ID A0A087GK54_ARAAL Unreviewed; 520 AA.
AC A0A087GK54;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Ferulate-5-hydroxylase {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=AALP_Aa7g237600 {ECO:0000313|EMBL:KFK30256.1};
OS Arabis alpina (Alpine rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Arabideae; Arabis.
OX NCBI_TaxID=50452 {ECO:0000313|EMBL:KFK30256.1, ECO:0000313|Proteomes:UP000029120};
RN [1] {ECO:0000313|Proteomes:UP000029120}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Pajares {ECO:0000313|Proteomes:UP000029120};
RX PubMed=27246759; DOI=10.1038/nplants.2014.23;
RA Willing E.M., Rawat V., Mandakova T., Maumus F., James G.V.,
RA Nordstroem K.J., Becker C., Warthmann N., Chica C., Szarzynska B.,
RA Zytnicki M., Albani M.C., Kiefer C., Bergonzi S., Castaings L.,
RA Mateos J.L., Berns M.C., Bujdoso N., Piofczyk T., de Lorenzo L.,
RA Barrero-Sicilia C., Mateos I., Piednoel M., Hagmann J., Chen-Min-Tao R.,
RA Iglesias-Fernandez R., Schuster S.C., Alonso-Blanco C., Roudier F.,
RA Carbonero P., Paz-Ares J., Davis S.J., Pecinka A., Quesneville H.,
RA Colot V., Lysak M.A., Weigel D., Coupland G., Schneeberger K.;
RT "Genome expansion of Arabis alpina linked with retrotransposition and
RT reduced symmetric DNA methylation.";
RL Nat. Plants 1:14023-14023(2015).
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|RuleBase:RU000461}.
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DR EMBL; CM002875; KFK30256.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087GK54; -.
DR EnsemblPlants; KFK30256; KFK30256; AALP_AA7G237600.
DR Gramene; KFK30256; KFK30256; AALP_AA7G237600.
DR eggNOG; KOG0156; Eukaryota.
DR OMA; LPCLDDQ; -.
DR OrthoDB; 368727at2759; -.
DR Proteomes; UP000029120; Chromosome 7.
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 GO; GO:0009809; P:lignin biosynthetic process; IEA:EnsemblPlants.
DR GO; GO:0010224; P:response to UV-B; IEA:EnsemblPlants.
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; PTHR47945; CYTOCHROME P450 84A1-RELATED; 1.
DR PANTHER; PTHR47945:SF5; CYTOCHROME P450 84A1-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:UP000029120};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 520 AA; 58655 MW; 01FC30EEA96C4E4D CRC64;
MEFSISQTLS KVLDPTTAVL IVVSLFIFIG LISRRRRLPY PPGPGGWPII GNMLMMDQLT
HRGLASLAKK YGGLCHLRMG FLHMFAVSSP EVAKQVLQVQ DSIFSNRPAT IAISYLTYDR
ADMAFAHYGP FWRQMRKVCV MKVFSRKRAE SWASVRDEVD KMVRSVSSNV GKPINVGEQI
FALTRNITYR AAFGSACITG QDEFIRILQE FSKLFGAFNV ADFIPYFGWI DPQGINKRLV
KARNDLDGFI DEIIDEHMKK KEDQNTVDDG DIVDTDMVDD LLTFYSEEAK LVSEATDLQN
SIKLTRDNIK AIIMDVMFGG TETVASAIEW ALTELLRSPE DLKRVQQELA DVVGLDRRVE
ESDIEKLTFL KCTLKETLRL HPPIPLLLHE TSEDAEIDGY YVPKRSRIMI NAFAIGRDPK
SWVDPDTFRP ARFLEPGVPD FKGSNFEFIP FGSGRRSCPG MQLGLYALDL AVAHILHCFT
WELPDGMKPN DLDMSDVFGL TAPKATRLFA VPITRLTCDV
//