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Isoflavone 2'-hydroxylase (EC 1.14.13.53) (4'-methoxyisoflavone 2'-hydroxylase) (Cytochrome P450 81E7)

 C81E7_MEDTR             Reviewed;         498 AA.
Q6WNR0;
29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
23-MAY-2018, entry version 62.
RecName: Full=Isoflavone 2'-hydroxylase {ECO:0000303|PubMed:14617078};
EC=1.14.13.53 {ECO:0000269|PubMed:14617078};
AltName: Full=4'-methoxyisoflavone 2'-hydroxylase;
AltName: Full=Cytochrome P450 81E7 {ECO:0000303|PubMed:14617078};
Name=CYP81E7 {ECO:0000303|PubMed:14617078};
Medicago truncatula (Barrel medic) (Medicago tribuloides).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae;
Trifolieae; Medicago.
NCBI_TaxID=3880 {ECO:0000312|EMBL:AAQ20040.1};
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND INDUCTION.
PubMed=14617078; DOI=10.1046/j.1365-313X.2003.01893.x;
Liu C.J., Huhman D., Sumner L.W., Dixon R.A.;
"Regiospecific hydroxylation of isoflavones by cytochrome p450 81E
enzymes from Medicago truncatula.";
Plant J. 36:471-484(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Jemalong A17 {ECO:0000312|Proteomes:UP000002051};
PubMed=22089132; DOI=10.1038/nature10625;
Young N.D., Debelle F., Oldroyd G.E.D., Geurts R., Cannon S.B.,
Udvardi M.K., Benedito V.A., Mayer K.F.X., Gouzy J., Schoof H.,
Van de Peer Y., Proost S., Cook D.R., Meyers B.C., Spannagl M.,
Cheung F., De Mita S., Krishnakumar V., Gundlach H., Zhou S.,
Mudge J., Bharti A.K., Murray J.D., Naoumkina M.A., Rosen B.,
Silverstein K.A.T., Tang H., Rombauts S., Zhao P.X., Zhou P.,
Barbe V., Bardou P., Bechner M., Bellec A., Berger A., Berges H.,
Bidwell S., Bisseling T., Choisne N., Couloux A., Denny R.,
Deshpande S., Dai X., Doyle J.J., Dudez A.-M., Farmer A.D.,
Fouteau S., Franken C., Gibelin C., Gish J., Goldstein S.,
Gonzalez A.J., Green P.J., Hallab A., Hartog M., Hua A.,
Humphray S.J., Jeong D.-H., Jing Y., Jocker A., Kenton S.M.,
Kim D.-J., Klee K., Lai H., Lang C., Lin S., Macmil S.L.,
Magdelenat G., Matthews L., McCorrison J., Monaghan E.L., Mun J.-H.,
Najar F.Z., Nicholson C., Noirot C., O'Bleness M., Paule C.R.,
Poulain J., Prion F., Qin B., Qu C., Retzel E.F., Riddle C.,
Sallet E., Samain S., Samson N., Sanders I., Saurat O., Scarpelli C.,
Schiex T., Segurens B., Severin A.J., Sherrier D.J., Shi R., Sims S.,
Singer S.R., Sinharoy S., Sterck L., Viollet A., Wang B.-B., Wang K.,
Wang M., Wang X., Warfsmann J., Weissenbach J., White D.D.,
White J.D., Wiley G.B., Wincker P., Xing Y., Yang L., Yao Z., Ying F.,
Zhai J., Zhou L., Zuber A., Denarie J., Dixon R.A., May G.D.,
Schwartz D.C., Rogers J., Quetier F., Town C.D., Roe B.A.;
"The Medicago genome provides insight into the evolution of rhizobial
symbioses.";
Nature 480:520-524(2011).
-!- FUNCTION: Involved in the biosynthesis of the pterocarpin
phytoalexins. Acts on isoflavones with a 4'-methoxy group on the
B-ring, such as formononetin and biochanin A, and on
pseudobaptigenin. Has a low activity with daidzein and genistein
and no activity with the 7-O-methylated isoflavonoids
isoformononetin and prunetin. {ECO:0000269|PubMed:14617078}.
-!- CATALYTIC ACTIVITY: Formononetin + NADPH + O(2) = 2'-
hydroxyformononetin + NADP(+) + H(2)O.
{ECO:0000269|PubMed:14617078}.
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413;
Evidence={ECO:0000250|UniProtKB:P04798};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.17 uM for NADPH {ECO:0000269|PubMed:14617078};
KM=67 uM for formononetin {ECO:0000269|PubMed:14617078};
KM=51 uM for biochanin A {ECO:0000269|PubMed:14617078};
Note=kcat is 0.015 sec(-1) with formononetin as substrate. kcat
is 0.033 sec(-1) with biochanin A as substrate.
{ECO:0000269|PubMed:14617078};
pH dependence:
Optimum pH is 8.0. {ECO:0000269|PubMed:14617078};
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:14617078}; Single-pass membrane protein
{ECO:0000255}.
-!- TISSUE SPECIFICITY: Expressed constitutively in roots, but present
at very low levels in uninfected stems and leaves.
{ECO:0000269|PubMed:14617078}.
-!- INDUCTION: Down-regulated in roots by drought Up-regulated in
leaves upon infection with fungus. No regulation by methyl
jasmonate or elicitor treatment. {ECO:0000269|PubMed:14617078}.
-!- SIMILARITY: Belongs to the cytochrome P450 family.
{ECO:0000255|RuleBase:RU000461}.
-----------------------------------------------------------------------
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EMBL; AY278227; AAQ20040.1; -; mRNA.
EMBL; CM001220; KEH31433.1; -; Genomic_DNA.
RefSeq; XP_013457402.1; XM_013601948.1.
UniGene; Mtr.1188; -.
ProteinModelPortal; Q6WNR0; -.
SMR; Q6WNR0; -.
EnsemblPlants; KEH31433; KEH31433; MTR_4g094775.
GeneID; 25493449; -.
Gramene; KEH31433; KEH31433; MTR_4g094775.
KEGG; mtr:MTR_4g094775; -.
KO; K13260; -.
BRENDA; 1.14.13.89; 3201.
SABIO-RK; Q6WNR0; -.
Proteomes; UP000002051; Chromosome 4.
Proteomes; UP000002051; Unassembled WGS sequence.
ExpressionAtlas; Q6WNR0; differential.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0047957; F:4'-methoxyisoflavone 2'-hydroxylase activity; IEA:UniProtKB-EC.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
Gene3D; 1.10.630.10; -; 1.
InterPro; IPR001128; Cyt_P450.
InterPro; IPR017972; Cyt_P450_CS.
InterPro; IPR002401; Cyt_P450_E_grp-I.
InterPro; IPR036396; Cyt_P450_sf.
Pfam; PF00067; p450; 1.
PRINTS; PR00463; EP450I.
PRINTS; PR00385; P450.
SUPFAM; SSF48264; SSF48264; 1.
PROSITE; PS00086; CYTOCHROME_P450; 1.
1: Evidence at protein level;
Complete proteome; Endoplasmic reticulum; Heme; Iron; Membrane;
Metal-binding; Monooxygenase; NADP; Oxidoreductase;
Reference proteome; Transmembrane; Transmembrane helix.
CHAIN 1 498 Isoflavone 2'-hydroxylase.
/FTId=PRO_0000430742.
TRANSMEM 3 23 Helical. {ECO:0000255}.
COMPBIAS 76 79 Poly-Val. {ECO:0000255}.
METAL 436 436 Iron (heme axial ligand).
{ECO:0000250|UniProtKB:P04798}.
SEQUENCE 498 AA; 57641 MW; B8887C0B4E71B89D CRC64;
MGILSYLCYS LFYLSIFFII RLLFQSRKFK NLPPGPTSLP IIGNLHHLKR PLNRTFKALT
EKYGNVISLW FGSRLVVVVS SLSEFQECFT KNDVVLANRP RFLSGKYIFY NYTTLGSTSY
GEHWRNLRRI TSLDVLSNHR INNFAPIRRD ETQRLIKKLA EDSSTKFAEV ELTFRFFDMT
FNNIMRMISG KRYYGDDCDI SEVQEASQFR DMVSELLQLS GANNKTDFMP LLKFLDFENL
EKRVKRIGEK NDVFLSGLLQ EQRSKKERTN TMIDHLLNMQ ESQPEYYTDT IIKGLCLAML
LAGTDSSAVT LEWTMSNILN YPEVLKKVRD EVDTHVGQDR LVDESDLPKL TYLRNVIYET
LRLYTPAPLL LPHSTADECI MGGYKVPRDT IVLINAWAIH RDPETWSEAT TFKPERFDKK
GELEKMIAFG MGRRACPGEG LALRAISMTL ALLVQCFDWK RINDEKIDMS ERDGFTMTKL
LPLKAMCKTR PVVNKVFK


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