AO2B_TOBAC
ID AO2B_TOBAC Reviewed; 648 AA.
AC A0A1S4BJT3;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 1.
DT 03-AUG-2022, entry version 27.
DE RecName: Full=L-aspartate oxidase 2-b, chloroplastic {ECO:0000303|PubMed:32242247};
DE EC=1.4.3.16 {ECO:0000250|UniProtKB:Q94AY1};
DE Flags: Precursor;
GN Name=AO-2B {ECO:0000303|PubMed:32242247};
GN ORFNames=LOC107809102 {ECO:0000312|RefSeq:XP_016489183.1};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 517-648.
RC STRAIN=cv. K326; TISSUE=Root;
RA Coates S.A., Dorlhac de Borne F., Ross J., Verrier J.L., Ward M., Delon R.;
RT "A comprehensive survey of the N. tabacum transcriptome.";
RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
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 EMBL; DW001381; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_016489183.1; XM_016633697.1.
DR SMR; A0A1S4BJT3; -.
DR GeneID; 107809102; -.
DR KEGG; nta:107809102; -.
DR OMA; DSPDIHY; -.
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 2: Evidence at transcript level;
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 ?..648
FT /note="L-aspartate oxidase 2-b, chloroplastic"
FT /id="PRO_0000455774"
FT ACT_SITE 373
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 98..101
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 120
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 127..134
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 298
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 458
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 474..475
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT SITE 199
FT /note="Important in orienting the L-aspartate substrate"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT CONFLICT 525
FT /note="C -> R (in Ref. 2; DW001381)"
FT /evidence="ECO:0000305"
FT CONFLICT 548
FT /note="N -> T (in Ref. 2; DW001381)"
FT /evidence="ECO:0000305"
FT CONFLICT 559
FT /note="R -> K (in Ref. 2; DW001381)"
FT /evidence="ECO:0000305"
FT CONFLICT 604
FT /note="H -> Q (in Ref. 2; DW001381)"
FT /evidence="ECO:0000305"
FT CONFLICT 635..639
FT /note="NSWSS -> STWST (in Ref. 2; DW001381)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 648 AA; 71728 MW; 9713920BE1026D1D CRC64;
MATGIASGCG QLHLRKPVYL RNSYGNKAHC HSNVILNGTQ NQIAWSSWVS NVLRVNRSSY
PECQVIKTNW KSSRGTIKSC QQRDGSVTRY FDFTVIGSGI AGLRYALEVA KHGTVAVITK
AEPHESSTNY AQGGVSAVLC PLDSVESHMQ DTIVAGAYLC DKETVRVVCT EGPERIRELI
AMGASFDHGE DGNLDLAREG GHSHRRIVHA ADMTGREIER ALLEAVFKNP NIHVFQHHFA
IDLLTTQDGS DIVCHGVDTI HTETKEVIRF ISKVTLLASG GVGHIYPSTT NPTVATGDGM
AMAHRAQAVI SNMEFVQFHP TALADEGLPN IPSARENAFL ITEAVRGDGG ILYNLDMERF
MPMYDERAEL APRDVVARSI DDQLKKRGEK YVLLDISHKP REKVLSHFPN IAAECLRHGL
DITQQPIPVV PAAHYMCGGV RAGLEGETNV QGLYVAGEVA CTGLHGANRL ASNSLLEALV
FARRAVQPSI DHVNVSRIDH GASSWWPRPV APMVLGDTVL NKVICRTREV RKELQSIMWE
YVGIVRSNSR LNTAEKRIRE LELEWETYLF QHGWEPTMVG VEACEMRNLF CCANLVVSSA
LSRHESRGLH YTTDFPHVEE SERLPTVIFP SQRNNSWSSR QLHAQPIS
