NOA1_ARATH
ID NOA1_ARATH Reviewed; 561 AA.
AC Q66GP9; F4JBJ3; Q0WWY8; Q157M8; Q9STX8;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=NO-associated protein 1, chloroplastic/mitochondrial;
DE Short=AtNOA1;
DE AltName: Full=Dubious mitochondrial nitric oxide synthase 1;
DE Short=AtNOS1;
DE EC=1.14.13.39;
DE AltName: Full=GTPase NOA1;
DE AltName: Full=Protein RESISTANT TO INHIBITION BY FOSMIDOMYCIN 1;
DE Flags: Precursor;
GN Name=NOA1; Synonyms=NOS1, RIF1; OrderedLocusNames=At3g47450;
GN ORFNames=T21L8.200;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 109-244 (ISOFORM 1/2).
RC STRAIN=cv. Columbia;
RA Cai X.-Z., Zhang H.-Z.;
RT "Role of nitric oxide synthase in plant disease resistance.";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP IDENTIFICATION, CHARACTERIZATION, FUNCTION AS NOS, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=14526079; DOI=10.1126/science.1086770;
RA Guo F.-Q., Okamoto M., Crawford N.M.;
RT "Identification of a plant nitric oxide synthase gene involved in hormonal
RT signaling.";
RL Science 302:100-103(2003).
RN [7]
RP INDUCTION BY LIPOPOLYSACCHARIDES.
RX PubMed=15498873; DOI=10.1073/pnas.0404536101;
RA Zeidler D., Zaehringer U., Gerber I., Dubery I., Hartung T., Bors W.,
RA Hutzler P., Durner J.;
RT "Innate immunity in Arabidopsis thaliana: lipopolysaccharides activate
RT nitric oxide synthase (NOS) and induce defense genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15811-15816(2004).
RN [8]
RP FUNCTION AS NOS, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=16272429; DOI=10.1105/tpc.105.037770;
RA Guo F.-Q., Crawford N.M.;
RT "Arabidopsis nitric oxide synthase1 is targeted to mitochondria and
RT protects against oxidative damage and dark-induced senescence.";
RL Plant Cell 17:3436-3450(2005).
RN [9]
RP FUNCTION AS NOS, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=16690168; DOI=10.1016/j.jplph.2006.03.002;
RA Zhao M., Zhao X., Wu Y., Zhang L.;
RT "Enhanced sensitivity to oxidative stress in an Arabidopsis nitric oxide
RT synthase mutant.";
RL J. Plant Physiol. 164:737-745(2007).
RN [10]
RP TISSUE SPECIFICITY.
RX PubMed=17220360; DOI=10.1104/pp.106.093435;
RA Bethke P.C., Libourel I.G.L., Aoyama N., Chung Y.-Y., Still D.W.,
RA Jones R.L.;
RT "The Arabidopsis aleurone layer responds to nitric oxide, gibberellin, and
RT abscisic acid and is sufficient and necessary for seed dormancy.";
RL Plant Physiol. 143:1173-1188(2007).
RN [11]
RP FUNCTION AS NOS, AND DISRUPTION PHENOTYPE.
RX PubMed=17351048; DOI=10.1104/pp.107.096842;
RA Zhao M.-G., Tian Q.-Y., Zhang W.-H.;
RT "Nitric oxide synthase-dependent nitric oxide production is associated with
RT salt tolerance in Arabidopsis.";
RL Plant Physiol. 144:206-217(2007).
RN [12]
RP FUNCTION AS GTPASE, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF
RP THR-327.
RX PubMed=18801746; DOI=10.1074/jbc.m804838200;
RA Moreau M., Lee G.I., Wang Y., Crane B.R., Klessig D.F.;
RT "AtNOS/AtNOA1 is a functional Arabidopsis thaliana cGTPase and not a
RT nitric-oxide synthase.";
RL J. Biol. Chem. 283:32957-32967(2008).
RN [13]
RP FUNCTION AS GTPASE, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=18469163; DOI=10.1105/tpc.108.058768;
RA Flores-Perez U., Sauret-Gueeto S., Gas E., Jarvis P.,
RA Rodriguez-Concepcion M.;
RT "A mutant impaired in the production of plastome-encoded proteins uncovers
RT a mechanism for the homeostasis of isoprenoid biosynthetic enzymes in
RT Arabidopsis plastids.";
RL Plant Cell 20:1303-1315(2008).
RN [14]
RP FUNCTION IN NO ACCUMULATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Wassilewskija;
RX PubMed=19321706; DOI=10.1104/pp.109.137067;
RA Li J.-H., Liu Y.-Q., Lue P., Lin H.-F., Bai Y., Wang X.-C., Chen Y.-L.;
RT "A signaling pathway linking nitric oxide production to heterotrimeric G
RT protein and hydrogen peroxide regulates extracellular calmodulin induction
RT of stomatal closure in Arabidopsis.";
RL Plant Physiol. 150:114-124(2009).
RN [15]
RP FUNCTION IN NO ACCUMULATION, AND DISRUPTION PHENOTYPE.
RX PubMed=20657186; DOI=10.4161/psb.5.8.12293;
RA Sun L.R., Hao F.S., Lu B.S., Ma L.Y.;
RT "AtNOA1 modulates nitric oxide accumulation and stomatal closure induced by
RT salicylic acid in Arabidopsis.";
RL Plant Signal. Behav. 5:1022-1024(2010).
RN [16]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21392840; DOI=10.1016/j.jplph.2011.01.021;
RA Majlath I., Szalai G., Papp I., Vankova R., Janda T.;
RT "Atnoa1 mutant Arabidopsis plants induce compensation mechanisms to reduce
RT the negative effects of the mutation.";
RL J. Plant Physiol. 168:1184-1190(2011).
RN [17]
RP REVIEW ON NOS.
RX PubMed=16356941; DOI=10.1093/jxb/erj050;
RA Crawford N.M.;
RT "Mechanisms for nitric oxide synthesis in plants.";
RL J. Exp. Bot. 57:471-478(2006).
RN [18]
RP REVIEW ON CONTROVERSY.
RX PubMed=19168714; DOI=10.1105/tpc.108.065243;
RA Gas E., Flores-Perez U., Sauret-Gueeto S., Rodriguez-Concepcion M.;
RT "Hunting for plant nitric oxide synthase provides new evidence of a central
RT role for plastids in nitric oxide metabolism.";
RL Plant Cell 21:18-23(2009).
CC -!- FUNCTION: Exhibits cGTPase activity; binds and hydrolyzes specifically
CC GTP (PubMed:18801746). May participate in ribosome assembly and
CC stability and thus regulates protein synthesis in chloroplasts. The
CC GTPase activity requires MgCl(2)and the presence of either KCl or
CC (NH(4))(2)SO(4). Involved in the post-transcriptional regulation of the
CC methylerythritol phosphate (MEP) pathway. Involved in chlorophyll-a
CC fluorescence regulation. {ECO:0000269|PubMed:18801746}.
CC -!- FUNCTION: May mediate the production or accumulation of nitric oxide
CC (NO) which is a messenger molecule involved in hormonal signaling and
CC defense responses in plant (PubMed:14526079, PubMed:16272429,
CC PubMed:16690168 and PubMed:17351048). Acts as an antisenescence agent.
CC Plays a crucial role in both extracellular calmodulin (ExtCaM)-
CC triggered and salicylic acid (SA)-mediated H(2)O(2)-dependent stomatal
CC closure.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + 2 L-arginine + 3 NADPH + 4 O2 = 4 H2O + 2 L-citrulline
CC + 3 NADP(+) + 2 nitric oxide; Xref=Rhea:RHEA:19897,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16480, ChEBI:CHEBI:32682, ChEBI:CHEBI:57743,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.14.13.39;
CC -!- ACTIVITY REGULATION: Stimulated by calcium/calmodulin. Inhibited by L-
CC NAME. Not activated by tetrahydrobiopterin (BH4), FAD, FMN, or heme.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=12.5 uM for arginine {ECO:0000269|PubMed:14526079};
CC KM=64.5 uM for GTP (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:18801746};
CC Vmax=5.0 nmol/min/mg enzyme with arginine as substrate
CC {ECO:0000269|PubMed:14526079};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16272429}.
CC Plastid, chloroplast {ECO:0000269|PubMed:18469163}. Note=Was initially
CC thought to be mitochondrial (PubMed:16272429). In fact seems to be
CC chloroplastic (PubMed:18469163). {ECO:0000269|PubMed:16272429,
CC ECO:0000269|PubMed:18469163}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q66GP9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q66GP9-2; Sequence=VSP_044128;
CC -!- TISSUE SPECIFICITY: Expressed in aleurone layer and the embryo.
CC {ECO:0000269|PubMed:17220360}.
CC -!- INDUCTION: Constitutively expressed. Induced by abscisic acid (ABA) and
CC lipopolysaccharides. {ECO:0000269|PubMed:15498873}.
CC -!- DISRUPTION PHENOTYPE: Pale seedlings with a delayed development and
CC greening of true leaves resulting in small plants with a characteristic
CC virescent phenotype of pale young leaves but green mature leaves. Loss
CC of NOS activity in mitochondria. Reduced extracellular
CC calmodulin- (ExtCaM-) triggered and salicylic acid (SA)-mediated
CC increase in NO levels and subsequent H(2)O(2)-dependent stomatal
CC closure. Faster dark-induced senescence in leaves. Higher accumulation
CC of hydrogen peroxide, superoxide anion, oxidized lipid, and oxidized
CC protein. Increased hypersensitivity to salt stress and methyl viologen
CC (MV) treatment. Enhanced accumulation of Na(+) but reduced accumulation
CC of K(+) when exposed to NaCl leading to an enhanced sensitivity to
CC salt. Post-transcriptional up-regulation of the methylerythritol
CC phosphate (MEP) pathway. Enhanced resistance to fosmidomycin (FSM).
CC Disturbed chlorophyll-a fluorescence induction in response to
CC temperature variation, accompanied with altered polyamines
CC accumulation. {ECO:0000269|PubMed:16272429,
CC ECO:0000269|PubMed:16690168, ECO:0000269|PubMed:17351048,
CC ECO:0000269|PubMed:18469163, ECO:0000269|PubMed:19321706,
CC ECO:0000269|PubMed:20657186, ECO:0000269|PubMed:21392840}.
CC -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family. NOA1
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01058}.
CC -!- CAUTION: Nitric oxide synthase (NOS) activity is dubious.
CC {ECO:0000305|PubMed:18801746}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB51217.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL096860; CAB51217.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE78282.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78283.1; -; Genomic_DNA.
DR EMBL; BT015353; AAU05476.1; -; mRNA.
DR EMBL; BT015887; AAU95423.1; -; mRNA.
DR EMBL; AK226195; BAE98360.1; -; mRNA.
DR EMBL; DQ539437; ABG25038.1; -; mRNA.
DR PIR; T13000; T13000.
DR RefSeq; NP_190329.2; NM_114613.3. [Q66GP9-2]
DR RefSeq; NP_850666.1; NM_180335.1. [Q66GP9-1]
DR AlphaFoldDB; Q66GP9; -.
DR SMR; Q66GP9; -.
DR STRING; 3702.AT3G47450.1; -.
DR SwissPalm; Q66GP9; -.
DR PaxDb; Q66GP9; -.
DR PRIDE; Q66GP9; -.
DR ProteomicsDB; 239053; -. [Q66GP9-1]
DR EnsemblPlants; AT3G47450.1; AT3G47450.1; AT3G47450. [Q66GP9-2]
DR EnsemblPlants; AT3G47450.2; AT3G47450.2; AT3G47450. [Q66GP9-1]
DR GeneID; 823899; -.
DR Gramene; AT3G47450.1; AT3G47450.1; AT3G47450. [Q66GP9-2]
DR Gramene; AT3G47450.2; AT3G47450.2; AT3G47450. [Q66GP9-1]
DR KEGG; ath:AT3G47450; -.
DR Araport; AT3G47450; -.
DR TAIR; locus:2099520; AT3G47450.
DR eggNOG; KOG1249; Eukaryota.
DR HOGENOM; CLU_017878_2_1_1; -.
DR InParanoid; Q66GP9; -.
DR OMA; HYNEVQD; -.
DR OrthoDB; 612803at2759; -.
DR PhylomeDB; Q66GP9; -.
DR BioCyc; ARA:AT3G47450-MON; -.
DR PRO; PR:Q66GP9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q66GP9; baseline and differential.
DR Genevisible; Q66GP9; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IDA:TAIR.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0048366; P:leaf development; IMP:TAIR.
DR GO; GO:0006809; P:nitric oxide biosynthetic process; IDA:TAIR.
DR GO; GO:0009657; P:plastid organization; IMP:TAIR.
DR GO; GO:0010322; P:regulation of isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IMP:TAIR.
DR GO; GO:0051246; P:regulation of protein metabolic process; IMP:TAIR.
DR GO; GO:0006979; P:response to oxidative stress; IDA:TAIR.
DR GO; GO:0010193; P:response to ozone; IMP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IMP:UniProtKB.
DR GO; GO:0010027; P:thylakoid membrane organization; IMP:TAIR.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030378; G_CP_dom.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR044229; NOA1.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR47569; PTHR47569; 1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51721; G_CP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; GTP-binding; Hydrolase; Mitochondrion;
KW NADP; Nucleotide-binding; Oxidoreductase; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..31
FT /note="Chloroplast and mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 32..561
FT /note="NO-associated protein 1,
FT chloroplastic/mitochondrial"
FT /id="PRO_0000213736"
FT DOMAIN 175..351
FT /note="CP-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT BINDING 108..111
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 166..174
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 223..226
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 260..261
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 289..294
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT VAR_SEQ 443..444
FT /note="KE -> AK (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_044128"
FT MUTAGEN 327
FT /note="T->A: Loss of GTPase activity."
FT /evidence="ECO:0000269|PubMed:18801746"
SQ SEQUENCE 561 AA; 61957 MW; 35CF40F9E191FDF1 CRC64;
MALRTLSTFP SLPRRHTTTR REPNLTVIYR NPTTSIVCKS IANSEPPVSL SERDGFAAAA
PTPGERFLEN QRAHEAQKVV KKEIKKEKKK KKEEIIARKV VDTSVSCCYG CGAPLQTSDV
DSPGFVDLVT YELKKKHHQL RTMICGRCQL LSHGHMITAV GGNGGYPGGK QFVSADELRE
KLSHLRHEKA LIVKLVDIVD FNGSFLARVR DLVGANPIIL VITKIDLLPK GTDMNCIGDW
VVEVTMRKKL NVLSVHLTSS KSLDGVSGVA SEIQKEKKGR DVYILGAANV GKSAFINALL
KTMAERDPVA AAAQKYKPIQ SAVPGTTLGP IQINAFVGGE KLYDTPGVHL HHRQAAVVHS
DDLPALAPQN RLRGQSFDIS TLPTQSSSSP KGESLNGYTF FWGGLVRIDI LKALPETCFT
FYGPKALEIH AVPTKTATAF YEKELGVLLT PPSGKNQMQE WKGLQSHRLL QIEINDAKRP
ASDVAISGLG WISIEPIRKT RGTEPRDLNE AEHEIHICVS VPKPVEVFLR PTLPIGTSGT
EWYQYRELTD KEEEVRPKWY F
