NEC3_NICLS
ID NEC3_NICLS Reviewed; 274 AA.
AC Q84UV8;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Bifunctional monodehydroascorbate reductase and carbonic anhydrase nectarin-3;
DE EC=1.6.5.4;
DE EC=4.2.1.1;
DE AltName: Full=Nectarin-III;
DE Contains:
DE RecName: Full=Nectarin-2;
DE Flags: Precursor;
GN Name=NEC3 {ECO:0000312|EMBL:AAO85482.1};
OS Nicotiana langsdorffii x Nicotiana sanderae (Ornamental tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=164110;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAO85482.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 26-36 AND 74-87, FUNCTION,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, PROTEOLYTIC
RP CLEAVAGE AT GLU-73, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15284496; DOI=10.1023/b:plan.0000036373.84579.13;
RA Carter C.J., Thornburg R.W.;
RT "Tobacco nectarin III is a bifunctional enzyme with monodehydroascorbate
RT reductase and carbonic anhydrase activities.";
RL Plant Mol. Biol. 54:415-425(2004).
CC -!- FUNCTION: Bifunctional enzyme which has both carbonate dehydratase and
CC monodehydroascorbate reductase activities. May be involved in
CC regulation of nectar pH. May also regulate nectar ascorbate
CC concentration, protecting floral tissues from free radical damage.
CC {ECO:0000269|PubMed:15284496}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + 2 monodehydro-L-ascorbate radical + NADH = 2 L-
CC ascorbate + NAD(+); Xref=Rhea:RHEA:14581, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:38290, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:59513; EC=1.6.5.4;
CC Evidence={ECO:0000269|PubMed:15284496};
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:15284496};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P00918};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15284496}.
CC Note=Found in the nectar.
CC -!- TISSUE SPECIFICITY: Expressed most strongly in nectary gland. Also at
CC lower levels in the ovary, style, stigma, floral tube and at low levels
CC in anthers/filaments. {ECO:0000269|PubMed:15284496}.
CC -!- DEVELOPMENTAL STAGE: Expressed at low levels in stage 2 nectaries.
CC Levels then increase and expression is even throughout subsequent
CC stages of nectary development. {ECO:0000269|PubMed:15284496}.
CC -!- PTM: Proteolytically cleaved to produce a shorter protein, nectarin-2.
CC {ECO:0000269|PubMed:15284496}.
CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC {ECO:0000255}.
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DR EMBL; AF492468; AAO85482.1; -; mRNA.
DR AlphaFoldDB; Q84UV8; -.
DR SMR; Q84UV8; -.
DR BRENDA; 1.6.5.4; 14563.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0004089; F:carbonate dehydratase activity; IDA:UniProtKB.
DR GO; GO:0016656; F:monodehydroascorbate reductase (NADH) activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0006885; P:regulation of pH; NAS:UniProtKB.
DR GO; GO:0000305; P:response to oxygen radical; NAS:UniProtKB.
DR CDD; cd03124; alpha_CA_prokaryotic_like; 1.
DR Gene3D; 3.10.200.10; -; 1.
DR InterPro; IPR041891; Alpha_CA_prokaryot-like.
DR InterPro; IPR001148; CA_dom.
DR InterPro; IPR036398; CA_dom_sf.
DR InterPro; IPR023561; Carbonic_anhydrase_a-class.
DR InterPro; IPR018338; Carbonic_anhydrase_a-class_CS.
DR PANTHER; PTHR18952; PTHR18952; 1.
DR Pfam; PF00194; Carb_anhydrase; 1.
DR SMART; SM01057; Carb_anhydrase; 1.
DR SUPFAM; SSF51069; SSF51069; 1.
DR PROSITE; PS00162; ALPHA_CA_1; 1.
DR PROSITE; PS51144; ALPHA_CA_2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Lyase; Metal-binding; NAD;
KW Oxidoreductase; Secreted; Signal; Zinc.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:15284496"
FT CHAIN 26..274
FT /note="Bifunctional monodehydroascorbate reductase and
FT carbonic anhydrase nectarin-3"
FT /id="PRO_0000248263"
FT CHAIN 74..274
FT /note="Nectarin-2"
FT /evidence="ECO:0000269|PubMed:15284496"
FT /id="PRO_0000248264"
FT DOMAIN 32..265
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT ACT_SITE 97
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 122
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
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 141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 211..212
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 73..74
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:15284496"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 274 AA; 31495 MW; 4E116CF99B6BCC99 CRC64;
MRMAAITKML FISFLFLSSV FLARSGEVDD ESEFSYDEKS ENGPANWGNI RPDWKECSGK
LQSPIDIFDL RAEVVSNLRI LQKDYKPSNA TLLNRGHDIM LRLDDGGYLK INETQYQLKQ
LHWHTPSEHT INGERFNLEA HLVHESNNGK FVVIGIVYEI GLWPDPFLSM IENDLKVPAN
KKGIERGIGI IDPNQIKLDG KKYFRYIGSL TTPPCTEGVV WIIDRKVKTV TRRQIKLLQE
AVHDGFETNA RPTQPENERY INSTYHSFGI EKQQ
