NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Kinmaze;
TISSUE=Leaf;
PubMed=8541663 [NCBI, ExPASy, EBI, Israel, Japan]
Terada Y., Aoki H., Tanaka T., Morikawa H., Ida S.;
"Cloning and nucleotide sequence of a leaf ferredoxin-nitrite reductase cDNA of rice.";
Biosci. Biotechnol. Biochem. 59:2183-2185(1995).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Nipponbare;
DOI=10.1038/nature01184; PubMed=12447438 [NCBI, ExPASy, EBI, Israel, Japan]
Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y., Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H., Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M., Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M., Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T., Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S., Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H., Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y., Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S., Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y., Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S., Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H., Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
"The genome sequence and structure of rice chromosome 1.";
Nature 420:312-316(2002).

Comments

FUNCTION: Catalyzes the six-electron reduction of nitrite to ammonium.
CATALYTIC ACTIVITY: NH₃ + 2 H₂O + 6 oxidized ferredoxin = nitrite + 6 reduced ferredoxin + 7 H⁺.
COFACTOR: Binds 1 siroheme per subunit (By similarity).
COFACTOR: Binds 1 4Fe-4S cluster per subunit (By similarity).
PATHWAY: Nitrogen metabolism; nitrate reduction (assimilation).
SUBUNIT: Monomer (By similarity).
SUBCELLULAR LOCATION: Plastid, chloroplast (Probable).
SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain family.
SEQUENCE CAUTION:
- Sequence=BAD53072.1; Type=Erroneous gene model prediction;

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

D50556; BAA09122.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP003312; BAC10721.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP003312; BAD53072.1; ALT_SEQ; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JC4395; JC4395.

3D structure databases

SMR

Q42997; 55-589.

ModBase

Q42997.

Organism-specific databases

Gramene

Q42997; -.

Ontologies

GO:0048307;	Molecular function: ferredoxin-nitrite reductase activity (inferred from electronic annotation from EC).
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; 1.
PF03460; NIR_SIR_ferr; 2.
Pfam graphical view of domain structure.

PR00397; SIROHAEM.

PS00365; NIR_SIR; 1.

Genome annotation databases

NMPDR

fig|39947.1.peg.10934; -.

Other

ProtoNet

Q42997.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

4Fe-4S; Chloroplast; Electron transport; Heme; Iron; Iron-sulfur; Metal-binding; Nitrate assimilation; Oxidoreductase; Plastid; Repeat; Transit peptide; Transport.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 28`	`28`	`Chloroplast (Potential).`
`CHAIN`	`29 596`	`568`	`Ferredoxin--nitrite reductase, chloroplastic.`	`PRO_0000247480`
`METAL`	`474 474`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`480 480`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`515 515`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`519 519`		`Iron (siroheme axial ligand) (By similarity).`
`METAL`	`519 519`		`Iron-sulfur (4Fe-4S) (By similarity).`

Sequence information

Length: 596 AA [This is the length of the unprocessed precursor]

Molecular weight: 66143 Da [This is the MW of the unprocessed precursor]

CRC64: B69BC7FCD11390F5 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MASSASLQRF LPPYPHAAAS RCRPPGVRAR PVQSSTVSAP SSSTPAADEA VSAERLEPRV 

        70         80         90        100        110        120 
EQREGRYWVL KEKYRTGLNP QEKVKLGKEP MSLFMEGGIK ELAKMPMEEI EADKLSKEDI 

       130        140        150        160        170        180 
DVRLKWLGLF HRRKHQYGRF MMRLKLPNGV TTSEQTRYLA SVIEAYGKEG CADVTTRQNW 

       190        200        210        220        230        240 
QIRGVTLPDV PAILDGLNAV GLTSLQSGMD NVRNPVGNPL AGIDPDEIVD TRSYTNLLSS 

       250        260        270        280        290        300 
YITSNFQGNP TITNLPRKWN VCVIGSHDLY EHPHINDLAY MPAVKGGKFG FNLLVGGFIS 

       310        320        330        340        350        360 
PKRWEEALPL DAWVPGDDII PVCKAVLEAY RDLGTRGNRQ KTRMMWLIDE LGMEAFRSEV 

       370        380        390        400        410        420 
EKRMPNGVLE RAAPEDLIDK KWQRRDYLGV HPQKQEGMSY VGLHVPVGRV QAADMFELAR 

       430        440        450        460        470        480 
LADEYGSGEL RLTVEQNIVI PNVKNEKVEA LLSEPLLQKF SPQPSLLLKG LVACTGNQFC 

       490        500        510        520        530        540 
GQAIIETKQR ALLVTSQVEK LVSVPRAVRM HWTGCPNSCG QVQVADIGFM GCLTKDSAGK 

       550        560        570        580        590 
IVEAADIFVG GRVGSDSHLA GAYKKSVPCD ELAPIVADIL VERFGAVRRE REEDEE

Q42997 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools