NEC1_NESMA
ID NEC1_NESMA Reviewed; 276 AA.
AC P0DO50;
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=Carbonic anhydrase Nec1 {ECO:0000303|PubMed:35074876};
DE EC=4.2.1.1 {ECO:0000269|PubMed:35074876};
DE AltName: Full=Nectar protein 1 {ECO:0000303|PubMed:35074876};
DE Short=NmNec1 {ECO:0000303|PubMed:35074876};
DE Flags: Precursor;
GN Name=NEC1 {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 NEC2 and NEC3, 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). Mediates the alkalinization (pH
CC increase) of the flower nectar by catalyzing the reversible hydration
CC of carbon dioxide (PubMed:35074876). {ECO:0000269|PubMed:35074876}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hydrogencarbonate = CO2 + H2O; Xref=Rhea:RHEA:10748,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:17544; EC=4.2.1.1;
CC Evidence={ECO:0000269|PubMed:35074876};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10749;
CC Evidence={ECO:0000269|PubMed:35074876};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q50940};
CC -!- PATHWAY: One-carbon metabolism. {ECO:0000269|PubMed:35074876}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q50940}.
CC -!- TISSUE SPECIFICITY: Confined to nectaries.
CC {ECO:0000269|PubMed:35074876}.
CC -!- SIMILARITY: Belongs to the alpha-class carbonic anhydrase family.
CC {ECO:0000305}.
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DR EMBL; OK664972.1; UIE54576.1; -; mRNA.
DR PROSITE; PS00162; ALPHA_CA_1; 1.
DR PROSITE; PS51144; ALPHA_CA_2; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Lyase; Metal-binding; Signal; Zinc.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..276
FT /note="Carbonic anhydrase Nec1"
FT /id="PRO_0000456308"
FT DOMAIN 34..270
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT REGION 216..217
FT /note="Substrate binding"
FT /evidence="ECO:0000250|UniProtKB:Q50940"
FT ACT_SITE 98
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 59..220
FT /evidence="ECO:0000250|UniProtKB:Q50940"
SQ SEQUENCE 276 AA; 31559 MW; 1DC27C6A301B392D CRC64;
MKMINSIFTH GSLIILLLLF HSISIKAQEV DDEREFDYLE GSELGPEKWG ELRPEWGTCK
RGKMQSPIDI SNPVQVTSKE LLQTKYKAQN AIINNRGHDI MVRWEGDAGS ILINEREFDL
LQAHWHAPSE HAINGTRYAM ELHMLHRSTD PKLTPTMVVV AVFYEIGDVD PFLSRLGPIM
SSLIDQTNEH KQAGVINPME IQLDDECYYK YIGSLTTPSC TEGVTWIINK RINTVSSDQV
KLLREAVHDH AKNNARPLQA LNHREVQLHC HKDRKD
