ID A0A176W8H0_MARPO Unreviewed; 537 AA.
AC A0A176W8H0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Cytochrome P450 {ECO:0008006|Google:ProtNLM};
GN ORFNames=AXG93_4831s1270 {ECO:0000313|EMBL:OAE29367.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE29367.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE29367.1, 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:OAE29367.1};
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|RuleBase:RU000461}.
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:OAE29367.1}.
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DR EMBL; LVLJ01001470; OAE29367.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A176W8H0; -.
DR OrthoDB; 455777at2759; -.
DR Proteomes; UP000077202; Unassembled WGS sequence.
DR GO; GO:0016020; C: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: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 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; PTHR47946:SF6; CYTOCHROME P450 78A7; 1.
DR PANTHER; PTHR47946; CYTOCHROME P450 78A7-RELATED; 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}; Iron {ECO:0000256|RuleBase:RU000461};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|RuleBase:RU000461};
KW Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW Reference proteome {ECO:0000313|Proteomes:UP000077202};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..23
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 35..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 537 AA; 59831 MW; 85BEBA72DB06F862 CRC64;
MSIDGVMSGG AGGFWMFALP LLTKGGRSTL NEQGHCGMTI LTLGVICAFI LLLFWAGPGG
AAWALYRGRK PIPGPRGFPI VGSLMDMGSK AHRTLSELAE IHCAKRLMAL SMGSTRLIVA
STPASAREIL HSTAFSDRPI KQSAQQLLFA RAIGFAPHGE YWRRLRRIAA NHLFSPKRIT
AHEPSRQQEF KRVIGFLHEQ IQERPDETVQ IRSYLQHAAL NNIMGGVFGR LYDFQSSEGI
QLKEMVREGF ELLGAFNWAD HLPLLQPFDP QNIHQRCSEL VIKVVAFVQN IIDEHRSRGA
SSEDCSAYGD FVDILLGMQG EDKLSDADMI SVLWEMIFRG TDTTAILTEW VMAELVKNPE
IQARLRNELR SIVGDEDNVS ESHISRASFL QAVVKETLRL HPPGPLLSWA RLSNRDVNIA
GHFVPAGTTA MVNMWSITHD PKVWERPLEF RPERFVVADG GIDFDVKGSD LRLAPFGAGR
RVCPGRALGM ATVQMWVAKL VMEFEWRSSP EHGVCLDEVL KLSSEMRIPL TVCLTKL
//
