ID   C0KHL8_9POAL            Unreviewed;       507 AA.
AC   C0KHL8;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Putative ferulate 5-hydroxylase {ECO:0000313|EMBL:ACM69384.1};
GN   Name=F5H2 {ECO:0000313|EMBL:ACM69384.1};
OS   Phyllostachys praecox.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Bambusoideae; Arundinarodae; Arundinarieae; Arundinariinae; Phyllostachys.
OX   NCBI_TaxID=326921 {ECO:0000313|EMBL:ACM69384.1};
RN   [1] {ECO:0000313|EMBL:ACM69384.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Yang X., Peng Z., Gao Z., Li X.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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; FJ604600; ACM69384.1; -; mRNA.
DR   AlphaFoldDB; C0KHL8; -.
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   CDD; cd11072; CYP71-like; 1.
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; PTHR47954:SF2; OS09G0275400 PROTEIN; 1.
DR   PANTHER; PTHR47954; OS09G0275400 PROTEIN-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   2: Evidence at transcript level;
KW   Heme {ECO:0000256|RuleBase:RU000461}; Iron {ECO:0000256|RuleBase:RU000461};
KW   Membrane {ECO:0000256|ARBA:ARBA00022989};
KW   Metal-binding {ECO:0000256|RuleBase:RU000461};
KW   Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
SQ   SEQUENCE   507 AA;  56282 MW;  DC682067AEA2A6A7 CRC64;
     MDEFFFQSLL LSVVAVALLQ LVKVALRPRP RMPPGPWKLP VIGSMHHLVN VLPHRALKDM
     ADVHGPLMML QLGETPLVVA SSKETAREVL KTHDTNFATR PKLLAGEIVG YEWADILFSP
     SGDYWRKLRQ LCAAEILSPK RVLSFRHIRE EEVMMRVEEV RAAGPSTPVN LSVMFHTLTN
     SIVSRAAFGK KRKNAPEFLA AIKAGVGLSS GFNIPDLFPT WTAVLATVTG MKRSLQDIHR
     TVDSILEDII EERKGVRDEK IKSGADNVEE NLVDVLITLQ EKGGFGFHLD NSRIKAIILD
     MFAGGTGTSA SALEWGMSEL MRNPEVMKKL QGQIREAFRG KAVVTEGDLQ TSNLRYLKLV
     IKEALRLHPP APLLVPRESI DVCELDGYTI PAKSRVIINA WAIGRDPRYW DDAEEFKPER
     FEEGTVDFMG SSYEFIPFGS GRRMCPGFNY GLASMELALV GLLYHFDWSL PEGVAELDMA
     EAPGLGVRRR SPLLLCATPF VPAVSAA
//