CYC13_CATRO
ID CYC13_CATRO Reviewed; 507 AA.
AC W8JIS9;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 14-MAY-2014, sequence version 1.
DT 03-AUG-2022, entry version 16.
DE RecName: Full=Cytochrome P450 81C13 {ECO:0000303|PubMed:24710322};
DE Short=CrCYP81C13 {ECO:0000303|PubMed:24710322};
DE EC=1.14.-.- {ECO:0000305};
DE Flags: Precursor;
GN Name=CYP81C13 {ECO:0000303|PubMed:24710322};
GN ORFNames=Caros008992 {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; KF302071; AHK60838.1; -; mRNA.
DR AlphaFoldDB; W8JIS9; -.
DR SMR; W8JIS9; -.
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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..507
FT /note="Cytochrome P450 81C13"
FT /id="PRO_0000446411"
FT BINDING 443
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 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 475
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 507 AA; 58975 MW; 9BF14F1BD755C8C5 CRC64;
MANFISFFIL FSALFFLFKR LFFPNRKQKL PPGPPSLPIV GHLHHIKTSL YQALARLSNE
YGPVIFLRFG CRSFVAVSSP SAIEECFTKN DIIFANRPKS MATDRLTFNY IGFAWAPYGQ
FWRIVRRFTV VEFFSTNCLG KSRPIREEEI QSILRSIFKI TKMKSEKIDL KHWVSVFTFN
VLMRTMADKW AVDEEDSGVE KGKEIMKELR EIFFTNVAMN VCDFFPIFRW FGYKGIEQRM
INLHNRRNEF LQGLVDKVRI NKKSGFVRNK ESHRSLIEAF LSHQDQDPEF FTDDLIKSVL
LIMFVAGTET SAVIIEWAMS LLLSNPDVLN KLRIEIDKQI GNKRLINESD IPKLPYLRCI
INETMRLFPP VPLLLPHCSS EDCKIAGYDI PKGTVLFVNA WATHRDPKLW DEPEKFIPER
FENMEVEKEG YKFIPFGIGR RACPGTSMGI RTVSLALGAF IQCFDWKKVE EYELNTSYDY
RITLQKANQL EASCSPRQDF FPILSQL