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 24-JAN-2024, entry version 64.
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 STRING; 4577.B1P123; -.
DR GeneID; 100147731; -.
DR KEGG; zma:100147731; -.
DR MaizeGDB; 1204241; -.
DR InParanoid; B1P123; -.
DR OrthoDB; 948580at2759; -.
DR BioCyc; MetaCyc:MONOMER-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; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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; O-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR11746:SF142; TRIBOA-GLUCOSIDE O-METHYLTRANSFERASE BX7; 1.
DR Pfam; PF08100; Dimerisation; 1.
DR Pfam; PF00891; Methyltransf_2; 1.
DR PIRSF; PIRSF005739; O-mtase; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 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
//
