AO2A_TOBAC
ID AO2A_TOBAC Reviewed; 644 AA.
AC A0A1S3YEG8;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 1.
DT 03-AUG-2022, entry version 26.
DE RecName: Full=L-aspartate oxidase 2-a, chloroplastic {ECO:0000303|PubMed:32242247};
DE EC=1.4.3.16 {ECO:0000250|UniProtKB:Q94AY1};
DE Flags: Precursor;
GN Name=AO-2A {ECO:0000303|PubMed:32242247};
GN ORFNames=LOC107775324 {ECO:0000312|RefSeq:XP_016450537.1,
GN ECO:0000312|RefSeq:XP_016450538.1, ECO:0000312|RefSeq:XP_016450539.1,
GN ECO:0000312|RefSeq:XP_016450540.1};
OS Nicotiana tabacum (Common 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=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. TN90;
RX PubMed=24807620; DOI=10.1038/ncomms4833;
RA Sierro N., Battey J.N., Ouadi S., Bakaher N., Bovet L., Willig A.,
RA Goepfert S., Peitsch M.C., Ivanov N.V.;
RT "The tobacco genome sequence and its comparison with those of tomato and
RT potato.";
RL Nat. Commun. 5:3833-3833(2014).
RN [2]
RP REVIEW ON ALKALOID BIOSYNTHESIS IN NICOTIANA TABACUM.
RX PubMed=23953973; DOI=10.1016/j.phytochem.2013.06.002;
RA Dewey R.E., Xie J.;
RT "Molecular genetics of alkaloid biosynthesis in Nicotiana tabacum.";
RL Phytochemistry 94:10-27(2013).
RN [3]
RP REVIEW ON NICOTINE BIOSYNTHESIS.
RX PubMed=25582664; DOI=10.1007/s00438-015-0989-7;
RA Wang X., Bennetzen J.L.;
RT "Current status and prospects for the study of Nicotiana genomics,
RT genetics, and nicotine biosynthesis genes.";
RL Mol. Genet. Genomics 290:11-21(2015).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RC STRAIN=cv. K326-ALCS3;
RX PubMed=32242247; DOI=10.1007/s00425-020-03387-1;
RA Hidalgo Martinez D., Payyavula R.S., Kudithipudi C., Shen Y., Xu D.,
RA Warek U., Strickland J.A., Melis A.;
RT "Genetic attenuation of alkaloids and nicotine content in tobacco
RT (Nicotiana tabacum).";
RL Planta 251:92-92(2020).
CC -!- FUNCTION: Involved in the biosynthesis of pyridine alkaloid natural
CC products, leading mainly to the production of anabasine, anatabine,
CC nicotine and nornicotine, effective deterrents against herbivores with
CC antiparasitic and pesticide properties (neurotoxins); nornicotine
CC serves as the precursor in the synthesis of the carcinogen compound N'-
CC nitrosonornicotine (NNN) (PubMed:32242247). Catalyzes the oxidation of
CC L-aspartate to iminoaspartate (By similarity).
CC {ECO:0000250|UniProtKB:Q94AY1, ECO:0000269|PubMed:32242247}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-aspartate + O2 = H2O2 + iminosuccinate;
CC Xref=Rhea:RHEA:25876, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:29991, ChEBI:CHEBI:77875; EC=1.4.3.16;
CC Evidence={ECO:0000250|UniProtKB:Q94AY1};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P10902};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P10902};
CC -!- PATHWAY: Alkaloid biosynthesis; nicotine biosynthesis.
CC {ECO:0000269|PubMed:32242247}.
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate
CC from L-aspartate (oxidase route): step 1/1.
CC {ECO:0000250|UniProtKB:Q94AY1}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Reduced alkaloids and nicotin levels associated
CC with a lower putrescine production (PubMed:32242247). Occasionally, an
CC early senescence and a lower viability of the older leaves is observed
CC (PubMed:32242247). {ECO:0000269|PubMed:32242247}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family. NadB
CC subfamily. {ECO:0000305}.
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DR RefSeq; XP_016450537.1; XM_016595051.1.
DR RefSeq; XP_016450538.1; XM_016595052.1.
DR RefSeq; XP_016450539.1; XM_016595053.1.
DR RefSeq; XP_016450540.1; XM_016595054.1.
DR SMR; A0A1S3YEG8; -.
DR GeneID; 107775324; -.
DR KEGG; nta:107775324; -.
DR OMA; HCVQWLI; -.
DR OrthoDB; 606981at2759; -.
DR UniPathway; UPA00107; -.
DR UniPathway; UPA00253; UER00326.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0008734; F:L-aspartate oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0044318; F:L-aspartate:fumarate oxidoreductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.50.50.60; -; 1.
DR Gene3D; 3.90.700.10; -; 1.
DR InterPro; IPR003953; FAD-binding_2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR037099; Fum_R/Succ_DH_flav-like_C_sf.
DR InterPro; IPR015939; Fum_Rdtase/Succ_DH_flav-like_C.
DR InterPro; IPR005288; NadB.
DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR PANTHER; PTHR42716; PTHR42716; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR Pfam; PF02910; Succ_DH_flav_C; 1.
DR SUPFAM; SSF46977; SSF46977; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF56425; SSF56425; 1.
DR TIGRFAMs; TIGR00551; nadB; 1.
PE 3: Inferred from homology;
KW Alkaloid metabolism; Chloroplast; FAD; Flavoprotein; Oxidoreductase;
KW Plastid; Pyridine nucleotide biosynthesis; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN ?..644
FT /note="L-aspartate oxidase 2-a, chloroplastic"
FT /id="PRO_0000455773"
FT ACT_SITE 369
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 94..97
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 116
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 123..130
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 294
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 454
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 470..471
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT SITE 195
FT /note="Important in orienting the L-aspartate substrate"
FT /evidence="ECO:0000250|UniProtKB:P10902"
SQ SEQUENCE 644 AA; 71673 MW; 85E16DEFE0F6FA2E CRC64;
MATGIASGSG QLHLRKPVYW RSSYGKAHCH SNAILNGMQN QIPWSYWVSK FLRVHRSNYS
QCQVKTNWKS HTGTINSCQR DGSTRYFDFA VIGSGIAGLR YALEVAKHGT VAVITKAEPH
ESNTNYAQGG VSAVFCPMDS VESHMQDTIV AGAYLCDEET VRVVCTEGPE RIRELIAMGA
SFDHGEDGNL HLAREGGHSH RRIVHAADMT GREIERALLE AVFKHPNIHV FQHHFAIDFL
TTQDGSDIIC HGVDAINTET QEVIRFISKV TLLASGGAGH IYPSTTNPPV ATGDGMAMAH
RAQAVISNME FVQFHPTALA DEGLPNRPSA RENAFLITEA VRGDGGILYN LDMERFMPMY
DKRAELAPRD VVARSIDDQL KKRGEKYVLL DISHKPREKV LSHFPNIAAE CLRHGLDITQ
QPIPVVPAAH YMCGGVRAGL EGETNVQGLY VAGEVACTGL HGANRLASNS LLEALVFARR
AVQPSIDHVN VSRIDHCASS WWPRPVAPVV IGDTVLNKVI RRTREVRKEL QSIMWEYVGI
VRSTSRLTAA EKRINELELE WETYLFQHGW EPTMVGLEAC EMRNLFCCAN LVVSSALSRH
ESRGLHYTID FPHVVESKRL PTIIFPSQRN SSWSSRQLHR QQIC
