CYBT1_CATRO
ID CYBT1_CATRO Reviewed; 512 AA.
AC W8JCE8;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 14-MAY-2014, sequence version 1.
DT 03-AUG-2022, entry version 14.
DE RecName: Full=Cytochrome P450 71BT1 {ECO:0000303|PubMed:24710322};
DE Short=CrCYP71BT1 {ECO:0000303|PubMed:24710322};
DE EC=1.14.-.- {ECO:0000305};
DE Flags: Precursor;
GN Name=CYP71BT1 {ECO:0000303|PubMed:24710322};
GN Synonyms=CYP71B34 {ECO:0000305}; ORFNames=Caros004638 {ECO:0000305};
OS Catharanthus roseus (Madagascar periwinkle) (Vinca rosea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Gentianales; Apocynaceae; Rauvolfioideae; Vinceae;
OC Catharanthinae; Catharanthus.
OX NCBI_TaxID=4058;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Little Bright Eyes;
RX PubMed=24710322; DOI=10.1038/ncomms4606;
RA Miettinen K., Dong L., Navrot N., Schneider T., Burlat V., Pollier J.,
RA Woittiez L., van der Krol S., Lugan R., Ilc T., Verpoorte R.,
RA Oksman-Caldentey K.M., Martinoia E., Bouwmeester H., Goossens A.,
RA Memelink J., Werck-Reichhart D.;
RT "The seco-iridoid pathway from Catharanthus roseus.";
RL Nat. Commun. 5:3606-3606(2014).
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=ORCAE database;
CC URL="https://bioinformatics.psb.ugent.be/orcae/overview/Catro";
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DR EMBL; KF302073; AHK60840.1; -; mRNA.
DR AlphaFoldDB; W8JCE8; -.
DR SMR; W8JCE8; -.
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; -; 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 Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase;
KW Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..512
FT /note="Cytochrome P450 71BT1"
FT /id="PRO_0000446414"
FT BINDING 447
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:0000250|UniProtKB:P04798"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 512 AA; 58923 MW; 237A71DB3BF07ADA CRC64;
MENLFIFLFA LLLFCFMLLK LSKKYSALKL PPGPRPLPII GNLHQIGGGL MHHILREMAR
TYGPLFRIKF GQVSTIVVSS PEIAKEIFRT HDVVFSYRPQ NIAVFNVMTY NFSNIAFAPY
GNYWRQMRKI CVMEILGASR VRSFGSIRQE EVMNLIRFVG SHKGKLVNVS EKIYGLTYSI
TARAAFGKVS KYQQVFKEHM DKYDDLARGL DIADFYPSMK FLRLVTGMER KLKVMFKEVD
EILQVIIDEH RDQRMKKIRS KVDDNEKEEE EGNEDIVDVL MNLQQSGQTE LPVTDDNIKA
VILDIFGAGG DTTAATLEWA LAESLKNKQV LKRAQEELRT IFHSKRNVDE SGFNQLKYLP
AIVKETLRLH PPAPLSLPRE CSEECNIYGY DIPAKTRVMV NIWAMGRDPK YWSEPEEFKP
ERFIDSRIDY KGNDFEYIPF GAGRRICPGM SFAIPNVALP LAQLLFHFDW KVDDDAGKLE
DLDMVEHPVL EARRKNELKL IPVIYEGSCL KN