CYQ32_CATRO
ID CYQ32_CATRO Reviewed; 499 AA.
AC W8JMU7;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 14-MAY-2014, sequence version 1.
DT 03-AUG-2022, entry version 21.
DE RecName: Full=Cytochrome P450 81Q32 {ECO:0000303|PubMed:24710322};
DE Short=CrCYP81Q32 {ECO:0000303|PubMed:24710322};
DE EC=1.14.-.- {ECO:0000305};
GN Name=CYP81Q32 {ECO:0000303|PubMed:24710322};
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], AND TISSUE SPECIFICITY.
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in leaf epidermis and in the leaf
CC internal phloem-associated parenchyma (IPAP) inside the mesophyll.
CC {ECO:0000269|PubMed:24710322}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; KF302070; AHK60837.1; -; mRNA.
DR AlphaFoldDB; W8JMU7; -.
DR SMR; W8JMU7; -.
DR GO; GO:0016021; C:integral component of 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 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; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Transmembrane; Transmembrane helix.
FT CHAIN 1..499
FT /note="Cytochrome P450 81Q32"
FT /id="PRO_0000446416"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 434
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 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 499 AA; 56111 MW; 3C248F0B64AF908D CRC64;
MESSTLLYTF LAVVLLSISL KLFPVSRRRR NLPPSPGLAL PVIGHLHLIG KLLHRSLYDL
SKKYGSVFSL QLGNRLVLVV SSPAAAEECF TKNDIVFANR PLFILGKYIG YNYTTMVGSP
YGEHWRNLRR LAAVEIFSAG SLNRFLSIRE DEVKQLLLSL YQSSGQDFGK VEMKSKLSEL
SFNVTMRMVA GKRYFGQDVD SDEAKLFRAL IGEVFEHAGA SNPGDFVPFL RWIDFKNYEK
KVSKISQEMD AFLQRLIHES RINKNNVTMI DHLLSLQESQ PEYYTDQIIK GIIMVLLLAG
TDTSAVTVEW AMSLLLNHPE TLEKARTEIE TQVGSNRLIE EQDLPKLTYL HNIISETFRL
CPAAPMLVPH ESSDDCKVQG YDVPKGTILL VNAWAIHRDP EFWDEPTLFK PERHGGVELE
PSKLMPFGMG RRSCPGSGLA QRVVGLTLGA LIQCFEWKRI GEAKIDMAEG SGLTMPKAQP
LEALCKPRNI LHKVVSETS