NADA_ORYSJ
ID NADA_ORYSJ Reviewed; 711 AA.
AC Q2QTL0; A0A0P0Y9A3;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 2.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Quinolinate synthase, chloroplastic {ECO:0000250|UniProtKB:Q9FGS4};
DE EC=2.5.1.72 {ECO:0000250|UniProtKB:Q9FGS4};
DE Flags: Precursor;
GN Name=QS {ECO:0000250|UniProtKB:Q9FGS4};
GN OrderedLocusNames=Os12g0290150, LOC_Os12g19304;
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=16188032; DOI=10.1186/1741-7007-3-20;
RG The rice chromosomes 11 and 12 sequencing consortia;
RT "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT genes and recent gene duplications.";
RL BMC Biol. 3:20-20(2005).
RN [2]
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 [3]
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 [4]
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 condensation of iminoaspartate with
CC dihydroxyacetone phosphate to form quinolinate.
CC {ECO:0000250|UniProtKB:Q9FGS4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dihydroxyacetone phosphate + iminosuccinate = H(+) + 2 H2O +
CC phosphate + quinolinate; Xref=Rhea:RHEA:25888, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29959, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57642, ChEBI:CHEBI:77875; EC=2.5.1.72;
CC Evidence={ECO:0000250|UniProtKB:Q9FGS4};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:Q9FGS4};
CC Note=Binds 1 [4Fe-4S] cluster per subunit.
CC {ECO:0000250|UniProtKB:Q9FGS4};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from
CC iminoaspartate: step 1/1. {ECO:0000250|UniProtKB:Q9FGS4}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9FGS4}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000250|UniProtKB:Q9FGS4}.
CC -!- SIMILARITY: Belongs to the quinolinate synthase family. Type 1
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABA97161.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=ABG21971.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DP000011; ABA97161.1; ALT_SEQ; Genomic_DNA.
DR EMBL; DP000011; ABG21971.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008218; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP014968; BAT16777.1; -; Genomic_DNA.
DR RefSeq; XP_015619876.1; XM_015764390.1.
DR AlphaFoldDB; Q2QTL0; -.
DR SMR; Q2QTL0; -.
DR STRING; 4530.OS12T0290150-00; -.
DR PaxDb; Q2QTL0; -.
DR PRIDE; Q2QTL0; -.
DR EnsemblPlants; Os12t0290150-00; Os12t0290150-00; Os12g0290150.
DR GeneID; 107275865; -.
DR Gramene; Os12t0290150-00; Os12t0290150-00; Os12g0290150.
DR KEGG; osa:107275865; -.
DR eggNOG; ENOG502QPQ6; Eukaryota.
DR HOGENOM; CLU_020092_1_0_1; -.
DR OMA; VSMQKKT; -.
DR OrthoDB; 1016662at2759; -.
DR PlantReactome; R-OSA-1119384; NAD biosynthesis I (from aspartate).
DR UniPathway; UPA00253; UER00327.
DR Proteomes; UP000000763; Chromosome 12.
DR Proteomes; UP000059680; Chromosome 12.
DR Genevisible; Q2QTL0; OS.
DR GO; GO:0009507; C:chloroplast; IBA:GO_Central.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0008047; F:enzyme activator activity; IEA:EnsemblPlants.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:EnsemblPlants.
DR GO; GO:0008987; F:quinolinate synthetase A activity; IBA:GO_Central.
DR GO; GO:0034628; P:'de novo' NAD biosynthetic process from aspartate; IBA:GO_Central.
DR GO; GO:0009060; P:aerobic respiration; IEA:EnsemblPlants.
DR GO; GO:0051176; P:positive regulation of sulfur metabolic process; IEA:EnsemblPlants.
DR Gene3D; 3.40.50.10800; -; 3.
DR InterPro; IPR003808; Fe-S_metab-assoc_dom.
DR InterPro; IPR003473; NadA.
DR InterPro; IPR036094; NadA_sf.
DR PANTHER; PTHR30573; PTHR30573; 1.
DR Pfam; PF02445; NadA; 1.
DR Pfam; PF02657; SufE; 1.
DR SUPFAM; SSF142754; SSF142754; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Chloroplast; Iron; Iron-sulfur; Metal-binding; Plastid;
KW Pyridine nucleotide biosynthesis; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..41
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 42..711
FT /note="Quinolinate synthase, chloroplastic"
FT /id="PRO_0000423477"
FT REGION 17..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 114
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9FGS4"
FT BINDING 263
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000250|UniProtKB:O57767"
FT BINDING 289
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000250|UniProtKB:O57767"
FT BINDING 343
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:O57767"
FT BINDING 372..374
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000250|UniProtKB:O57767"
FT BINDING 394
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000250|UniProtKB:O57767"
FT BINDING 467
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:O57767"
FT BINDING 493..495
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000250|UniProtKB:O57767"
FT BINDING 518
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000250|UniProtKB:O57767"
FT BINDING 631
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:O57767"
SQ SEQUENCE 711 AA; 76683 MW; ED3626965A2A6A3C CRC64;
MDVSSLAAAA PSLVAPPLHH KPHLAFPPHH PSPARGSIGV RCAHSPSPHP LRPSAATADE
EVSLPPSLRV SRLAEEFRVS PDAADRARRL LARAAALPRL GEADRVAANR VMGCVAQVWL
VGRCDGAGRM RFAADSDSEL SRGYCACLVS ALDGARPEEV LDVDPADLAP LGGAAAGTGA
RSRASTWHNV LIGMQKRARA AIAAREGRPA GEPFPSLIIG RDGAIRAQGT YAEAQAMFLS
PNESKTSELV KSLREKKIGI VAHFYMDPEV QGILTASKKH WPHIHISDSL VMADSAVKMA
EAGCEYITVL GVDFMSENVR AILDQAGYSK VGVYRMSSDQ IGCSLADAAS SSAYTHFLKE
ASRSPPSLHV IYINTSLETK AHAHELVPTI TCTSSNVVAT ILQAFAQIPG LNVWYGPDSY
MGANIADLFQ RMAVMSDEEI AEVHPSHNKK SINALLPRLH YYQDGNCIVH DMFGHEVVDK
IKEQYCDAFL TAHFEVPGEM FSLSMEAKTR GMGVVGSTQN ILDFIKNHLM EALDRNIDDH
LQFVLGTESG MITSIVAAVR ELFDSYKTSQ QSANIEVEIV FPVSSDAVSN TSVNGSHHLD
SSTVTDLDNV SVVPGVSSGE GCSIHGGCAS CPYMKMNSLR SLLKVCHQLP DRDNRLVAYQ
ASRFNAKTPL GKLVAEVGCE PILHMRHFQA TKRLPDKLVH HVIHGKGEPT S
