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UniProtKB/Swiss-Prot entry Q39161


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name NIR_ARATH
Primary accession number Q39161
Secondary accession numbers Q8H163 Q8H164
Integrated into Swiss-Prot on October 11, 2004
Sequence was last modified on November 1, 1996 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 59)
Name and origin of the protein
Protein name Ferredoxin--nitrite reductase, chloroplastic [Precursor]
Synonyms NiR
EC 1.7.7.1
Gene name
Name: NIR1
Synonyms: NIR
OrderedLocusNames: At2g15620
ORFNames: F9O13.17
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=7894060 [NCBI, ExPASy, EBI, Israel, Japan]
Tanaka T., Ida S., Irifune K., Oeda K., Morikawa H.;
"Nucleotide sequence of a gene for nitrite reductase from Arabidopsis thaliana.";
DNA Seq. 5:57-61(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. C24;
TISSUE=Leaf;
Hara K., Komaba S., Takahashi M., Goshima N., Morikawa H.;
Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/45471; PubMed=10617197 [NCBI, ExPASy, EBI, Israel, Japan]
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
Nature 402:761-768(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
[5]
CHARACTERIZATION, AND INDUCTION.
PubMed=9161026 [NCBI, ExPASy, EBI, Israel, Japan]
Crete P., Caboche M., Meyer C.;
"Nitrite reductase expression is regulated at the post-transcriptional level by the nitrogen source in Nicotiana plumbaginifolia and Arabidopsis thaliana.";
Plant J. 11:625-634(1997).
[6]
FUNCTION, AND SUBCELLULAR LOCATION.
DOI=10.1104/pp.126.2.731; PubMed=11402201 [NCBI, ExPASy, EBI, Israel, Japan]
Takahashi M., Sasaki Y., Ida S., Morikawa H.;
"Nitrite reductase gene enrichment improves assimilation of NO(2) in Arabidopsis.";
Plant Physiol. 126:731-741(2001).
[7]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-103, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M600408-MCP200; PubMed=17272265 [NCBI, ExPASy, EBI, Israel, Japan]
Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
"Multidimensional protein identification technology (MudPIT) analysis of ubiquitinated proteins in plants.";
Mol. Cell. Proteomics 6:601-610(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
D14824; BAA03561.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB006032; BAA21672.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC006248; AAD17406.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF360320; AAK26030.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY045608; AAK73966.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY093995; AAM16256.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY142685; AAN13223.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT000685; AAN31830.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT000686; AAN31831.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR C84531; C84531.
RefSeq NP_179164.1; -.
UniGene At.21870
3D structure databases
SMR Q39161; 45-579.
ModBase Q39161.
Protein-protein interaction databases
IntAct Q39161; -.
Organism-specific databases
GeneFarm 4362; -.
TAIR At2g15620; -.
Gene expression databases
ArrayExpress Q39161; -.
GermOnline AT2G15620; Arabidopsis thaliana.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (inferred from direct assay from TAIR).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.
Family and domain databases
InterPro IPR006066; Nir_Si_BS.
IPR006067; Nir_Sir_4Fe4S.
IPR005117; NiRdtase/SiRdtase_haem-b_fer.
Graphical view of domain structure.
Pfam PF01077; NIR_SIR; 2.
PF03460; NIR_SIR_ferr; 2.
Pfam graphical view of domain structure.
PRINTS PR00397; SIROHAEM.
PROSITE PS00365; NIR_SIR; 1.
BLOCKS Q39161.
Genome annotation databases
GeneID 816055; -.
GenomeReviews CT485783_GR; AT2G15620.
KEGG ath:AT2G15620; -.
NMPDR fig|3702.1.peg.8566; -.
Other
ProtoNet Q39161.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
4Fe-4S; Chloroplast; Complete proteome; Electron transport; Heme; Iron; Iron-sulfur; Metal-binding; Nitrate assimilation; Oxidoreductase; Plastid; Repeat; Transit peptide; Transport; Ubl conjugation.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    25  25     Chloroplast (Potential). 
CHAIN   26   586  561     Ferredoxin--nitrite reductase, chloroplastic. PRO_0000019703
METAL   464   464        Iron-sulfur (4Fe-4S) (By similarity). 
METAL   470   470        Iron-sulfur (4Fe-4S) (By similarity). 
METAL   505   505        Iron-sulfur (4Fe-4S) (By similarity). 
METAL   509   509        Iron (siroheme axial ligand) (By similarity). 
METAL   509   509        Iron-sulfur (4Fe-4S) (By similarity). 
CROSSLNK   103   103        Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin). 
CONFLICT   77    77        R -> G (in Ref. 4; AAN31831). 
CONFLICT   214   214        P -> Q (in Ref. 4; AAN31830). 
Sequence information
Length: 586 AA [This is the length of the unprocessed precursor] Molecular weight: 65505 Da [This is the MW of the unprocessed precursor] CRC64: 6AACF1FE9FF7E1F2 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTSFSLTFTS PLLPSSSTKP KRSVLVAAAQ TTAPAESTAS VDADRLEPRV ELKDGFFILK 

        70         80         90        100        110        120 
EKFRKGINPQ EKVKIEREPM KLFMENGIEE LAKKSMEELD SEKSSKDDID VRLKWLGLFH 

       130        140        150        160        170        180 
RRKHQYGKFM MRLKLPNGVT TSAQTRYLAS VIRKYGEDGC ADVTTRQNWQ IRGVVLPDVP 

       190        200        210        220        230        240 
EILKGLASVG LTSLQSGMDN VRNPVGNPIA GIDPEEIVDT RPYTNLLSQF ITANSQGNPD 

       250        260        270        280        290        300 
FTNLPRKWNV CVVGTHDLYE HPHINDLAYM PANKDGRFGF NLLVGGFFSP KRCEEAIPLD 

       310        320        330        340        350        360 
AWVPADDVLP LCKAVLEAYR DLGTRGNRQK TRMMWLIDEL GVEGFRTEVE KRMPNGKLER 

       370        380        390        400        410        420 
GSSEDLVNKQ WERRDYFGVN PQKQEGLSFV GLHVPVGRLQ ADDMDELARL ADTYGSGELR 

       430        440        450        460        470        480 
LTVEQNIIIP NVETSKTEAL LQEPFLKNRF SPEPSILMKG LVACTGSQFC GQAIIETKLR 

       490        500        510        520        530        540 
ALKVTEEVER LVSVPRPIRM HWTGCPNTCG QVQVADIGFM GCLTRGEEGK PVEGADVYVG 

       550        560        570        580 
GRIGSDSHIG EIYKKGVRVT ELVPLVAEIL IKEFGAVPRE REENED 

Q39161 in FASTA format

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