C81E7_MEDTR
ID C81E7_MEDTR Reviewed; 498 AA.
AC Q6WNR0;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Isoflavone 2'-hydroxylase {ECO:0000303|PubMed:14617078};
DE EC=1.14.14.89 {ECO:0000269|PubMed:14617078};
DE AltName: Full=4'-methoxyisoflavone 2'-hydroxylase;
DE AltName: Full=Cytochrome P450 81E7 {ECO:0000303|PubMed:14617078};
GN Name=CYP81E7 {ECO:0000303|PubMed:14617078};
OS Medicago truncatula (Barrel medic) (Medicago tribuloides).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX NCBI_TaxID=3880 {ECO:0000312|EMBL:AAQ20040.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND INDUCTION.
RX PubMed=14617078; DOI=10.1046/j.1365-313x.2003.01893.x;
RA Liu C.J., Huhman D., Sumner L.W., Dixon R.A.;
RT "Regiospecific hydroxylation of isoflavones by cytochrome P450 81E enzymes
RT from Medicago truncatula.";
RL Plant J. 36:471-484(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Jemalong A17 {ECO:0000312|Proteomes:UP000002051};
RX PubMed=22089132; DOI=10.1038/nature10625;
RA Young N.D., Debelle F., Oldroyd G.E.D., Geurts R., Cannon S.B.,
RA Udvardi M.K., Benedito V.A., Mayer K.F.X., Gouzy J., Schoof H.,
RA Van de Peer Y., Proost S., Cook D.R., Meyers B.C., Spannagl M., Cheung F.,
RA De Mita S., Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K.,
RA Murray J.D., Naoumkina M.A., Rosen B., Silverstein K.A.T., Tang H.,
RA Rombauts S., Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M.,
RA Bellec A., Berger A., Berges H., Bidwell S., Bisseling T., Choisne N.,
RA Couloux A., Denny R., Deshpande S., Dai X., Doyle J.J., Dudez A.-M.,
RA Farmer A.D., Fouteau S., Franken C., Gibelin C., Gish J., Goldstein S.,
RA Gonzalez A.J., Green P.J., Hallab A., Hartog M., Hua A., Humphray S.J.,
RA Jeong D.-H., Jing Y., Jocker A., Kenton S.M., Kim D.-J., Klee K., Lai H.,
RA Lang C., Lin S., Macmil S.L., Magdelenat G., Matthews L., McCorrison J.,
RA Monaghan E.L., Mun J.-H., Najar F.Z., Nicholson C., Noirot C.,
RA O'Bleness M., Paule C.R., Poulain J., Prion F., Qin B., Qu C., Retzel E.F.,
RA Riddle C., Sallet E., Samain S., Samson N., Sanders I., Saurat O.,
RA Scarpelli C., Schiex T., Segurens B., Severin A.J., Sherrier D.J., Shi R.,
RA Sims S., Singer S.R., Sinharoy S., Sterck L., Viollet A., Wang B.-B.,
RA Wang K., Wang M., Wang X., Warfsmann J., Weissenbach J., White D.D.,
RA White J.D., Wiley G.B., Wincker P., Xing Y., Yang L., Yao Z., Ying F.,
RA Zhai J., Zhou L., Zuber A., Denarie J., Dixon R.A., May G.D.,
RA Schwartz D.C., Rogers J., Quetier F., Town C.D., Roe B.A.;
RT "The Medicago genome provides insight into the evolution of rhizobial
RT symbioses.";
RL Nature 480:520-524(2011).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Jemalong A17;
RX PubMed=24767513; DOI=10.1186/1471-2164-15-312;
RA Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S.,
RA Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F.,
RA Schwartz D.C., Town C.D.;
RT "An improved genome release (version Mt4.0) for the model legume Medicago
RT truncatula.";
RL BMC Genomics 15:312-312(2014).
CC -!- FUNCTION: Involved in the biosynthesis of the pterocarpin phytoalexins.
CC Acts on isoflavones with a 4'-methoxy group on the B-ring, such as
CC formononetin and biochanin A, and on pseudobaptigenin. Has a low
CC activity with daidzein and genistein and no activity with the 7-O-
CC methylated isoflavonoids isoformononetin and prunetin.
CC {ECO:0000269|PubMed:14617078}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=formononetin + O2 + reduced [NADPH--hemoprotein reductase] =
CC 2'-hydroxyformononetin + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:12388, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:77687,
CC ChEBI:CHEBI:77688; EC=1.14.14.89;
CC Evidence={ECO:0000269|PubMed:14617078};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=67 uM for formononetin {ECO:0000269|PubMed:14617078};
CC KM=51 uM for biochanin A {ECO:0000269|PubMed:14617078};
CC Note=kcat is 0.015 sec(-1) with formononetin as substrate. kcat is
CC 0.033 sec(-1) with biochanin A as substrate.
CC {ECO:0000269|PubMed:14617078};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:14617078};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:14617078}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed constitutively in roots, but present at
CC very low levels in uninfected stems and leaves.
CC {ECO:0000269|PubMed:14617078}.
CC -!- INDUCTION: Down-regulated in roots by drought Up-regulated in leaves
CC upon infection with fungus. No regulation by methyl jasmonate or
CC elicitor treatment. {ECO:0000269|PubMed:14617078}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000255|RuleBase:RU000461}.
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DR EMBL; AY278227; AAQ20040.1; -; mRNA.
DR EMBL; CM001220; KEH31433.1; -; Genomic_DNA.
DR RefSeq; XP_013457402.1; XM_013601948.1.
DR AlphaFoldDB; Q6WNR0; -.
DR SMR; Q6WNR0; -.
DR EnsemblPlants; KEH31433; KEH31433; MTR_4g094775.
DR GeneID; 25493449; -.
DR Gramene; KEH31433; KEH31433; MTR_4g094775.
DR KEGG; mtr:MTR_4g094775; -.
DR HOGENOM; CLU_001570_4_0_1; -.
DR OrthoDB; 702827at2759; -.
DR BRENDA; 1.14.14.90; 3201.
DR SABIO-RK; Q6WNR0; -.
DR Proteomes; UP000002051; Chromosome 4.
DR ExpressionAtlas; Q6WNR0; differential.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0047957; F:4'-methoxyisoflavone 2'-hydroxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IBA:GO_Central.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..498
FT /note="Isoflavone 2'-hydroxylase"
FT /id="PRO_0000430742"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 436
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P04798"
SQ 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
