C72A1_CATRO
ID C72A1_CATRO Reviewed; 524 AA.
AC Q05047;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Secologanin synthase;
DE Short=SLS;
DE EC=1.14.19.62 {ECO:0000269|PubMed:11135113};
DE AltName: Full=CYPLXXII;
DE AltName: Full=Cytochrome P450 72A1;
GN Name=CYP72A1; Synonyms=CYP72, P450CR3;
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. CP3A;
RX PubMed=16653087; DOI=10.1104/pp.100.2.998;
RA Vetter H.-P., Mangold U., Schroeder G., Marner F.-J., Werck-Reichhart D.,
RA Schroeder J.;
RT "Molecular analysis and heterologous expression of an inducible cytochrome
RT P-450 protein from periwinkle (Catharanthus roseus L.).";
RL Plant Physiol. 100:998-1007(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 469-524.
RC STRAIN=cv. G. Don;
RX PubMed=8507838; DOI=10.1007/bf00014944;
RA Meijer A.H., Souer E., Verpoorte R., Hoge J.H.C.;
RT "Isolation of cytochrome P-450 cDNA clones from the higher plant
RT Catharanthus roseus by a PCR strategy.";
RL Plant Mol. Biol. 22:379-383(1993).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. CP3A;
RX PubMed=11135113; DOI=10.1046/j.1365-313x.2000.00922.x;
RA Irmler S., Schroeder G., St Pierre B., Crouch N.P., Hotze M., Schmidt J.,
RA Strack D., Matern U., Schroeder J.;
RT "Indole alkaloid biosynthesis in Catharanthus roseus: new enzyme activities
RT and identification of cytochrome P450 CYP72A1 as secologanin synthase.";
RL Plant J. 24:797-804(2000).
CC -!- FUNCTION: Converts loganin into secologanin.
CC {ECO:0000269|PubMed:11135113}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=loganin + O2 + reduced [NADPH--hemoprotein reductase] = H(+) +
CC 2 H2O + oxidized [NADPH--hemoprotein reductase] + secologanin;
CC Xref=Rhea:RHEA:20585, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:15771, ChEBI:CHEBI:18002, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210; EC=1.14.19.62;
CC Evidence={ECO:0000269|PubMed:11135113};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- PATHWAY: Alkaloid biosynthesis; secologanin biosynthesis.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000305}. Note=Tonoplast.
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Upper and lower leaf epidermis.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; L10081; AAA33106.1; -; mRNA.
DR EMBL; X69775; CAA49430.1; -; mRNA.
DR PIR; S35168; S35168.
DR PIR; T09944; T09944.
DR AlphaFoldDB; Q05047; -.
DR SMR; Q05047; -.
DR KEGG; ag:AAA33106; -.
DR BRENDA; 1.14.19.62; 1211.
DR UniPathway; UPA00328; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
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:0050616; F:secologanin synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0009820; P:alkaloid metabolic process; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW Alkaloid metabolism; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Transmembrane; Transmembrane helix; Vacuole.
FT CHAIN 1..524
FT /note="Secologanin synthase"
FT /id="PRO_0000052124"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 470
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"
FT VARIANT 190
FT /note="I -> L"
FT VARIANT 194
FT /note="Q -> E"
FT VARIANT 223
FT /note="E -> D"
FT VARIANT 312
FT /note="K -> R"
FT VARIANT 318
FT /note="S -> T"
FT VARIANT 403
FT /note="V -> I"
FT VARIANT 405
FT /note="K -> E"
FT VARIANT 411
FT /note="S -> P"
SQ SEQUENCE 524 AA; 60558 MW; EF5D864E43C751E8 CRC64;
MEMDMDTIRK AIAATIFALV MAWAWRVLDW AWFTPKRIEK RLRQQGFRGN PYRFLVGDVK
ESGKMHQEAL SKPMEFNNDI VPRLMPHINH TINTYGRNSF TWMGRIPRIH VMEPELIKEV
LTHSSKYQKN FDVHNPLVKF LLTGVGSFEG AKWSKHRRII SPAFTLEKLK SMLPAFAICY
HDMLTKWEKI AEKQGSHEVD IFPTFDVLTS DVISKVAFGS TYEEGGKIFR LLKELMDLTI
DCMRDVYIPG WSYLPTKRNK RMKEINKEIT DMLRFIINKR MKALKAGEPG EDDLLGVLLE
SNIQEIQKQG NKKDGGMSIN DVIEECKLFY FAGQETTGVL LTWTTILLSK HPEWQERARE
EVLQAFGKNK PEFERLNHLK YVSMILYEVL RLYPPVIDLT KIVHKDTKLG SYTIPAGTQV
MLPTVMLHRE KSIWGEDAME FNPMRFVDGV ANATKNNVTY LPFSWGPRVC LGQNFALLQA
KLGLAMILQR FKFDVAPSYV HAPFTILTVQ PQFGSHVIYK KLES
