidence={ECO:0000269|PubMed:11851909,
CC         ECO:0000269|PubMed:16666853};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=DIBOA + UDP-alpha-D-glucose = DIBOA beta-D-glucoside + H(+) +
CC         UDP; Xref=Rhea:RHEA:33955, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:58885, ChEBI:CHEBI:63558, ChEBI:CHEBI:63670;
CC         EC=2.4.1.202; Evidence={ECO:0000269|PubMed:11851909,
CC         ECO:0000269|PubMed:16666853};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:16666853};
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000269|PubMed:16666853};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=71 uM for 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one
CC         (DIMBOA) {ECO:0000269|PubMed:11851909, ECO:0000269|PubMed:16666853};
CC         KM=1300 uM for 2,4-dihydroxy-2H-1,4-benzoxazin-3(4H)-one (DIBOA)
CC         {ECO:0000269|PubMed:11851909, ECO:0000269|PubMed:16666853};
CC         KM=96 uM for uridine 5'-diphosphoglucose (UDPG)
CC         {ECO:0000269|PubMed:11851909, ECO:0000269|PubMed:16666853};
CC         Note=kcat is 11.6 sec(-1) for DIMBOA. kcat is 12.5 sec(-1) for DIBOA.
CC         kcat is 22.6 sec(-1) for UDPG.;
CC       pH dependence:
CC         Optimum pH is 8.5. {ECO:0000269|PubMed:11851909,
CC         ECO:0000269|PubMed:16666853};
CC       Temperature dependence:
CC         Optimum temperature is 45 degrees Celsius.
CC         {ECO:0000269|PubMed:11851909, ECO:0000269|PubMed:16666853};
CC   -!- TISSUE SPECIFICITY: Expressed at the same levels in roots and shoots.
CC       {ECO:0000269|PubMed:11851909}.
CC   -!- DEVELOPMENTAL STAGE: Highly expressed in young seedlings up to 4 days
CC       after imbibition. {ECO:0000269|PubMed:11851909}.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AF331855; AAL57038.1; -; Genomic_DNA.
DR   EMBL; BT042760; ACF87765.1; -; mRNA.
DR   RefSeq; NP_001142152.1; NM_001148680.1.
DR   AlphaFoldDB; B4G072; -.
DR   SMR; B4G072; -.
DR   STRING; 4577.GRMZM2G161335_P01; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   PaxDb; B4G072; -.
DR   PRIDE; B4G072; -.
DR   EnsemblPlants; Zm00001eb033030_T001; Zm00001eb033030_P001; Zm00001eb033030.
DR   GeneID; 100274317; -.
DR   Gramene; Zm00001eb033030_T001; Zm00001eb033030_P001; Zm00001eb033030.
DR   KEGG; zma:100274317; -.
DR   MaizeGDB; 9021865; -.
DR   eggNOG; KOG1192; Eukaryota.
DR   HOGENOM; CLU_001724_0_0_1; -.
DR   OMA; IVVAWAP; -.
DR   OrthoDB; 508327at2759; -.
DR   BioCyc; MetaCyc:MON-10603; -.
DR   SABIO-RK; B4G072; -.
DR   Proteomes; UP000007305; Chromosome 1.
DR   ExpressionAtlas; B4G072; baseline and differential.
DR   Genevisible; B4G072; ZM.
DR   GO; GO:0047254; F:2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one 2-D-glucosyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0080043; F:quercetin 3-O-glucosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0080044; F:quercetin 7-O-glucosyltransferase activity; IBA:GO_Central.
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   Direct protein sequencing; Glycosyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..462
FT                   /note="DIMBOA UDP-glucosyltransferase BX9"
FT                   /id="PRO_0000415307"
FT   BINDING         278
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
FT   BINDING         336..338
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
FT   BINDING         353..361
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
FT   BINDING         375..378
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        6
FT                   /note="T -> TGA (in Ref. 1; AAL57038)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        176
FT                   /note="L -> R (in Ref. 1; AAL57038)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        334
FT                   /note="A -> T (in Ref. 1; AAL57038)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        446
FT                   /note="A -> T (in Ref. 1; AAL57038)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   462 AA;  50017 MW;  2314E86FA7AF9A6F CRC64;
     MASSRTGAGA GGRVVVFPFP FQGHFNPVMR LARALHARGL AITVFHSGAL DPADYPADYR
     FVPVTVEADP KLLASEDIAA IVTTLNASCD APFRARLSAL LAAEGRDSVR CVFTDVSWNA
     VLTASSDLGV PALGMMTASA ASLRDYMAYR TLIDKGYLPV KEERKEDPVP ELPPYLVKDL
     LRVDTSDLEE FAELLARTVT AARRASGLIF NTFPLIETDT LAEIHKALSV PVFAVAPLNK
     LVPTATASLH GVVQADRGCL QWLDTQQPGS VLYVSFGSMA AMDPHEFVEL AWGLADSKRP
     FVWVVRPNLI RGFESGALPD GVEDEVRGRG IVVAWAPQEE VLAHPAVGGF LTHNGWNSTV
     EAISEGVPMV CCPRHGDQFG NMRYVCDVWK VGTELVGEQL ERGQVKAAID RLFGTKEGEE
     IKERMKEFKI AAAKGIGIGV DVDETASPRT DLTDLVDLIK SF
 
 
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