NADB_ORYSJ
ID NADB_ORYSJ Reviewed; 645 AA.
AC Q6Z836; A0A0N7KEM7;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=L-aspartate oxidase, chloroplastic;
DE EC=1.4.3.16;
DE AltName: Full=Protein FLAGELLIN-INSENSITIVE 4;
DE Flags: Precursor;
GN OrderedLocusNames=Os02g0134400, LOC_Os02g04170; ORFNames=P0585B01.16;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
CC -!- FUNCTION: Catalyzes the oxidation of L-aspartate to iminoaspartate.
CC {ECO:0000250}.
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 -!- 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 -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family. NadB
CC subfamily. {ECO:0000305}.
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DR EMBL; AP004799; BAD10088.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF07726.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS76849.1; -; Genomic_DNA.
DR RefSeq; XP_015622817.1; XM_015767331.1.
DR RefSeq; XP_015622818.1; XM_015767332.1.
DR AlphaFoldDB; Q6Z836; -.
DR SMR; Q6Z836; -.
DR STRING; 4530.OS02T0134400-01; -.
DR PaxDb; Q6Z836; -.
DR PRIDE; Q6Z836; -.
DR EnsemblPlants; Os02t0134400-01; Os02t0134400-01; Os02g0134400.
DR GeneID; 4328220; -.
DR Gramene; Os02t0134400-01; Os02t0134400-01; Os02g0134400.
DR KEGG; osa:4328220; -.
DR eggNOG; KOG2403; Eukaryota.
DR HOGENOM; CLU_014312_3_0_1; -.
DR InParanoid; Q6Z836; -.
DR OMA; HCVQWLI; -.
DR OrthoDB; 606981at2759; -.
DR PlantReactome; R-OSA-1119384; NAD biosynthesis I (from aspartate).
DR UniPathway; UPA00253; UER00326.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR Genevisible; Q6Z836; OS.
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-EC.
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 Chloroplast; FAD; Flavoprotein; Nucleotide-binding; Oxidoreductase;
KW Plastid; Pyridine nucleotide biosynthesis; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..70
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 71..645
FT /note="L-aspartate oxidase, chloroplastic"
FT /id="PRO_0000423479"
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 645 AA; 71100 MW; C2BEC7E772D9ED97 CRC64;
MAALMNGFGS LQCKATVHVE KGHMQASGMA FFSPVNRCAQ VHISSIPHFI GAKSVSASQL
RMRHKVGSIR ASAASCLQDE TTKYFDFVVI GSGVAGLRYA LEVSKYGSVA IITKAEPHES
NTNYAQGGVS AVLCPSDSVE SHMQDTIVAG AYLCDEETVR VVCTEGPERV KELIAMGASF
DHGEDGRLHL AREGGHSHNR IVHSADMTGR EIERALLQAV DNDDNISLFG HHFAIDLLTC
QSNGEIYCYG VDSLDAETQK AIRFISKVTL LASGGVGHIY PSTTNPPVAT GDGIAMSHRA
QAVISNMEFV QFHPTALSDE GLPIKPATRR ENAFLITEAV RGDGGILYNQ SMERFMTSYD
DRAELAPRDV VARSIDDQLK KRGEKYVLLD ISHKPREKVL AHFPNIAAEC LRHGLDITQQ
PIPVVPAAHY MCGGVRAGLQ GETNVKGLYV AGEVACTGLH GANRLASNSL LEALVFARRA
VQPSIDHMVD ADVDPSFAKK WARPVLSVSL RDSILSDIIE KTKQARMELQ SIMWEYVGIV
RSTNRLKHAE WKISDLESEW EEFLFRRGWK PTMVGVETCE MRNLFCCAKL VVKSALARHE
SRGLHFTEDF PYLEESKRKP TVIFPTHIQE LTWSSKPLQK QLQCK
