Reviewed, UniProtKB/Swiss-Prot P0A9I8 (NIRD_ECOLI)

Names and origin

Protein names

Recommended name:
    Nitrite reductase [NAD(P)H] small subunit
    EC=1.7.1.4

Gene names

Name:	nirD
Ordered Locus Names:	b3366, JW3329

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	108 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Required for activity of the reductase. Ref.5
Catalytic activity	Ammonium hydroxide + 3 NAD(P)+ + H2O = nitrite + 3 NAD(P)H.
Subunit structure	Associates with nirB.
Subcellular location	Cytoplasm.
Sequence similarities	To B.subtilis nasE.

Ontologies

Keywords
Biological process	Nitrate assimilation
Cellular component	Cytoplasm
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	nitrate assimilation Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro nitrite reductase [NAD(P)H] activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 108

108

Nitrite reductase [NAD(P)H] small subunit

PRO_0000096855

Experimental info

Sequence conflict

102

1

G → D Ref.1

Sequence conflict

102

1

G → D Ref.2

Secondary structure

1

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108

Helix Strand Turn

Details...

Beta strand

5 – 9

5

Turn

10 – 12

3

Beta strand

17 – 23

7

Beta strand

26 – 32

7

Beta strand

34 – 37

4

Beta strand

40 – 45

6

Beta strand

47 – 49

3

Beta strand

57 – 62

6

Beta strand

65 – 70

6

Turn

71 – 74

4

Beta strand

75 – 78

4

Turn

79 – 82

4

Turn

85 – 90

6

Beta strand

94 – 100

7

Beta strand

103 – 107

5

Sequences

	Sequence		Length	Mass (Da)
	P0A9I8-1 [UniParc]. Last modified July 19, 2005. Version 1. Checksum: 4B16AAE73EC4B786	FASTA	108	12,284
	10 20 30 40 50 60 MSQWKDICKI DDILPETGVC ALLGDEQVAI FRPYHSDQVF AISNIDPFFE SSVLSRGLIA 70 80 90 100 EHQGELWVAS PLKKQRFRLS DGLCMEDEQF SVKHYEARVK DGVVQLRG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of binding sequences for the Escherichia coli transcription activators, FNR and CRP: location of bases involved in discrimination between FNR and CRP." Bell A.I., Gaston K.L., Cole J.A., Busby S.J.W. Nucleic Acids Res. 17:3865-3874(1989) [PubMed: 2543955] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"Nucleotide sequence, organisation and structural analysis of the products of genes in the nirB-cysG region of the Escherichia coli K-12 chromosome." Peakman T., Crouzet J., Mayaux J.F., Busby S.J.W., Mohan S., Harborne N., Wootton J., Nicolson R., Cole J.A. Eur. J. Biochem. 191:315-323(1990) [PubMed: 2200672] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[3]	"The complete genome sequence of Escherichia coli K-12." 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. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Transcriptional control, translation and function of the products of the five open reading frames of the Escherichia coli nir operon." Harborne N., Griffiths L., Busby S.J., Cole J.A. Mol. Microbiol. 6:2805-2813(1992) [PubMed: 1435259] [Abstract] Cited for: FUNCTION.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X14202 Genomic DNA. Translation: CAA32417.1. Sequence problems.
U18997 Genomic DNA. Translation: AAA58163.1.
U00096 Genomic DNA. Translation: AAC76391.1.
AP009048 Genomic DNA. Translation: BAE77924.1.

PIR

A65131.

RefSeq

AP_004423.1.
NP_417825.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2JO6	NMR	-	A	1-108	[»]

ModBase

Search...

Genome annotation databases

GeneID

947881.

GenomeReviews

Gene locus JW3329 in contig AP009048_GR.
Gene locus b3366 in contig U00096_GR.

KEGG

ecj:JW3329.
eco:b3366.

Organism-specific databases

EchoBASE

EB0649.

EcoGene

EG10655. nirD.

CMR

Search...

Phylogenomic databases

HOGENOM

P0A9I8.

OMA

P0A9I8. GVCALVE.

Enzyme and pathway databases

BioCyc

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

Family and domain databases

InterPro

IPR012748. Nitri_red_NirD.
IPR017881. Nitrite_Rdtase_lsu_NirD_bac.
IPR017941. Rieske_2Fe-2S.
[Graphical view]

Gene3D

G3DSA:2.102.10.10. Rieske_reg. 1 hit.

TIGRFAMs

TIGR02378. nirD_assim_sml. 1 hit.

PROSITE

PS51300. NIRD. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

NIRD_ECOLI

Accession

Primary (citable) accession number: P0A9I8
Secondary accession number(s): P23675, Q2M732

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2005
Last sequence update:	July 19, 2005
Last modified:	June 16, 2009
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)