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BX7_MAIZE
ID   BX7_MAIZE               Reviewed;         386 AA.
AC   B1P123;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=TRIBOA-glucoside O-methyltransferase BX7;
DE            EC=2.1.1.241;
DE   AltName: Full=2,4,7-trihydroxy-1,4-benzoxazin-3-one-glucoside 7-O-methyltransferase;
DE   AltName: Full=Protein BENZOXAZINONE SYNTHESIS 7;
GN   Name=BX7; Synonyms=ZRP4;
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 [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC
RP   ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DEVELOPMENTAL STAGE, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=cv. CI31A;
RX   PubMed=18192444; DOI=10.1104/pp.107.111237;
RA   Jonczyk R., Schmidt H., Osterrieder A., Fiesselmann A., Schullehner K.,
RA   Haslbeck M., Sicker D., Hofmann D., Yalpani N., Simmons C., Frey M.,
RA   Gierl A.;
RT   "Elucidation of the Final Reactions of DIMBOA-Glucoside Biosynthesis in
RT   Maize: Characterization of Bx6 and Bx7.";
RL   Plant Physiol. 146:1053-1063(2008).
CC   -!- FUNCTION: O-methyltransferase involved in the benzoxazinoid glucoside
CC       biosynthesis. Can use 2,4,7-trihydroxy-2H-1,4-benzoxazin-3(4H)-one 2-D-
CC       glucoside (TRIBOA-glucoside) as substrate, but not aglucone TRIBOA,
CC       caffeic acid, ferulic acid, apigenin or quercetin.
CC       {ECO:0000269|PubMed:18192444}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-adenosyl-L-methionine + TRIBOA beta-D-glucoside = DIMBOA
CC         beta-D-glucoside + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:32099, ChEBI:CHEBI:15378, ChEBI:CHEBI:37573,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:63671;
CC         EC=2.1.1.241; Evidence={ECO:0000269|PubMed:18192444};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=272 uM for 2,4,7-trihydroxyy-2H-1,4-benzoxazin-3(4H)-one 2-D-
CC         glucoside (TRIBOA-glucoside) {ECO:0000269|PubMed:18192444};
CC         Vmax=6.79 umol/sec/g enzyme with TRIBOA-glucoside as substrate
CC         {ECO:0000269|PubMed:18192444};
CC         Note=kcat is 0.249 sec(-1) for TRIBOA-glucoside.;
CC       pH dependence:
CC         Optimum pH is 7.0. {ECO:0000269|PubMed:18192444};
CC   -!- TISSUE SPECIFICITY: Expressed in seedlings and newly formed crown
CC       roots. Highest expression in the scutellar node. Low to non detectable
CC       levels in cob, tassel and mature organs like husk or leaves.
CC       {ECO:0000269|PubMed:18192444}.
CC   -!- DEVELOPMENTAL STAGE: Peak of expression in 3- and 4-day-old seedlings.
CC       {ECO:0000269|PubMed:18192444}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Cation-independent O-methyltransferase family. COMT
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU01020}.
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DR   EMBL; EU192149; ABY59051.1; -; mRNA.
DR   RefSeq; NP_001120719.1; NM_001127247.1.
DR   AlphaFoldDB; B1P123; -.
DR   SMR; B1P123; -.
DR   PRIDE; B1P123; -.
DR   GeneID; 100147731; -.
DR   KEGG; zma:100147731; -.
DR   MaizeGDB; 1204241; -.
DR   OrthoDB; 817726at2759; -.
DR   BioCyc; MetaCyc:MON-16976; -.
DR   BRENDA; 2.1.1.241; 6752.
DR   SABIO-RK; B1P123; -.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; B1P123; baseline and differential.
DR   GO; GO:0008171; F:O-methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0102718; F:TRIBOA-glucoside methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019438; P:aromatic compound biosynthetic process; IBA:GO_Central.
DR   GO; GO:0032259; P:methylation; IBA:GO_Central.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR016461; COMT-like.
DR   InterPro; IPR001077; O_MeTrfase_dom.
DR   InterPro; IPR012967; Plant_MeTrfase_dimerisation.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR11746; PTHR11746; 1.
DR   Pfam; PF08100; Dimerisation; 1.
DR   Pfam; PF00891; Methyltransf_2; 1.
DR   PIRSF; PIRSF005739; O-mtase; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51683; SAM_OMT_II; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Methyltransferase; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..386
FT                   /note="TRIBOA-glucoside O-methyltransferase BX7"
FT                   /id="PRO_0000415305"
FT   ACT_SITE        287
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         224
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         248
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         270
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         283
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ   SEQUENCE   386 AA;  42131 MW;  28C5504F334812CB CRC64;
     MGHQAQHGTD DTEELLAAHR QLWCHALGYV KSMALKCALD LRIPDTIDRC GGSATLGELL
     AASEISASNH DYLRRVMRTL TAMRIFAASH DPAKADDAAA ISYQLTPASR LLVSSSSSVD
     DAAGASKENT TTPSILPNIA HLVRPNTISL LFSMGEWMKD ESAASVSLYE TVHRQGMWAC
     VEDDAANRAS FYESMDADTR LVMQAVVRRC PHVFDGIKSL VDVGGGRGTA AAAVVAAFPH
     IQRCTVMDLP HVVAEAPAGT AGLSFHGGDM FEHIPSADAL MLKWILHDWD EDKCIKIMER
     CKEAIGGKEA GGKVIIIDTV LGSRADDDDD DKTCRETYVL DLHILSFVNG AEREEHEWRR
     IFLAAGFRDY KITHTRGIPS IIEVFP
 
 
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