ID   86A22_PETHY             Reviewed;         553 AA.
AC   B3RFJ6;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 43.
DE   RecName: Full=Cytochrome P450 86A22 {ECO:0000303|PubMed:19940120};
DE            EC=1.14.14.129 {ECO:0000269|PubMed:19940120};
DE   AltName: Full=Long-chain acyl-CoA omega-monooxygenase {ECO:0000305};
GN   Name=CYP86A22 {ECO:0000303|PubMed:19940120};
OS   Petunia hybrida (Petunia).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia.
OX   NCBI_TaxID=4102 {ECO:0000312|EMBL:AAZ39642.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP   SPECIFICITY, AND SUBSTRATE SPECIFICITY.
RX   PubMed=19940120; DOI=10.1074/jbc.m109.050765;
RA   Han J., Clement J.M., Li J., King A., Ng S., Jaworski J.G.;
RT   "The cytochrome P450 CYP86A22 is a fatty acyl-CoA omega-hydroxylase
RT   essential for Estolide synthesis in the stigma of Petunia hybrida.";
RL   J. Biol. Chem. 285:3986-3996(2010).
CC   -!- FUNCTION: Fatty acyl-CoA omega-hydroxylase essential for the production
CC       of omega-hydroxy fatty acids and the biosynthesis of
CC       triacylglycerol-/diacylglycerol-based estolide polyesters in the
CC       stigma. Substrate preference is 16:0-CoA > 18:1-CoA > 18:0-CoA.
CC       {ECO:0000269|PubMed:19940120}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-octadecenoyl-CoA + O2 + reduced [NADPH--hemoprotein
CC         reductase] = (9Z)-18-hydroxyoctadecenoyl-CoA + H(+) + H2O + oxidized
CC         [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:45072, Rhea:RHEA-
CC         COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57387,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:86044;
CC         EC=1.14.14.129; Evidence={ECO:0000269|PubMed:19940120};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z,12Z)-octadecadienoyl-CoA + O2 + reduced [NADPH--
CC         hemoprotein reductase] = (9Z,12Z)-18-hydroxyoctadecadienoyl-CoA +
CC         H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC         Xref=Rhea:RHEA:45076, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:57383, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:84904; EC=1.14.14.129;
CC         Evidence={ECO:0000269|PubMed:19940120};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Mostly expressed in the developing stigma of floral
CC       buds. Weakly detected in leaves, stems and flowers.
CC       {ECO:0000269|PubMed:19940120}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC       {ECO:0000255|RuleBase:RU000461}.
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DR   EMBL; DQ099538; AAZ39642.1; -; mRNA.
DR   AlphaFoldDB; B3RFJ6; -.
DR   SMR; B3RFJ6; -.
DR   PRIDE; B3RFJ6; -.
DR   KEGG; ag:AAZ39642; -.
DR   BioCyc; MetaCyc:MON-15481; -.
DR   BRENDA; 1.14.14.129; 4700.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IDA:UniProtKB.
DR   GO; GO:0035336; P:long-chain fatty-acyl-CoA metabolic process; IDA:UniProtKB.
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   Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..553
FT                   /note="Cytochrome P450 86A22"
FT                   /id="PRO_0000434399"
FT   TRANSMEM        8..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         459
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   553 AA;  62504 MW;  85DE8B317F4AFF0A CRC64;
     MEVSTTMMIV AIVAAYLLWF KSITKSMKGP KGPTMWPVVG SLPGLIENGN RMHEWIADNL
     RACSGTYQTC ICAIPFLARK QLVTVTCDPK NLEHILKVRF DNYPKGPTWQ AVFHDLLGEG
     IFNSDGDTWL FQRKTAALEF TTRTLRQAMG RWVNRAIKNR FCPILEMAQV QGKPVDLQDL
     LLRLTFDNIC GLAFGKDPET LSPELPENNF ATSFDRATEA TLHRFIMPEF VWKLKKMLGL
     GLEVSLNNSL KQVDNYMTDV INTRKLELLN HQNGGPQHDD LLSRFMKKKE SYSDKFLQHV
     ALNFILAGRD TSSVALSWFF WLVSSNPRVE EKILVEICTI LAETRGNDTS KWLEEPLVFE
     EVDQLMYLKA ALSETLRLYP SVPEDSKHVI SDDYLPDGTF VPAGSNITYS IYSTGRMKFI
     WGEDCLEFKP ERWMSQDGDK FQVQDTFRFV AFNAGPRICL GKDLAYLQMK SIAAAVLLRH
     RLAVAPGHKV EQKMSLTLFM KDGLVMNVTP RDLTPILAKI EKFGKVESCA GEHHLINNGI
     HQPGSIAVNG IAA