NADA_ARATH
ID NADA_ARATH Reviewed; 718 AA.
AC Q9FGS4;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Quinolinate synthase, chloroplastic {ECO:0000303|PubMed:16698895};
DE EC=2.5.1.72 {ECO:0000269|PubMed:17452319};
DE AltName: Full=Protein ONSET OF LEAF DEATH 5 {ECO:0000303|PubMed:18978034};
DE AltName: Full=Protein SULFUR E 3 {ECO:0000303|PubMed:17452319};
DE Flags: Precursor;
GN Name=QS {ECO:0000303|PubMed:16698895};
GN Synonyms=OLD5 {ECO:0000303|PubMed:18978034},
GN SUFE3 {ECO:0000303|PubMed:17452319};
GN OrderedLocusNames=At5g50210 {ECO:0000312|Araport:AT5G50210};
GN ORFNames=K6A12.7 {ECO:0000312|EMBL:BAB09392.1};
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, PATHWAY, COFACTOR, SUBUNIT,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF CYS-132.
RX PubMed=17452319; DOI=10.1074/jbc.m701428200;
RA Narayana Murthy U.M., Ollagnier-de-Choudens S., Sanakis Y.,
RA Abdel-Ghany S.E., Rousset C., Ye H., Fontecave M., Pilon-Smits E.A.,
RA Pilon M.;
RT "Characterization of Arabidopsis thaliana SufE2 and SufE3: functions in
RT chloroplast iron-sulfur cluster assembly and Nad synthesis.";
RL J. Biol. Chem. 282:18254-18264(2007).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, MUTAGENESIS OF PRO-101, 3D-STRUCTURE
RP MODELING, AND INTERACTION WITH NFS2; CPNIFS3 AND AO.
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 [8]
RP CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER ALA-70, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Catalyzes the condensation of iminoaspartate with
CC dihydroxyacetone phosphate to form quinolinate. Can complement nadA-
CC deficient E.coli mutant. Essential for the de novo synthesis of NAD.
CC Participates also in cysteine desulfurization mediated by NFS2. Can
CC activate the cysteine desulfurase activity of NFS2 in vitro.
CC {ECO:0000269|PubMed:16698895, ECO:0000269|PubMed:17452319,
CC ECO:0000269|PubMed:18978034}.
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:0000269|PubMed:17452319, ECO:0000269|PubMed:18978034};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:17452319};
CC Note=Binds 1 [4Fe-4S] cluster per subunit.
CC {ECO:0000269|PubMed:17452319};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from
CC iminoaspartate: step 1/1. {ECO:0000269|PubMed:17452319,
CC ECO:0000269|PubMed:18978034}.
CC -!- SUBUNIT: Homodimer (PubMed:17452319). Interacts in vitro with NFS2,
CC CpNIFS3 and AO (PubMed:18978034). Part of a Cys defulfurase complex
CC (Probable). {ECO:0000269|PubMed:17452319, ECO:0000269|PubMed:18978034,
CC ECO:0000305|PubMed:18978034}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:16698895, ECO:0000269|PubMed:17452319}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems and flowers.
CC {ECO:0000269|PubMed:17452319}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality when homozygous.
CC {ECO:0000269|PubMed:16698895, ECO:0000269|PubMed:17452319}.
CC -!- MISCELLANEOUS: The highly oxygen-sensitive (4Fe-4S) cluster at its NadA
CC domain, can be reconstituted by its own SufE domain in the presence of
CC NFS2, cysteine and ferrous iron. {ECO:0000305|PubMed:17452319}.
CC -!- SIMILARITY: Belongs to the quinolinate synthase family. Type 1
CC subfamily. {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; AB024031; BAB09392.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95912.1; -; Genomic_DNA.
DR EMBL; AY035115; AAK59620.1; -; mRNA.
DR EMBL; AY113860; AAM44908.1; -; mRNA.
DR EMBL; AY085553; AAM62776.1; -; mRNA.
DR RefSeq; NP_199832.1; NM_124400.3.
DR AlphaFoldDB; Q9FGS4; -.
DR SMR; Q9FGS4; -.
DR STRING; 3702.AT5G50210.1; -.
DR SwissPalm; Q9FGS4; -.
DR PaxDb; Q9FGS4; -.
DR PRIDE; Q9FGS4; -.
DR ProteomicsDB; 251234; -.
DR EnsemblPlants; AT5G50210.1; AT5G50210.1; AT5G50210.
DR GeneID; 835086; -.
DR Gramene; AT5G50210.1; AT5G50210.1; AT5G50210.
DR KEGG; ath:AT5G50210; -.
DR Araport; AT5G50210; -.
DR TAIR; locus:2157747; AT5G50210.
DR eggNOG; ENOG502QPQ6; Eukaryota.
DR HOGENOM; CLU_020092_1_0_1; -.
DR InParanoid; Q9FGS4; -.
DR OMA; VSMQKKT; -.
DR OrthoDB; 1016662at2759; -.
DR PhylomeDB; Q9FGS4; -.
DR BioCyc; ARA:AT5G50210-MON; -.
DR UniPathway; UPA00253; UER00327.
DR PRO; PR:Q9FGS4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FGS4; baseline and differential.
DR Genevisible; Q9FGS4; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:TAIR.
DR GO; GO:0008047; F:enzyme activator activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:TAIR.
DR GO; GO:0008987; F:quinolinate synthetase A activity; IMP:TAIR.
DR GO; GO:0034628; P:'de novo' NAD biosynthetic process from aspartate; IBA:GO_Central.
DR GO; GO:0009060; P:aerobic respiration; IMP:TAIR.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IC:TAIR.
DR GO; GO:0009435; P:NAD biosynthetic process; IMP:TAIR.
DR GO; GO:0051176; P:positive regulation of sulfur metabolic process; IDA:TAIR.
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 1: Evidence at protein level;
KW 4Fe-4S; Chloroplast; Iron; Iron-sulfur; Metal-binding; Plastid;
KW Pyridine nucleotide biosynthesis; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..70
FT /note="Chloroplast"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 71..718
FT /note="Quinolinate synthase, chloroplastic"
FT /id="PRO_0000423476"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 132
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000303|PubMed:17452319"
FT BINDING 280
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000250|UniProtKB:O57767"
FT BINDING 306
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000250|UniProtKB:O57767"
FT BINDING 360
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:O57767"
FT BINDING 389..391
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000250|UniProtKB:O57767"
FT BINDING 411
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000250|UniProtKB:O57767"
FT BINDING 484
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:O57767"
FT BINDING 510..512
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000250|UniProtKB:O57767"
FT BINDING 535
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000250|UniProtKB:O57767"
FT BINDING 640
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:O57767"
FT MUTAGEN 101
FT /note="P->S: In old5; early senescence, high levels of
FT tricarboxylic acid cycle intermediates and nitrogen-
FT containing amino acids, decreased stimulation of the Cys
FT desulfurase activity of NFS2, and increased respiration
FT rate and antioxidant accumulation."
FT /evidence="ECO:0000269|PubMed:18978034"
FT MUTAGEN 132
FT /note="C->S: Loss of quinolinate synthase activity."
FT /evidence="ECO:0000269|PubMed:17452319"
SQ SEQUENCE 718 AA; 78934 MW; 53EB2647EABF3435 CRC64;
MALALSVAPT SSSLSSLLSR TPNPSPNFRT THLNFGSQRR IYTINPLLRS FKCLQSSSRD
VNASPFSISA IASSSSSSQT TELVPYKLQR LVKEFKSLTE PIDRLKWVLH YASLLPQMPE
SSKTESNRVM GCTARVWLDA ELGQDGKMRF CADSDSDVSK GMCSCLIQVL DEASPVEVME
LKTEDLAELN VGLLGGERSR VNTWYNVLVS MQKKTRRLVA EREGKVPSFE PFPSLVLTAH
GIEAKGSFAQ AQAKYLFPEE SRVEELVNVL KEKKIGVVAH FYMDPEVQGV LTAAQKHWPH
ISISDSLVMA DSAVTMAKAG CQFITVLGVD FMSENVRAIL DQAGFEKVGV YRMSDETIGC
SLADAASAPA YLNYLEAASR SPPSLHVVYI NTSLETKAFA HELVPTITCT SSNVVQTILQ
AFAQMPELTV WYGPDSYMGA NIVKLFQQMT LMTNEEIANI HPKHSLDSIK SLLPRLHYFQ
EGTCIVHHLF GHEVVERIKY MYCDAFLTAH LEVPGEMFSL AMEAKKREMG VVGSTQNILD
FIKQKVQEAV DRNVDDHLQF VLGTESGMVT SIVAVIRSLL GSSANSKLKV EVVFPVSSDS
MTKTSSDSSN SIKVGDVALP VVPGVAGGEG CSIHGGCASC PYMKMNSLSS LLKVCHKLPD
LENVYGGFIA ERFKRQTPQG KLIADVGCEP ILHMRHFQAN KELPDKLVHQ VLSCESKR
