C93A1_SOYBN
ID C93A1_SOYBN Reviewed; 509 AA.
AC Q42798;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=3,9-dihydroxypterocarpan 6A-monooxygenase;
DE EC=1.14.14.93 {ECO:0000269|PubMed:9720921};
DE AltName: Full=Cytochrome P450 93A1;
DE AltName: Full=Dihydroxypterocarpan 6a-hydroxylase;
DE Short=D6aH;
GN Name=CYP93A1; OrderedLocusNames=Glyma03g29950;
OS Glycine max (Soybean) (Glycine hispida).
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; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION BY METHYL JASMONATE.
RC STRAIN=cv. Corsoy;
RX PubMed=8612798; DOI=10.1016/0014-5793(96)00229-3;
RA Suzuki G., Ohta H., Kato T., Igarashi T., Sakai F., Shibata D., Takano A.,
RA Masuda T., Shioi Y., Takamiya K.;
RT "Induction of a novel cytochrome P450 (CYP93 family) by methyl jasmonate in
RT soybean suspension-cultured cells.";
RL FEBS Lett. 383:83-86(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82;
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [3]
RP PROTEIN SEQUENCE OF 331-340, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION BY ELICITOR.
RX PubMed=9720921; DOI=10.1016/s0014-5793(98)00866-7;
RA Schopfer C.R., Kochs G., Lottspeich F., Ebel J.;
RT "Molecular characterization and functional expression of
RT dihydroxypterocarpan 6a-hydroxylase, an enzyme specific for pterocarpanoid
RT phytoalexin biosynthesis in soybean (Glycine max L.).";
RL FEBS Lett. 432:182-186(1998).
RN [4]
RP INDUCTION BY GMSUBPEP.
RC STRAIN=cv. A3525;
RX PubMed=20679205; DOI=10.1073/pnas.1007568107;
RA Pearce G., Yamaguchi Y., Barona G., Ryan C.A.;
RT "A subtilisin-like protein from soybean contains an embedded, cryptic
RT signal that activates defense-related genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:14921-14925(2010).
RN [5]
RP INDUCTION BY GMPEP890 AND GMPEP914.
RC STRAIN=cv. A3525;
RX PubMed=21478368; DOI=10.1104/pp.111.173096;
RA Yamaguchi Y., Barona G., Ryan C.A., Pearce G.;
RT "GmPep914, an eight-amino acid peptide isolated from soybean leaves,
RT activates defense-related genes.";
RL Plant Physiol. 156:932-942(2011).
RN [6]
RP IDENTIFICATION AS CYP93A1.
RX PubMed=24826896; DOI=10.1371/journal.pone.0097250;
RA Shearer A.G., Altman T., Rhee C.D.;
RT "Finding sequences for over 270 orphan enzymes.";
RL PLoS ONE 9:E97250-E97250(2014).
CC -!- FUNCTION: Cytochrome P450 involved in the biosynthesis of the
CC phytoalexin glyceollin. Stereospecific for (6aR,11aR)-3,9-
CC dihydroxypterocarpan. {ECO:0000269|PubMed:9720921}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6aR,11aR)-3,9-dihydroxypterocarpan + O2 + reduced [NADPH--
CC hemoprotein reductase] = (6aS,11aS)-3,6a,9-trihydroxypterocarpan +
CC H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:15321, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:15648, ChEBI:CHEBI:15649, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210; EC=1.14.14.93;
CC Evidence={ECO:0000269|PubMed:9720921};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.1 uM for (6aR,11aR)-3,9-dihydroxypterocarpan
CC {ECO:0000269|PubMed:9720921};
CC pH dependence:
CC Optimum pH is 7.4. {ECO:0000269|PubMed:9720921};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius.
CC {ECO:0000269|PubMed:9720921};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}.
CC -!- INDUCTION: Up-regulated by methyl jasmonate, elicitor treatments and
CC elicitor peptides GmSubPep, GmPEP890 and GmPEP914.
CC {ECO:0000269|PubMed:20679205, ECO:0000269|PubMed:21478368,
CC ECO:0000269|PubMed:8612798, ECO:0000269|PubMed:9720921}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; D83968; BAA12159.1; -; mRNA.
DR PIR; S62899; S62899.
DR RefSeq; NP_001241186.1; NM_001254257.2.
DR AlphaFoldDB; Q42798; -.
DR SMR; Q42798; -.
DR STRING; 3847.GLYMA03G29950.1; -.
DR PRIDE; Q42798; -.
DR EnsemblPlants; KRH67050; KRH67050; GLYMA_03G143700.
DR GeneID; 100776878; -.
DR Gramene; KRH67050; KRH67050; GLYMA_03G143700.
DR KEGG; gmx:100776878; -.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_4_0_1; -.
DR InParanoid; Q42798; -.
DR OMA; HRYDTMM; -.
DR OrthoDB; 702827at2759; -.
DR Proteomes; UP000008827; Chromosome 3.
DR Genevisible; Q42798; GM.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0047082; F:3,9-dihydroxypterocarpan 6a-monooxygenase 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 GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
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 Direct protein sequencing; Heme; Iron; Membrane; Metal-binding;
KW Monooxygenase; Oxidoreductase; Plant defense; Reference proteome.
FT CHAIN 1..509
FT /note="3,9-dihydroxypterocarpan 6A-monooxygenase"
FT /id="PRO_0000052188"
FT BINDING 447
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"
SQ SEQUENCE 509 AA; 57870 MW; EC8B1EA66A34A0FB CRC64;
MAYQVLLICL VSTIVFAYIL WRKQSKKNLP PSPKALPIIG HLHLVSPIPH QDFYKLSTRH
GPIMQLFLGS VPCVVASTAE AAKEFLKTHE INFSNRPGQN VAVKGLAYDS QDFLFAFAPF
GPYWKFMKKL CMSELLSGRM MDQFLPVRQQ ETKRFISRVF RKGVAGEAVD FGDELMTLSN
NIVSRMTLSQ KTSENDNQAE EMKKLVSNIA ELMGKFNVSD FIWYLKPFDL QGFNRKIKET
RDRFDVVVDG IIKQRQEERR KNKETGTAKQ FKDMLDVLLD MHEDENAEIK LDKKNIKAFI
MDIFVAGTDT SAVSIEWAMA ELINNPDVLE KARQEIDAVV GKSRMVEESD IANLPYLQAI
VRETLRLHPG GPLVVRESSK SAVVCGYDIP AKTRLFVNVW AIGRDPNHWE KPFEFRPERF
IRDGQNQLDV RGQHYHFIPF GSGRRTCPGA SLAWQVVPVN LAIIIQCFQW KLVGGNGKVD
MEEKSGITLP RANPIICVPV PRINPFPTI
