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BX8_MAIZE
ID   BX8_MAIZE               Reviewed;         459 AA.
AC   Q8W2B7;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=DIMBOA UDP-glucosyltransferase BX8;
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 BX8;
DE   AltName: Full=Protein BENZOXAZINLESS 8;
GN   Name=Bx8;
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. B73;
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   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=81 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=61 uM for 2,4-dihydroxy-2H-1,4-benzoxazin-3(4H)-one (DIBOA)
CC         {ECO:0000269|PubMed:11851909, ECO:0000269|PubMed:16666853};
CC         KM=81 uM for uridine 5'-diphosphoglucose (UDPG) with DIMBOA as
CC         {ECO:0000269|PubMed:11851909, ECO:0000269|PubMed:16666853};
CC         Note=kcat is 22.7 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; AF331854; AAL57037.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8W2B7; -.
DR   SMR; Q8W2B7; -.
DR   STRING; 4577.GRMZM2G085054_P01; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   PaxDb; Q8W2B7; -.
DR   PRIDE; Q8W2B7; -.
DR   MaizeGDB; 9021865; -.
DR   eggNOG; KOG1192; Eukaryota.
DR   BioCyc; MetaCyc:MON-10602; -.
DR   SABIO-RK; Q8W2B7; -.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; Q8W2B7; baseline and differential.
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   InterPro; IPR035595; UDP_glycos_trans_CS.
DR   Pfam; PF00201; UDPGT; 1.
DR   PROSITE; PS00375; UDPGT; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycosyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..459
FT                   /note="DIMBOA UDP-glucosyltransferase BX8"
FT                   /id="PRO_0000415306"
FT   BINDING         282
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
FT   BINDING         340..342
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
FT   BINDING         357..365
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
FT   BINDING         379..382
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   459 AA;  49470 MW;  0F5AE7AAA56AD3E7 CRC64;
     MAASCGGRVV VFPFPFQGHF NPVMRLARAL HARGVGITVF HTAGARAPDP ADYPADYRFV
     PVPVEVAPEL MASEDIAAIV TALNAACEAP FRDRLSALLS AADGEAGEAG GRVRCVLTDV
     SWDAVLSAAR GLGVPALGVM TASAATFRVY MAYRTLVDKG YLPVREERKD DAVAELPPYR
     VKDLLRHETC DLEEFADLLG RVIAAARLSS GLIFHTFPFI EAGTLGEIRD DMSVPVYAVA
     PLNKLVPAAT ASLHGEVQAD RGCLRWLDAQ RARSVLYVSF GSMAAMDPHE FVELAWGLAD
     AGRPFVWVVR PNLIRGFESG ALPDGVEDRV RGRGVVVSWA PQEEVLAHPA VGGFFTHCGW
     NSTVEAVSEG VPMICHPRHG DQYGNARYVC HVWKVGTEVA GDQLERGEIK AAIDRLMGGS
     EEGEGIRKRM NELKIAADKG IDESAGSDLT NLVHLINSY
 
 
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