ID A0A176VFP3_MARPO Unreviewed; 441 AA.
AC A0A176VFP3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Allene oxide synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AXG93_2958s1040 {ECO:0000313|EMBL:OAE19729.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE19729.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE19729.1, ECO:0000313|Proteomes:UP000077202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE19729.1};
RA Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT "Mechanisms controlling the formation of the plant cell surface in tip-
RT growing cells are functionally conserved among land plants.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971};
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAE19729.1}.
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DR EMBL; LVLJ01003787; OAE19729.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A176VFP3; -.
DR OrthoDB; 447408at2759; -.
DR Proteomes; UP000077202; Unassembled WGS sequence.
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:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd11071; CYP74; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24286; CYTOCHROME P450 26; 1.
DR PANTHER; PTHR24286:SF49; INACTIVE LINOLENATE HYDROPEROXIDE LYASE-RELATED; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000077202}.
SQ SEQUENCE 441 AA; 49627 MW; 58C7F4A98694CB88 CRC64;
MAESTPLLKA SDLPLKEIPG SYGPVFWGAF KDKMDFYWRE GTPKFYETRR DKYKSTVYRT
NVAPGPPGFS NPQVVMLLDQ KSYPILFDVS KVEKRDVFTG TYMPSTKYNG GYRILPYLDP
SEEKHTKTKE FCFDVLKLSV PRILPSFHSA ISECFNSWEA ALAKSGKVNF ATALTPATFK
FNVKAFIGRD PTEAGTNSLG TSGPTYTQLW QFPQIAPILV VPVPKILIPL AEVVVHTFPI
PFLFVKYFYG KLTKFFQTYA TELLDLAESK HGLGREEATH NLLFYTLFNS WGGINIFFPG
MLKRLGALSP EEQLEVANDV RKAISAEGGL TLKALSQMTL VTSLVYEALR IDPPVPFQYA
HAKMDLVIES HDSSFSVKKG EMLAGYMPLA CKDPVVFKEP DTFLPKRFMG DGSKLLKYDY
MQIDADGNLT ILTKKRIPRR A
//