ID A0A176W8Z1_MARPO Unreviewed; 587 AA.
AC A0A176W8Z1;
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=Cytochrome P450 {ECO:0008006|Google:ProtNLM};
GN ORFNames=AXG93_1335s1280 {ECO:0000313|EMBL:OAE28636.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE28636.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE28636.1, 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:OAE28636.1};
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|PIRSR:PIRSR602403-1};
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:OAE28636.1}.
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DR EMBL; LVLJ01001708; OAE28636.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A176W8Z1; -.
DR OrthoDB; 5479414at2759; -.
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:InterPro.
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; 2.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24282:SF258; CYTOCHROME P450; 1.
DR PANTHER; PTHR24282; CYTOCHROME P450 FAMILY MEMBER; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|PIRSR:PIRSR602403-1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR602403-1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR602403-1};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023033};
KW Reference proteome {ECO:0000313|Proteomes:UP000077202};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 83..112
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 516
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:0000256|PIRSR:PIRSR602403-1"
SQ SEQUENCE 587 AA; 65698 MW; 90F8DAA3B9BC43F5 CRC64;
MLLKLVASSR VLGDGGRQFG MELISTSPLL RATTISTTTT AEVVRDDSSR RLFKEVILTE
VRQAGRRGNS TGPLEKMMTA VEIIGSLGGL GWIATVVGSV LLLLSILYLG IWRPYKLHTF
YKSLHVKGPP HRPLVGNLAD IWTLQRQVTR IKWETADPAN LAARTLPHLT YWAKLYGRMF
TYTEGAKVNL CVLDTEIIRE LLVLKADCYR RSPSGWLWRN SHGASRQSKQ DIIDNKMIHC
EPERWSTLRR ILGPGSDKDH VQDCLQTIVE ISRTLIRNWD MQLTEASTSR VTVEARREIK
KISMEMLLTN LIGSTMTADQ LEELHSNFGE DEEDPVTTTD LLKAHFSRIR RSSTLDVQKL
VADCQMMVAA QKATTQLISQ TLQLLARHPD WQTQARAEVL EVRPLDSPTD DDGDSIPNST
YPKLAKLKVM NMILNESLRL FPPILSTEKL CEKRHRLGKY TVLPGTFVQV PIVLLHHSPE
LWGDDALSFR PDRFEHGAGA RRPFALLPFS AGPSVCLGYN FALLEAKIVL ASVLRSFHFS
PAPSTDPSPS PSPSAAASSC LLIRKLASDD VATAARQRLT RRHTSFL
//
