Q66GP9 (NOA1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
NO-associated protein 1, chloroplastic/mitochondrial
Short name=AtNOA1

Alternative name(s):
Dubious mitochondrial nitric oxide synthase 1
Short name=AtNOS1
EC=1.14.13.39
GTPase NOA1
Protein RESISTANT TO INHIBITION BY FOSMIDOMYCIN 1

Gene names

Name:	NOA1
Synonyms:	NOS1, RIF1
Ordered Locus Names:	At3g47450
ORF Names:	T21L8.200

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	561 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Exhibits cGTPase activity; binds and hydrolyzes specifically GTP (Ref.12). May participate in ribosome assembly and stability and thus regulates protein synthesis in chloroplasts. The GTPase activity requires MgCl2and the presence of either KCl or (NH4)2SO4. Involved in the post-transcriptional regulation of the methylerythritol phosphate (MEP) pathway. Involved in chlorophyll-a fluorescence regulation. Ref.6 Ref.8 Ref.9 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 May mediate the production or accumulation of nitric oxide (NO) which is a messenger molecule involved in hormonal signaling and defense responses in plant (Ref.6, Ref.8, Ref.9 and Ref.11). Acts as an antisenescence agent. Plays a crucial role in both extracellular calmodulin (ExtCaM)-triggered and salicylic acid (SA)-mediated H2O(2)-dependent stomatal closure. Ref.6 Ref.8 Ref.9 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16
Catalytic activity	2 L-arginine + 3 NADPH + 4 O2 = 2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O.
Enzyme regulation	Stimulated by calcium/calmodulin. Inhibited by L-NAME. Not activated by tetrahydrobiopterin (BH4), FAD, FMN, or heme.
Subcellular location	Mitochondrion. Plastid › chloroplast. Note: Was initialy thought to be mitochondrial (Ref.8) but seems to be chloroplastic (Ref.13). Ref.8 Ref.13
Tissue specificity	Expressed in aleurone layer and the embryo. Ref.10
Induction	Constitutively expressed. Induced by abscisic acid (ABA) and lipopolysaccharides. Ref.7
Disruption phenotype	Pale seedlings with a delayed development and greening of true leaves resulting in small plants with a characteristic virescent phenotype of pale young leaves but green mature leaves. Loss of NOS activity in mitochondria. Reduced extracellular calmodulin- (ExtCaM-) triggered and salicylic acid (SA)-mediated increase in NO levels and subsequent H2O(2)-dependent stomatal closure. Faster dark-induced senescence in leaves. Higher accumulation of hydrogen peroxide, superoxide anion, oxidized lipid, and oxidized protein. Increased hypersensitivity to salt stress and methyl viologen (MV) treatment. Enhanced accumulation of Na+ but reduced accumulation of K+ when exposed to NaCl leading to an enhanced sensitivity to salt. Post-transcriptional up-regulation of the methylerythritol phosphate (MEP) pathway. Enhanced resistance to fosmidomycin (FSM). Disturbed chlorophyll-a fluorescence induction in response to temperature variation, accompanied with altered polyamines accumulation. Ref.8 Ref.9 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16
Sequence similarities	Belongs to the plant NOS family. Contains 1 G (guanine nucleotide-binding) domain.
Caution	Nitric oxide synthase (NOS) activity is dubious (Ref.12).
Biophysicochemical properties	Kinetic parameters: KM=12.5 µM for arginine (Ref.6) Ref.6 Ref.12 KM=64.5 µM for GTP (at 37 degrees Celsius, Ref.12) Vmax=5.0 nmol/min/mg enzyme with arginine as substrate (Ref.6)
Sequence caution	The sequence CAB51217.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Chloroplast Mitochondrion Plastid
Coding sequence diversity	Alternative splicing
Domain	Transit peptide
Ligand	GTP-binding NADP Nucleotide-binding
Molecular function	Hydrolase Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	response to salt stress Inferred from mutant phenotype Ref.11. Source: UniProtKB
Cellular_component	chloroplast Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW hydrolase activity Inferred from electronic annotation. Source: UniProtKB-KW nitric-oxide synthase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q66GP9-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q66GP9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     443-444: KE → AK

Note: Derived from EST data. No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 31	31	Chloroplast and mitochondrion Potential
	Chain	32 – 561	530	NO-associated protein 1, chloroplastic/mitochondrial		PRO_0000213736
Regions
	Domain	281 – 353	73	G
	Nucleotide binding	108 – 111	4	GTP By similarity
	Nucleotide binding	166 – 174	9	GTP By similarity
	Nucleotide binding	223 – 226	4	GTP By similarity
	Nucleotide binding	260 – 261	2	GTP By similarity
	Nucleotide binding	289 – 294	6	GTP By similarity
	Compositional bias	85 – 92	8	Poly-Lys
Natural variations
	Alternative sequence	443 – 444	2	KE → AK in isoform 2.		VSP_044128
Experimental info
	Mutagenesis	327	1	T → A: Loss of GTPase activity. Ref.12

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: 35CF40F9E191FDF1	FASTA	561	61,957
	10 20 30 40 50 60 MALRTLSTFP SLPRRHTTTR REPNLTVIYR NPTTSIVCKS IANSEPPVSL SERDGFAAAA 70 80 90 100 110 120 PTPGERFLEN QRAHEAQKVV KKEIKKEKKK KKEEIIARKV VDTSVSCCYG CGAPLQTSDV 130 140 150 160 170 180 DSPGFVDLVT YELKKKHHQL RTMICGRCQL LSHGHMITAV GGNGGYPGGK QFVSADELRE 190 200 210 220 230 240 KLSHLRHEKA LIVKLVDIVD FNGSFLARVR DLVGANPIIL VITKIDLLPK GTDMNCIGDW 250 260 270 280 290 300 VVEVTMRKKL NVLSVHLTSS KSLDGVSGVA SEIQKEKKGR DVYILGAANV GKSAFINALL 310 320 330 340 350 360 KTMAERDPVA AAAQKYKPIQ SAVPGTTLGP IQINAFVGGE KLYDTPGVHL HHRQAAVVHS 370 380 390 400 410 420 DDLPALAPQN RLRGQSFDIS TLPTQSSSSP KGESLNGYTF FWGGLVRIDI LKALPETCFT 430 440 450 460 470 480 FYGPKALEIH AVPTKTATAF YEKELGVLLT PPSGKNQMQE WKGLQSHRLL QIEINDAKRP 490 500 510 520 530 540 ASDVAISGLG WISIEPIRKT RGTEPRDLNE AEHEIHICVS VPKPVEVFLR PTLPIGTSGT 550 560 EWYQYRELTD KEEEVRPKWY F
	Isoform 2 [UniParc]. Checksum: 9FCF40F7EB9550E7	FASTA	561	61,899
	10 20 30 40 50 60 MALRTLSTFP SLPRRHTTTR REPNLTVIYR NPTTSIVCKS IANSEPPVSL SERDGFAAAA 70 80 90 100 110 120 PTPGERFLEN QRAHEAQKVV KKEIKKEKKK KKEEIIARKV VDTSVSCCYG CGAPLQTSDV 130 140 150 160 170 180 DSPGFVDLVT YELKKKHHQL RTMICGRCQL LSHGHMITAV GGNGGYPGGK QFVSADELRE 190 200 210 220 230 240 KLSHLRHEKA LIVKLVDIVD FNGSFLARVR DLVGANPIIL VITKIDLLPK GTDMNCIGDW 250 260 270 280 290 300 VVEVTMRKKL NVLSVHLTSS KSLDGVSGVA SEIQKEKKGR DVYILGAANV GKSAFINALL 310 320 330 340 350 360 KTMAERDPVA AAAQKYKPIQ SAVPGTTLGP IQINAFVGGE KLYDTPGVHL HHRQAAVVHS 370 380 390 400 410 420 DDLPALAPQN RLRGQSFDIS TLPTQSSSSP KGESLNGYTF FWGGLVRIDI LKALPETCFT 430 440 450 460 470 480 FYGPKALEIH AVPTKTATAF YEAKLGVLLT PPSGKNQMQE WKGLQSHRLL QIEINDAKRP 490 500 510 520 530 540 ASDVAISGLG WISIEPIRKT RGTEPRDLNE AEHEIHICVS VPKPVEVFLR PTLPIGTSGT 550 560 EWYQYRELTD KEEEVRPKWY F

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana." Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[3]	"Arabidopsis ORF clones." Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: cv. Columbia.
[4]	"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs." Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K. Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: cv. Columbia.
[5]	"Role of nitric oxide synthase in plant disease resistance." Cai X.-Z., Zhang H.-Z. Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 109-244 (ISOFORM 1/2). Strain: cv. Columbia.
[6]	"Identification of a plant nitric oxide synthase gene involved in hormonal signaling." Guo F.-Q., Okamoto M., Crawford N.M. Science 302:100-103(2003) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION, CHARACTERIZATION, FUNCTION AS NOS, BIOPHYSICOCHEMICAL PROPERTIES.
[7]	"Innate immunity in Arabidopsis thaliana: lipopolysaccharides activate nitric oxide synthase (NOS) and induce defense genes." Zeidler D., Zaehringer U., Gerber I., Dubery I., Hartung T., Bors W., Hutzler P., Durner J. Proc. Natl. Acad. Sci. U.S.A. 101:15811-15816(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION BY LIPOPOLYSACCHARIDES.
[8]	"Arabidopsis nitric oxide synthase1 is targeted to mitochondria and protects against oxidative damage and dark-induced senescence." Guo F.-Q., Crawford N.M. Plant Cell 17:3436-3450(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS NOS, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
[9]	"Enhanced sensitivity to oxidative stress in an Arabidopsis nitric oxide synthase mutant." Zhao M., Zhao X., Wu Y., Zhang L. J. Plant Physiol. 164:737-745(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS NOS, DISRUPTION PHENOTYPE. Strain: cv. Columbia.
[10]	"The Arabidopsis aleurone layer responds to nitric oxide, gibberellin, and abscisic acid and is sufficient and necessary for seed dormancy." Bethke P.C., Libourel I.G.L., Aoyama N., Chung Y.-Y., Still D.W., Jones R.L. Plant Physiol. 143:1173-1188(2007) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[11]	"Nitric oxide synthase-dependent nitric oxide production is associated with salt tolerance in Arabidopsis." Zhao M.-G., Tian Q.-Y., Zhang W.-H. Plant Physiol. 144:206-217(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS NOS, DISRUPTION PHENOTYPE.
[12]	"AtNOS/AtNOA1 is a functional Arabidopsis thaliana cGTPase and not a nitric-oxide synthase." Moreau M., Lee G.I., Wang Y., Crane B.R., Klessig D.F. J. Biol. Chem. 283:32957-32967(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS GTPASE, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF THR-327.
[13]	"A mutant impaired in the production of plastome-encoded proteins uncovers a mechanism for the homeostasis of isoprenoid biosynthetic enzymes in Arabidopsis plastids." Flores-Perez U., Sauret-Gueeto S., Gas E., Jarvis P., Rodriguez-Concepcion M. Plant Cell 20:1303-1315(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS GTPASE, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION. Strain: cv. Columbia.
[14]	"A signaling pathway linking nitric oxide production to heterotrimeric G protein and hydrogen peroxide regulates extracellular calmodulin induction of stomatal closure in Arabidopsis." Li J.-H., Liu Y.-Q., Lue P., Lin H.-F., Bai Y., Wang X.-C., Chen Y.-L. Plant Physiol. 150:114-124(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN NO ACCUMULATION, DISRUPTION PHENOTYPE. Strain: cv. Wassilewskija.
[15]	"AtNOA1 modulates nitric oxide accumulation and stomatal closure induced by salicylic acid in Arabidopsis." Sun L.R., Hao F.S., Lu B.S., Ma L.Y. Plant Signal. Behav. 5:1022-1024(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN NO ACCUMULATION, DISRUPTION PHENOTYPE.
[16]	"Atnoa1 mutant Arabidopsis plants induce compensation mechanisms to reduce the negative effects of the mutation." Majlath I., Szalai G., Papp I., Vankova R., Janda T. J. Plant Physiol. 168:1184-1190(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[17]	"Mechanisms for nitric oxide synthesis in plants." Crawford N.M. J. Exp. Bot. 57:471-478(2006) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON NOS.
[18]	"Hunting for plant nitric oxide synthase provides new evidence of a central role for plastids in nitric oxide metabolism." Gas E., Flores-Perez U., Sauret-Gueeto S., Rodriguez-Concepcion M. Plant Cell 21:18-23(2009) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON CONTROVERSY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL096860 Genomic DNA. Translation: CAB51217.1. Sequence problems. CP002686 Genomic DNA. Translation: AEE78282.1. CP002686 Genomic DNA. Translation: AEE78283.1. BT015353 mRNA. Translation: AAU05476.1. BT015887 mRNA. Translation: AAU95423.1. AK226195 mRNA. Translation: BAE98360.1. DQ539437 mRNA. Translation: ABG25038.1.
IPI	IPI00520335. IPI00523671.
PIR	T13000.
RefSeq	NP_190329.2. NM_114613.3. NP_850666.1. NM_180335.1.
UniGene	At.43334.
3D structure databases
ProteinModelPortal	Q66GP9.
SMR	Q66GP9. Positions 176-533.
ModBase	Search...
Proteomic databases
PaxDb	Q66GP9.
PRIDE	Q66GP9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT3G47450.2; AT3G47450.2; AT3G47450.
GeneID	823899.
KEGG	ath:AT3G47450.
Organism-specific databases
TAIR	At3g47450.
Phylogenomic databases
eggNOG	COG1161.
HOGENOM	HOG000238714.
InParanoid	Q66GP9.
KO	K13427.
OMA	DFNGSWI.
PhylomeDB	Q66GP9.
ProtClustDB	CLSN2680353.
Gene expression databases
ArrayExpress	Q66GP9.
Genevestigator	Q66GP9.
Family and domain databases
InterPro	IPR006073. GTP_binding_domain. [Graphical view]
Pfam	PF01926. MMR_HSR1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NOA1_ARATH

Accession

Primary (citable) accession number: Q66GP9
Secondary accession number(s): F4JBJ3 , Q0WWY8, Q157M8, Q9STX8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 22, 2005
Last sequence update:	October 11, 2004
Last modified:	May 1, 2013
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program