NEC3_NESMA
ID NEC3_NESMA Reviewed; 558 AA.
AC P0DO52;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 03-AUG-2022, sequence version 1.
DT 03-AUG-2022, entry version 1.
DE RecName: Full=Sinalpyl alcohol oxidase Nec3 {ECO:0000303|PubMed:35074876};
DE EC=1.1.3.- {ECO:0000250|UniProtKB:P52707};
DE AltName: Full=Nectar protein 3 {ECO:0000303|PubMed:35074876};
DE Short=NmNec3 {ECO:0000303|PubMed:35074876};
DE Flags: Precursor;
GN Name=NEC3 {ECO:0000303|PubMed:35074876};
OS Nesocodon mauritianus (Blue Mauritius bellflower) (Wahlenbergia
OS mauritiana).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Campanulaceae; Nesocodon.
OX NCBI_TaxID=519296;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP TISSUE SPECIFICITY.
RX PubMed=35074876; DOI=10.1073/pnas.2114420119;
RA Roy R., Moreno N., Brockman S.A., Kostanecki A., Zambre A., Holl C.,
RA Solhaug E.M., Minami A., Snell-Rood E.C., Hampton M., Bee M.A., Chiari Y.,
RA Hegeman A.D., Carter C.J.;
RT "Convergent evolution of a blood-red nectar pigment in vertebrate-
RT pollinated flowers.";
RL Proc. Natl. Acad. Sci. U.S.A. 119:0-0(2022).
CC -!- FUNCTION: Involved in the production of blood-red nectar containing the
CC alkaloid nesocodin and that serves as a visual attractant for
CC pollinator visitation, including vertebrates such as Phelsuma geckos
CC (PubMed:35074876). The nectar is initially acidic and pale yellow, but
CC slowly becomes alkaline before turning into red within 24 hours
CC (PubMed:35074876). Together with NEC1 and NEC2, facilitates the
CC condensation of sinapaldehyde ((E)-3,5-dimethoxy-4-
CC hydroxycinnamaldehyde) and proline to form nesocodin, a pigment with a
CC stable imine bond (PubMed:35074876). Catalyzes the conversion of
CC sinapyl alcohol to sinapaldehyde (PubMed:35074876).
CC {ECO:0000269|PubMed:35074876}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-sinapyl alcohol + O2 = (E)-sinapaldehyde + H2O2;
CC Xref=Rhea:RHEA:72031, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:27949, ChEBI:CHEBI:64557;
CC Evidence={ECO:0000269|PubMed:35074876};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72032;
CC Evidence={ECO:0000269|PubMed:35074876};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q945K2};
CC -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:35074876}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q945K2}.
CC -!- TISSUE SPECIFICITY: Confined to nectaries.
CC {ECO:0000269|PubMed:35074876}.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
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DR EMBL; OK664974.1; UIE54578.1; -; mRNA.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; FAD; Flavoprotein; Glycoprotein; Oxidoreductase; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..558
FT /note="Sinalpyl alcohol oxidase Nec3"
FT /id="PRO_0000456307"
FT ACT_SITE 493
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q945K2"
FT ACT_SITE 531
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q945K2"
FT BINDING 64..65
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q945K2"
FT BINDING 83..84
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q945K2"
FT BINDING 131
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q945K2"
FT BINDING 135
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q945K2"
FT BINDING 139..142
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q945K2"
FT BINDING 247
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q945K2"
FT BINDING 492..493
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q945K2"
FT BINDING 532..533
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q945K2"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 386
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 473
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 433..484
FT /evidence="ECO:0000250|UniProtKB:Q945K2"
SQ SEQUENCE 558 AA; 60778 MW; B01B6E89571F8527 CRC64;
MATMAILQRT FSFILIFSIA LHLKSLFAME TDSGAELKYL ELIHEANEFT PDEEYDYIVV
GGGTAGCPLA ATLSENYSVL VLERGGDQHS HPNIIRQENV ANNALPADDE NSPSQAFTSE
DGVPGLVRGR VLGGSSMINF GFYSRGDDYF FKNTGIEWDM DSVKTAYEWV EETLVHRPDN
VSTWESSVRD ALLEVGVLPD NGNTLDHLVG TKVSGSTFDS TGNRHGAVEL LNKANPNNLR
VIVHATVDRI IFSSSESSGP SVVRVVYHDS HGKSYQVGIR ENGEVILSAG AFGSPQLLLV
SGVGPSQNLT SLEIPVVHDQ PFVGQYMIDN PRINLALMLP FSVVDSGTPV VGITGKGSYI
ETTSSSTPFT SPVSPLYFPY PYPPVNISMG YFFGKVSNPT SAGSLWLKSP SDVAITPSVR
FNYFSKPEDV HQCADAVATY EKILKTKAME MYKFKDHGGE KYFQIVGRQI PENTSDFESM
ATYCRKTVTT FYHYCGGCTV NKVVDSNLKV VGIGGLRVVD NSVFTSSPGT NPQATTMMLG
RYMGVKIQQE RAGSDGDN
