[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Omata T.; Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1007/BF00023618; PubMed=8490140 [NCBI, ExPASy, EBI, Israel, Japan] Luque I., Flores E., Herrero A.; "Nitrite reductase gene from Synechococcus sp. PCC 7942: homology between cyanobacterial and higher-plant nitrite reductases."; Plant Mol. Biol. 21:1201-1205(1993).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.; "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942."; Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 468-512. Omata T.; "Cloning and characterization of the nrtA gene that encodes a 45-kDa protein involved in nitrate transport in the cyanobacterium Synechococcus PCC 7942."; Plant Cell Physiol. 32:151-157(1991).

Comments

CATALYTIC ACTIVITY: NH₃ + 2 H₂O + 6 oxidized ferredoxin = nitrite + 6 reduced ferredoxin + 7 H⁺.
SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain family.

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

D12723; BAA02217.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X67680; CAA47912.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CP000100; ABB57270.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S33530; PQ0646.

RefSeq

YP_400257.1; -.

3D structure databases

ModBase

P39661.

Enzyme and pathway databases

BioCyc

MetaCyc:SYNPCC7942_1240-MON; -.
SELO1140:SYNPCC7942_1240-MON; -.

Ontologies

GO:0051539;	Molecular function: 4 iron, 4 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0048307;	Molecular function: ferredoxin-nitrite reductase activity (inferred from electronic annotation from EC).
GO:0020037;	Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0022900;	Biological process: electron transport chain (inferred from electronic annotation from UniProtKB-KW).
GO:0042128;	Biological process: nitrate assimilation (inferred from electronic annotation from UniProtKB-KW).
GO:0006810;	Biological process: transport (inferred from electronic annotation from UniProtKB-KW).
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.

PR00397; SIROHAEM.

PS00365; NIR_SIR; 1.

Genome annotation databases

GeneID

3773528; -.

GenomeReviews

CP000100_GR; Synpcc7942_1240.

KEGG

syf:Synpcc7942_1240; -.

Phylogenomic databases

HOGENOM

P39661; -.

Genome annotation databases

CMR

P39661; Synpcc7942_1240.

Other

UniRef

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

Keywords

4Fe-4S; Complete proteome; Electron transport; Heme; Iron; Iron-sulfur; Metal-binding; Nitrate assimilation; Oxidoreductase; Transport.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 512`	`512`	`Ferredoxin--nitrite reductase.`	`PRO_0000199957`
`METAL`	`396 396`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`402 402`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`437 437`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`441 441`		`Iron (siroheme axial ligand) (By similarity).`
`METAL`	`441 441`		`Iron-sulfur (4Fe-4S) (By similarity).`

Sequence information

Length: 512 AA [This is the length of the unprocessed precursor]

Molecular weight: 56541 Da [This is the MW of the unprocessed precursor]

CRC64: 9F469CAF60E816F0 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAQATATTEK LNKFEKLKLE KDGLAVRDQI QHFASIGWEA MDPGDREHRL KWLGIFWRPV 

        70         80         90        100        110        120 
TPGRFMARLR IPSGILQSQQ LNALANFLQR YGDQASIDIT TRQNLQLRGL LLEDTPEFLE 

       130        140        150        160        170        180 
RLHAVGLTSV QSGMDNVRNI TGSPVAGLDA AELFDTRSLI QALQDDLTAA GQGNSEFTNL 

       190        200        210        220        230        240 
PRKFNIAIEG GRDNSIHAEI NDLAFTPAYQ DGTLGFNVWV GGFFSSTRVA PAIPLNAWVP 

       250        260        270        280        290        300 
ADHSVIRLSR AILEVFRDNG SRGNRQKTRL MWLIDEWGIE RFRQVVSEAY GAPLAAAAPE 

       310        320        330        340        350        360 
LMDWEKRDFL GVHPQKQAGL NFVGLHVPVG RLTTEDLYEL ARLADTYGQG EVRLTVEQNV 

       370        380        390        400        410        420 
ILTHIPDAQL PTLLAEPLLT RFSPQPAPLS RGTVSCTGSQ YCNFALIETK QRAIAIAQSL 

       430        440        450        460        470        480 
EAELDLPRPV RIHWTGCPNS CGQPQVADIG LMGAKVRKDG QMVEGVDIFL GGKVGYDAHL 

       490        500        510 
GEKAMTGVAC EDLPDVLRQL LIERFGAQAR SH

P39661 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