NR_NARAP
ID NR_NARAP Reviewed; 257 AA.
AC A0A1C9II22;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2016, sequence version 1.
DT 03-AUG-2022, entry version 15.
DE RecName: Full=Noroxomaritidine/norcraugsodine reductase {ECO:0000303|PubMed:27252378};
DE Short=NorRed {ECO:0000305};
DE EC=1.1.1.- {ECO:0000269|PubMed:27252378};
GN Name=NR {ECO:0000303|PubMed:27252378};
OS Narcissus aff. pseudonarcissus MK-2014 (Daffodil).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Amaryllidaceae;
OC Amaryllidoideae; Narcissus.
OX NCBI_TaxID=1540222;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=27252378; DOI=10.1074/jbc.m116.717827;
RA Kilgore M.B., Holland C.K., Jez J.M., Kutchan T.M.;
RT "Identification of a noroxomaritidine reductase with amaryllidaceae
RT alkaloid biosynthesis related activities.";
RL J. Biol. Chem. 291:16740-16752(2016).
CC -!- FUNCTION: In the Amaryllidaceae alkaloids biosynthesic pathway,
CC catalyzes the conversion of noroxomaritidine to oxomaritidine, a
CC precursor of haemanthamine- and crinamine-type alkaloids, promising
CC anticancer agents (PubMed:27252378). Can also, to some extent, catalyze
CC the condensation of 3,4-dihydroxybenzaldehyde (3,4-DHBA) and tyramine
CC to produce norbelladine, and of isovanillin and tyramine to produce 4'-
CC O-methylnorbelladine (PubMed:27252378). {ECO:0000269|PubMed:27252378}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(10bR,4aS)-noroxomaritidine + H(+) + NADPH = (10bR,4aS)-
CC oxomaritidine + NADP(+); Xref=Rhea:RHEA:63196, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133995,
CC ChEBI:CHEBI:146208; Evidence={ECO:0000269|PubMed:27252378};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63197;
CC Evidence={ECO:0000269|PubMed:27252378};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(10bS,4aR)-noroxomaritidine + H(+) + NADPH = (10bS,4aR)-
CC oxomaritidine + NADP(+); Xref=Rhea:RHEA:63200, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133996,
CC ChEBI:CHEBI:146209; Evidence={ECO:0000269|PubMed:27252378};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63201;
CC Evidence={ECO:0000269|PubMed:27252378};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6. {ECO:0000269|PubMed:27252378};
CC Temperature dependence:
CC Optimum temperature is 35 degrees Celsius.
CC {ECO:0000269|PubMed:27252378};
CC -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:27252378}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. SDR65C subfamily. {ECO:0000305}.
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DR EMBL; KU295569; AOP04255.1; -; mRNA.
DR AlphaFoldDB; A0A1C9II22; -.
DR SMR; A0A1C9II22; -.
DR KEGG; ag:AOP04255; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0009820; P:alkaloid metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR InterPro; IPR045000; TR.
DR PANTHER; PTHR42898; PTHR42898; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW Alkaloid metabolism; NADP; Oxidoreductase.
FT CHAIN 1..257
FT /note="Noroxomaritidine/norcraugsodine reductase"
FT /id="PRO_0000450650"
FT ACT_SITE 161
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 15..39
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P50162"
FT BINDING 20..23
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:A0A1A9TAK5"
FT BINDING 42..43
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:A0A1A9TAK5"
FT BINDING 68..69
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:A0A1A9TAK5"
FT BINDING 96..98
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:A0A1A9TAK5"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1A9TAK5"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P50162"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1A9TAK5"
FT BINDING 161
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:A0A1A9TAK5"
FT BINDING 165
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:A0A1A9TAK5"
FT BINDING 194..199
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:A0A1A9TAK5"
SQ SEQUENCE 257 AA; 27605 MW; 109567013CC857F8 CRC64;
MSLEKRWSLE GTTALVTGGT KGIGHAIVEE LVGFGARVYT CSRNEAELRK CLQEWENLKY
DVTGSVCDVS SRTEREKLAE EVSSVFNGKL NILINNAGGY VNKPIDGFTA EDFSFLVAVN
LESAFHLCQL AHPMLKASGT GSIVHISSCC AQIAIPGHSI YSSTKGAINQ LTRNLACEWA
KDNIRTNSIA PGAIRTPGTE SFVIDKDALD REVSRVPFGR IGEPEEVASL AAFLCMPSAS
YITGQVICVD GGRTING
