NADB_ARATH
ID NADB_ARATH Reviewed; 651 AA.
AC Q94AY1; Q9LER1;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=L-aspartate oxidase, chloroplastic {ECO:0000303|PubMed:16698895, ECO:0000303|PubMed:22730426};
DE EC=1.4.3.16 {ECO:0000269|PubMed:16698895};
DE AltName: Full=Protein FLAGELLIN-INSENSITIVE 4 {ECO:0000303|PubMed:22730426};
DE Flags: Precursor;
GN Name=AO {ECO:0000303|PubMed:16698895, ECO:0000303|PubMed:22730426};
GN Synonyms=FIN4 {ECO:0000303|PubMed:22730426};
GN OrderedLocusNames=At5g14760 {ECO:0000312|Araport:AT5G14760};
GN ORFNames=T9L3.60 {ECO:0000312|EMBL:CAC01875.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY,
RP AND PATHWAY.
RX PubMed=16698895; DOI=10.1104/pp.106.081091;
RA Katoh A., Uenohara K., Akita M., Hashimoto T.;
RT "Early steps in the biosynthesis of NAD in Arabidopsis start with aspartate
RT and occur in the plastid.";
RL Plant Physiol. 141:851-857(2006).
RN [5]
RP INTERACTION WITH QS.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=18978034; DOI=10.1105/tpc.107.056341;
RA Schippers J.H., Nunes-Nesi A., Apetrei R., Hille J., Fernie A.R.,
RA Dijkwel P.P.;
RT "The Arabidopsis onset of leaf death5 mutation of quinolinate synthase
RT affects nicotinamide adenine dinucleotide biosynthesis and causes early
RT ageing.";
RL Plant Cell 20:2909-2925(2008).
RN [6]
RP FUNCTION.
RX PubMed=22730426; DOI=10.1104/pp.112.199810;
RA Macho A.P., Boutrot F., Rathjen J.P., Zipfel C.;
RT "Aspartate oxidase plays an important role in Arabidopsis stomatal
RT immunity.";
RL Plant Physiol. 159:1845-1856(2012).
CC -!- FUNCTION: Catalyzes the oxidation of L-aspartate to iminoaspartate. Can
CC complement nadB-deficient E.coli mutant. Plays a role in stomatal
CC immunity. {ECO:0000269|PubMed:16698895, ECO:0000269|PubMed:22730426}.
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:0000269|PubMed:16698895};
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: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate
CC from L-aspartate (oxidase route): step 1/1.
CC {ECO:0000269|PubMed:16698895}.
CC -!- SUBUNIT: Interacts in vitro with QS (PubMed:18978034).
CC {ECO:0000269|PubMed:18978034}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:16698895}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality when homozygous.
CC {ECO:0000269|PubMed:16698895}.
CC -!- MISCELLANEOUS: The viable mutant fin4 (T-DNA insertion in the promoter)
CC is impaired in the RBOHD-dependent pathogen-associated molecular
CC pattern (PAMP)-induced reactive oxygen species (ROS) burst and stomatal
CC closure. {ECO:0000305|PubMed:22730426}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family. NadB
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC01875.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL391149; CAC01875.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED92074.1; -; Genomic_DNA.
DR EMBL; AY045626; AAK73984.1; -; mRNA.
DR EMBL; BT001009; AAN46763.1; -; mRNA.
DR PIR; T51421; T51421.
DR RefSeq; NP_568304.1; NM_121480.4.
DR AlphaFoldDB; Q94AY1; -.
DR SMR; Q94AY1; -.
DR BioGRID; 16605; 42.
DR IntAct; Q94AY1; 4.
DR STRING; 3702.AT5G14760.1; -.
DR PaxDb; Q94AY1; -.
DR PRIDE; Q94AY1; -.
DR ProteomicsDB; 251019; -.
DR EnsemblPlants; AT5G14760.1; AT5G14760.1; AT5G14760.
DR GeneID; 831328; -.
DR Gramene; AT5G14760.1; AT5G14760.1; AT5G14760.
DR KEGG; ath:AT5G14760; -.
DR Araport; AT5G14760; -.
DR TAIR; locus:2185480; AT5G14760.
DR eggNOG; KOG2403; Eukaryota.
DR HOGENOM; CLU_014312_3_0_1; -.
DR InParanoid; Q94AY1; -.
DR OMA; HCVQWLI; -.
DR OrthoDB; 606981at2759; -.
DR PhylomeDB; Q94AY1; -.
DR BioCyc; ARA:AT5G14760-MON; -.
DR UniPathway; UPA00253; UER00326.
DR PRO; PR:Q94AY1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q94AY1; baseline and differential.
DR Genevisible; Q94AY1; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0008734; F:L-aspartate oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0044318; F:L-aspartate:fumarate oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0009435; P:NAD biosynthetic process; IMP:TAIR.
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 1: Evidence at protein level;
KW Chloroplast; FAD; Flavoprotein; Nucleotide-binding; Oxidoreductase;
KW Plastid; Pyridine nucleotide biosynthesis; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..74
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 75..651
FT /note="L-aspartate oxidase, chloroplastic"
FT /id="PRO_0000423478"
FT ACT_SITE 368
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 92..95
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 114
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 121..128
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 292
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 453
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 469..470
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT SITE 193
FT /note="Important in orienting the L-aspartate substrate"
FT /evidence="ECO:0000250|UniProtKB:P10902"
SQ SEQUENCE 651 AA; 71412 MW; 0CE18268085DB738 CRC64;
MAAHVSTGNI HNFYLAGQVY RGQAFSWSSA STFMANPFKE PSWSSGVFKA LKAERCGCYS
RGISPISETS KPIRAVSVSS STKYYDFTVI GSGVAGLRYA LEVAKQGTVA VITKDEPHES
NTNYAQGGVS AVLCPLDSVE SHMRDTMVAG AHLCDEETVR VVCTEGPERI RELIAMGASF
DHGEDGNLHL AREGGHSHCR IVHAADMTGR EIERALLEAV LNDPNISVFK HHFAIDLLTS
QDGLNTVCHG VDTLNIKTNE VVRFISKVTL LASGGAGHIY PSTTNPLVAT GDGMAMAHRA
QAVISNMEFV QFHPTALADE GLPIKLQTAR ENAFLITEAV RGDGGILYNL GMERFMPVYD
ERAELAPRDV VARSIDDQLK KRNEKYVLLD ISHKPREKIL AHFPNIASEC LKHGLDITRQ
PIPVVPAAHY MCGGVRAGLQ GETNVLGLFV AGEVACTGLH GANRLASNSL LEALVFARRA
VQPSTELMKR TRLDVCASEK WTRPVVATAR LLGDEVIAKI IALTKEVRRE LQEVMWKYVG
IVRSTIRLTT AERKIAELEA KWETFLFEHG WEQTVVALEA CEMRNLFCCA KLVVSSALAR
HESRGLHYMT DFPFVEESKR IPTIILPSSP TTASWSSRRL QNISSSSLID C
