BX6_MAIZE
ID BX6_MAIZE Reviewed; 374 AA.
AC Q84TC2;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=DIBOA-glucoside dioxygenase BX6;
DE EC=1.14.11.59 {ECO:0000269|PubMed:18192444};
DE AltName: Full=2,4-dihydroxy-1,4-benzoxazin-3-one-glucoside dioxygenase;
DE AltName: Full=2-oxoglutarate-dependent dioxygenase BX6;
DE AltName: Full=Protein BENZOXAZINONE SYNTHESIS 6;
GN Name=BX6;
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], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. CI31A;
RX PubMed=12620350; DOI=10.1016/s0031-9422(02)00556-3;
RA Frey M., Huber K., Park W.J., Sicker D., Lindberg P., Meeley R.B.,
RA Simmons C.R., Yalpani N., Gierl A.;
RT "A 2-oxoglutarate-dependent dioxygenase is integrated in DIMBOA-
RT biosynthesis.";
RL Phytochemistry 62:371-376(2003).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=18937034; DOI=10.1007/s11103-008-9415-4;
RA Alexandrov N.N., Brover V.V., Freidin S., Troukhan M.E., Tatarinova T.V.,
RA Zhang H., Swaller T.J., Lu Y.-P., Bouck J., Flavell R.B., Feldmann K.A.;
RT "Insights into corn genes derived from large-scale cDNA sequencing.";
RL Plant Mol. Biol. 69:179-194(2009).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND TISSUE 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: 2-oxoglutarate-dependent dioxygenase required for
CC hydroxylation in position C-7 of the benzoxazinoids. Can use 2,4-
CC dihydroxy-2H-1,4-benzoxazin-3(4H)-one 2-D-glucoside (DIBOA-glucoside)
CC as substrate, but not aglucone DIBOA. {ECO:0000269|PubMed:12620350,
CC ECO:0000269|PubMed:18192444}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + DIBOA beta-D-glucoside + O2 = CO2 + succinate
CC + TRIBOA beta-D-glucoside; Xref=Rhea:RHEA:32115, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:63670, ChEBI:CHEBI:63671; EC=1.14.11.59;
CC Evidence={ECO:0000269|PubMed:18192444};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000269|PubMed:18192444};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00805};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00805};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=373 uM for 2,4-dihydroxy-2H-1,4-benzoxazin-3(4H)-one 2-D-glucoside
CC (DIBOA-glucoside) {ECO:0000269|PubMed:18192444};
CC KM=70 uM for 2-oxoglutarate {ECO:0000269|PubMed:18192444};
CC Vmax=59 umol/sec/g enzyme with DIBOA-glucoside as substrate
CC {ECO:0000269|PubMed:18192444};
CC Note=kcat is 2.1 sec(-1) for DIBOA-glucoside.;
CC pH dependence:
CC Optimum pH is 6.0. {ECO:0000269|PubMed:18192444};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {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 -!- DISRUPTION PHENOTYPE: Loss of DIMBOA biosynthesis.
CC {ECO:0000269|PubMed:12620350}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; AF540907; AAO65850.1; -; mRNA.
DR EMBL; BT040894; ACF85899.1; -; mRNA.
DR EMBL; EU960746; ACG32864.1; -; mRNA.
DR RefSeq; NP_001105100.1; NM_001111630.1.
DR AlphaFoldDB; Q84TC2; -.
DR SMR; Q84TC2; -.
DR STRING; 4577.GRMZM6G617209_P01; -.
DR PRIDE; Q84TC2; -.
DR EnsemblPlants; Zm00001eb164860_T001; Zm00001eb164860_P001; Zm00001eb164860.
DR EnsemblPlants; Zm00001eb164860_T002; Zm00001eb164860_P002; Zm00001eb164860.
DR GeneID; 541977; -.
DR Gramene; Zm00001eb164860_T001; Zm00001eb164860_P001; Zm00001eb164860.
DR Gramene; Zm00001eb164860_T002; Zm00001eb164860_P002; Zm00001eb164860.
DR KEGG; zma:541977; -.
DR MaizeGDB; 1204247; -.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_0_0_1; -.
DR OMA; SVEHRVP; -.
DR OrthoDB; 755305at2759; -.
DR BioCyc; MetaCyc:MON-10142; -.
DR SABIO-RK; Q84TC2; -.
DR Proteomes; UP000007305; Chromosome 4.
DR ExpressionAtlas; Q84TC2; baseline and differential.
DR Genevisible; Q84TC2; ZM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; IDA:CACAO.
DR GO; GO:0102717; F:DIBOA-glucoside oxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.330; -; 1.
DR InterPro; IPR026992; DIOX_N.
DR InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR InterPro; IPR027443; IPNS-like_sf.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR Pfam; PF14226; DIOX_N; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Dioxygenase; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..374
FT /note="DIBOA-glucoside dioxygenase BX6"
FT /id="PRO_0000415304"
FT DOMAIN 214..326
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 228
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:D4N500"
FT BINDING 243
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 245
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 305
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 317
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 319
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:D4N500"
SQ SEQUENCE 374 AA; 41369 MW; 6C1A8E047EA07AEC CRC64;
MAPTTATKDD SGYGDERRRE LQAFDDTKLG VKGLVDSGVK SIPSIFHHPP EALSDIISPA
PLPSSPPSGA AIPVVDLSVT RREDLVEQVR HAAGTVGFFW LVNHGVAEEL MGGMLRGVRQ
FNEGPVEAKQ ALYSRDLARN LRFASNFDLF KAAAADWRDT LFCEVAPNPP PREELPEPLR
NVMLEYGAAV TKLARFVFEL LSESLGMPSD HLYEMECMQN LNVVCQYYPP CPEPHRTVGV
KRHTDPGFFT ILLQDGMGGL QVRLGNNGQS GGCWVDIAPR PGALMVNIGD LLQLVTNDRF
RSVEHRVPAN KSSDTARVSV ASFFNTDVRR SERMYGPIPD PSKPPLYRSV RARDFIAKFN
TIGLDGRALD HFRL
