C71A4_RAUSE
ID C71A4_RAUSE Reviewed; 503 AA.
AC P0DO13;
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=RsSBE {ECO:0000303|PubMed:29942076};
DE EC=1.14.14.- {ECO:0000269|PubMed:29942076};
DE AltName: Full=Cytochrome P450 71AY4 {ECO:0000303|PubMed:29942076};
GN Name=CYP71AY4 {ECO:0000303|PubMed:29942076};
OS Rauvolfia serpentina (Serpentine wood) (Ophioxylon serpentinum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Gentianales; Apocynaceae; Rauvolfioideae; Vinceae;
OC Rauvolfiinae; Rauvolfia.
OX NCBI_TaxID=4060;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
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=22.5 uM for geissoschizine {ECO:0000269|PubMed:29942076};
CC -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:29942076}; Single-pass type II membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Highly expressed in roots (PubMed:29942076).
CC Expressed at low levels in leaves, stems and flowers (PubMed:29942076).
CC {ECO:0000269|PubMed:29942076}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; MF537711; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; P0DO13; -.
DR SMR; P0DO13; -.
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..503
FT /note="Sarpagan bridge enzyme"
FT /id="PRO_0000446226"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 442
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 503 AA; 56236 MW; FF7D8BC77F32A419 CRC64;
MEISVTTSIA LATIVFFLYK LATRPKSTKK QLPEASRLPI IGHTLHQMVG SLPHRVLKNL
ADQYGPVMHL QIGELSAIVI SSADKAKEVL NTHGVLVADR PQTTVAKIML YNSLGATFAP
YGDYLKQLRQ IYALELLSPK TVRSFWTIME DELSTMVTSV KAEAGQPIVL HDKMLTYLYD
TLCRATVGSV CNGRETLIMA ARETSALSAA IRIEDLFPSV KILPVISGLK TRLTNLLKQL
DTVLEDIIGE REKKMFSSNN QPLTEEEDML GVLLMYKNGK GKDAKFRITN NDIKAIVWEL
ILAGTLSSAA IVEWCMSEMI KNPRVMKKAQ DEVRQVLKDK KTVSGSDLAK LEYVKMVVKE
SVRLHPPAPL LFPREVREDF EMDGMIIPKK SWVIINYWAV GTDPKTWHDA VKYEPERFSN
SSVDFYGSHF ELIPFGAGRR ICPGILFGTT NVELLLASFL YHFDWKLPGG MKPEELDMNE
LFGAGCVREN PLCLIPSISV AGN
