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Database: UniProt
Entry: A0A059B844_EUCGR
LinkDB: A0A059B844_EUCGR
Original site: A0A059B844_EUCGR 
ID   A0A059B844_EUCGR        Unreviewed;       507 AA.
AC   A0A059B844;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=noroxomaritidine synthase {ECO:0000256|ARBA:ARBA00039071};
DE            EC=1.14.19.50 {ECO:0000256|ARBA:ARBA00039071};
GN   ORFNames=EUGRSUZ_H04870 {ECO:0000313|EMBL:KCW62209.1};
OS   Eucalyptus grandis (Flooded gum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX   NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW62209.1};
RN   [1] {ECO:0000313|EMBL:KCW62209.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW62209.1};
RA   Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT   "The genome of Eucalyptus grandis.";
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4'-O-methylnorbelladine + O2 + reduced [NADPH--hemoprotein
CC         reductase] = (10bR,4aS)-noroxomaritidine + H(+) + 2 H2O + oxidized
CC         [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:51260, Rhea:RHEA-
CC         COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210, ChEBI:CHEBI:133993, ChEBI:CHEBI:133995;
CC         EC=1.14.19.50; Evidence={ECO:0000256|ARBA:ARBA00036965};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4'-O-methylnorbelladine + O2 + reduced [NADPH--hemoprotein
CC         reductase] = (10bS,4aR)-noroxomaritidine + H(+) + 2 H2O + oxidized
CC         [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:51264, Rhea:RHEA-
CC         COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210, ChEBI:CHEBI:133993, ChEBI:CHEBI:133996;
CC         EC=1.14.19.50; Evidence={ECO:0000256|ARBA:ARBA00035970};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC       {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR   EMBL; KK198760; KCW62209.1; -; Genomic_DNA.
DR   RefSeq; XP_010027344.1; XM_010029042.1.
DR   AlphaFoldDB; A0A059B844; -.
DR   EnsemblPlants; KCW62209; KCW62209; EUGRSUZ_H04870.
DR   Gramene; KCW62209; KCW62209; EUGRSUZ_H04870.
DR   eggNOG; KOG0157; Eukaryota.
DR   InParanoid; A0A059B844; -.
DR   OMA; NTRILWK; -.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   CDD; cd11064; CYP86A; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 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   PANTHER; PTHR24296; CYTOCHROME P450; 1.
DR   PANTHER; PTHR24296:SF1; CYTOCHROME P450, FAMILY 96, SUBFAMILY A, POLYPEPTIDE 10; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|RuleBase:RU000461};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU000461};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU000461};
KW   Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000461}.
SQ   SEQUENCE   507 AA;  58025 MW;  11400447F50D5D3B CRC64;
     MAVIGFLEIF LAGICFAVLC LLSKSDDGFP RNWPLVGMLP ALFLNLSRVH DWATGLVERS
     HGNFFFRSLW FSSMDMLVTA DPANFHYIMS ANFGNFPKGP EFKRVFDILG DGIINSDSNL
     WSTQRRVAQV FMKDQRFHRF LLSTTRDKAE NGLLRVLDEL SQRGVTVDLQ DLFHRFTFDS
     ACRFVTGFDP GSLSVEFPEV PISKALGDAE EVIFYRHLYP EWFGTLQRLL GIGVEEKLRR
     AWKDIDQILG NYIAMKRVEL REGTNKVKGD ENGADLLTLY MVENETLGAL ECNDKFLRDM
     IMNFMSAGIE TTGSTLTWFF WALSMNPSVD MRIREEIRSV IPKEEQNLMV FNISEHMHKM
     VYLHGAICES LRLYPPIPLL PKCPTNPDVL PSGHKVDPGA KIVVHMYAMG RMKSIWGEDC
     LEFRPERWIL ERGGIRHQPS YKFVAFNAGP RTCLGKDVAF TQIKMVAATV IHNYEVHVVE
     DHPVRPSNSI ILHMKHGLKV KVTRRRL
//
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