C71A5_GELSE
ID C71A5_GELSE Reviewed; 501 AA.
AC P0DO14;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 13-FEB-2019, sequence version 1.
DT 03-AUG-2022, entry version 8.
DE RecName: Full=Sarpagan bridge enzyme {ECO:0000303|PubMed:29942076};
DE Short=GsSBE {ECO:0000303|PubMed:29942076};
DE EC=1.14.14.- {ECO:0000269|PubMed:29942076};
DE AltName: Full=Cytochrome P450 71AY5 {ECO:0000303|PubMed:29942076};
GN Name=CYP71AY5 {ECO:0000303|PubMed:29942076};
OS Gelsemium sempervirens (Carolina jasmine) (Bignonia sempervirens).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Gentianales; Gelsemiaceae; Gelsemium.
OX NCBI_TaxID=28542;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=29942076; DOI=10.1038/s41589-018-0078-4;
RA Dang T.T., Franke J., Carqueijeiro I.S.T., Langley C., Courdavault V.,
RA O'Connor S.E.;
RT "Sarpagan bridge enzyme has substrate-controlled cyclization and
RT aromatization modes.";
RL Nat. Chem. Biol. 14:760-763(2018).
CC -!- FUNCTION: Involved in monoterpene indole alkaloids (MIAs) biosynthesis
CC (PubMed:29942076). Converts by cyclization the strictosidine-derived
CC geissoschizine to the sarpagan alkaloid polyneuridine aldehyde
CC (PubMed:29942076). Converts by aromatization the tetrahydro-beta-
CC carboline alkaloids tetrahydroalstonine and ajmalicine to the
CC corresponding beta-carboline alkaloids alstonine and serpentine,
CC respectively (PubMed:29942076). {ECO:0000269|PubMed:29942076}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(19S)-geissoschizine + O2 + reduced [NADPH--hemoprotein
CC reductase] = H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase] +
CC polyneuridine aldehyde; Xref=Rhea:RHEA:58124, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16829, ChEBI:CHEBI:17037,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:29942076};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + O2 + reduced [NADPH--hemoprotein reductase] +
CC tetrahydroalstonine = AH2 + alstonine + H(+) + 2 H2O + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:58128, Rhea:RHEA-
CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:17499, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:142526, ChEBI:CHEBI:142530;
CC Evidence={ECO:0000269|PubMed:29942076};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + ajmalicine + O2 + reduced [NADPH--hemoprotein reductase] =
CC AH2 + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase] +
CC serpentine; Xref=Rhea:RHEA:58132, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:142527, ChEBI:CHEBI:142531;
CC Evidence={ECO:0000269|PubMed:29942076};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q96242};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=35.3 uM for geissoschizine {ECO:0000269|PubMed:29942076};
CC -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P0DO13}; Single-pass type II membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Highly expressed in roots (PubMed:29942076).
CC Expressed at low levels in stems (PubMed:29942076).
CC {ECO:0000269|PubMed:29942076}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; MF537712; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; P0DO14; -.
DR SMR; P0DO14; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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 1: Evidence at protein level;
KW Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Transmembrane; Transmembrane helix.
FT CHAIN 1..501
FT /note="Sarpagan bridge enzyme"
FT /id="PRO_0000446227"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 441
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:Q96242"
SQ SEQUENCE 501 AA; 56593 MW; 4E71D9CBADBE0C38 CRC64;
MEVMQLSFSY PALFLFVFFL FMLVKQLRRP KNLPPGPNKL PIIGNLHQLA TELPHHTLKQ
LADKYGPIMH LQFGEVSAII VSSAKLAKVF LGNHGLAVAD RPKTMVATIM LYNSSGVTFA
PYGDYWKHLR QVYAVELLSP KSVRSFSMIM DEEISLMLKR IQSNAAGQPL KVHDEMMTYL
FATLCRTSIG SVCKGRDLLI DTAKDISAIS AAIRIEELFP SLKILPYITG LHRQLGKLSK
RLDGILEDII AQREKMQESS TGDNDERDIL GVLLKLKRSN SNDTKVRIRN DDIKAIVFEL
ILAGTLSTAA TVEWCLSELK KNPGAMKKAQ DEVRQVMKGE TICTNDVQKL EYIRMVIKET
FRMHPPAPLL FPRECREPIQ VEGYTIPEKS WLIVNYWAVG RDPELWNDPE KFEPERFRNS
PVDMSGNHYE LIPFGAGRRI CPGISFAATN AELLLASLIY HFDWKLPAGV KELDMDELFG
AGCVRKNPLH LIPKTVVPCQ D
