[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=K12; DOI=10.1093/nar/17.10.3865; PubMed=2543955 [NCBI, ExPASy, EBI, Israel, Japan] Bell A.I., Gaston K.L., Cole J.A., Busby S.J.W.; "Cloning of binding sequences for the Escherichia coli transcription activators, FNR and CRP: location of bases involved in discrimination between FNR and CRP."; Nucleic Acids Res. 17:3865-3874(1989).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=K12; PubMed=2200672 [NCBI, ExPASy, EBI, Israel, Japan] Peakman T., Crouzet J., Mayaux J.F., Busby S.J.W., Mohan S., Harborne N., Wootton J., Nicolson R., Cole J.A.; "Nucleotide sequence, organisation and structural analysis of the products of genes in the nirB-cysG region of the Escherichia coli K-12 chromosome."; Eur. J. Biochem. 191:315-323(1990).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.; "The complete genome sequence of Escherichia coli K-12."; Science 277:1453-1474(1997).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."; Mol. Syst. Biol. 2:E1-E5(2006).
[5]	FUNCTION. PubMed=1435259 [NCBI, ExPASy, EBI, Israel, Japan] Harborne N., Griffiths L., Busby S.J., Cole J.A.; "Transcriptional control, translation and function of the products of the five open reading frames of the Escherichia coli nir operon."; Mol. Microbiol. 6:2805-2813(1992).

Comments

FUNCTION: Required for activity of the reductase.
CATALYTIC ACTIVITY: Ammonium hydroxide + 3 NAD(P)⁺ + H₂O = nitrite + 3 NAD(P)H.
SUBUNIT: Associates with nirB.
SUBCELLULAR LOCATION: Cytoplasm.
SIMILARITY: To B.subtilis nasE.

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

X14202; CAA32417.1; ALT_SEQ; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U18997; AAA58163.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC76391.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE77924.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A65131; A65131.

RefSeq

AP_004423.1; -.
NP_417825.1; -.

3D structure databases

PDB

2JO6; NMR; -; A=1-108.

[ExPASy / RCSB / EBI]

PDBsum

2JO6; -.

ModBase

P0A9I8.

Enzyme and pathway databases

BioCyc

EcoCyc:NIRD-MON; -.
MetaCyc:NIRD-MON; -.

Organism-specific databases

EchoBASE

EB0649; -.

EcoGene

EG10655; nirD.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0051537;	Molecular function: 2 iron, 2 sulfur cluster binding (inferred from electronic annotation from InterPro).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0008942;	Molecular function: nitrite reductase [NAD(P)H] activity (inferred from electronic annotation from InterPro).
GO:0042128;	Biological process: nitrate assimilation (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR012748; Nitri_red_NirD.
IPR005806; Rieske_reg.
Graphical view of domain structure.

Gene3D

G3DSA:2.102.10.10; Rieske_reg; 1.

TIGRFAMs

TIGR02378; nirD_assim_sml; 1.

PROSITE

PS51300; NIRD; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

GeneID

947881; -.

GenomeReviews

AP009048_GR; JW3329.
U00096_GR; b3366.

KEGG

ecj:JW3329; -.
eco:b3366; -.

Phylogenomic databases

HOGENOM

P0A9I8; -.

Genome annotation databases

CMR

P0A9I8; b3366.

Other

ProtoNet

P0A9I8.

UniRef

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

Keywords

3D-structure; Complete proteome; Cytoplasm; NAD; Nitrate assimilation; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 108`	`108`	`Nitrite reductase [NAD(P)H] small subunit.`	`PRO_0000096855`
`CONFLICT`	`102 102`		`G -> D (in Ref. 1 and 2).`
`STRAND`	`5 9`	`5`
`TURN`	`10 12`	`3`
`STRAND`	`17 23`	`7`
`STRAND`	`26 32`	`7`
`STRAND`	`34 37`	`4`
`STRAND`	`40 45`	`6`
`STRAND`	`47 49`	`3`
`STRAND`	`57 62`	`6`
`STRAND`	`65 70`	`6`
`TURN`	`71 74`	`4`
`STRAND`	`75 78`	`4`
`TURN`	`79 82`	`4`
`TURN`	`85 90`	`6`
`STRAND`	`94 100`	`7`
`STRAND`	`103 107`	`5`

Sequence information

Length: 108 AA [This is the length of the unprocessed precursor]

Molecular weight: 12284 Da [This is the MW of the unprocessed precursor]

CRC64: 4B16AAE73EC4B786 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSQWKDICKI DDILPETGVC ALLGDEQVAI FRPYHSDQVF AISNIDPFFE SSVLSRGLIA 

        70         80         90        100 
EHQGELWVAS PLKKQRFRLS DGLCMEDEQF SVKHYEARVK DGVVQLRG

P0A9I8 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