ID H9X9X6_PINTA Unreviewed; 77 AA.
AC H9X9X6;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Cytochrome P450 {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=0_16841_01 {ECO:0000313|EMBL:AFG71069.1};
OS Pinus taeda (Loblolly pine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC Pinus subgen. Pinus.
OX NCBI_TaxID=3352 {ECO:0000313|EMBL:AFG71069.1};
RN [1] {ECO:0000313|EMBL:AFG71069.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=6382 {ECO:0000313|EMBL:AFG71070.1}, 6383
RC {ECO:0000313|EMBL:AFG71069.1}, and 6384 {ECO:0000313|EMBL:AFG71066.1};
RC TISSUE=Megagametophyte {ECO:0000313|EMBL:AFG71069.1};
RA Neale D.B., Wegrzyn J.L., Lee J.M., Eckert A.J., Liechty J.D.,
RA Stevens K.A., Langley C.H.;
RT "Nucleotide Diversity and Divergence in the Loblolly Pine Gene Space.";
RL Submitted (AUG-2008) 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|RuleBase:RU000461}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FJ060661; AFG71066.1; -; Genomic_DNA.
DR EMBL; FJ060658; AFG71069.1; -; Genomic_DNA.
DR EMBL; FJ060654; AFG71070.1; -; Genomic_DNA.
DR AlphaFoldDB; H9X9X6; -.
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; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24286; CYTOCHROME P450 26; 1.
DR PANTHER; PTHR24286:SF232; CYTOCHROME P450 SUPERFAMILY PROTEIN; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|PIRSR:PIRSR602403-1, ECO:0000256|RuleBase:RU000461};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR602403-1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR602403-1};
KW Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461}.
FT BINDING 49
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"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFG71069.1"
FT NON_TER 77
FT /evidence="ECO:0000313|EMBL:AFG71069.1"
SQ SEQUENCE 77 AA; 8941 MW; 22F147A57B080EDF CRC64;
VVCVFSSATH LDEKFHNEAL TFNPWRWELD QDVSNNHLFS PFGGGARLCP GSHLARLELV
LFLHIFITRF RWEALDD
//
