NIRD_ECOLI
ID NIRD_ECOLI Reviewed; 108 AA.
AC P0A9I8; P23675; Q2M732;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Nitrite reductase (NADH) small subunit;
DE EC=1.7.1.15;
GN Name=nirD; OrderedLocusNames=b3366, JW3329;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2543955; DOI=10.1093/nar/17.10.3865;
RA Bell A.I., Gaston K.L., Cole J.A., Busby S.J.W.;
RT "Cloning of binding sequences for the Escherichia coli transcription
RT activators, FNR and CRP: location of bases involved in discrimination
RT between FNR and CRP.";
RL Nucleic Acids Res. 17:3865-3874(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2200672; DOI=10.1111/j.1432-1033.1990.tb19125.x;
RA Peakman T., Crouzet J., Mayaux J.F., Busby S.J.W., Mohan S., Harborne N.,
RA Wootton J., Nicolson R., Cole J.A.;
RT "Nucleotide sequence, organisation and structural analysis of the products
RT of genes in the nirB-cysG region of the Escherichia coli K-12 chromosome.";
RL Eur. J. Biochem. 191:315-323(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION.
RX PubMed=1435259; DOI=10.1111/j.1365-2958.1992.tb01460.x;
RA Harborne N., Griffiths L., Busby S.J., Cole J.A.;
RT "Transcriptional control, translation and function of the products of the
RT five open reading frames of the Escherichia coli nir operon.";
RL Mol. Microbiol. 6:2805-2813(1992).
CC -!- FUNCTION: Required for activity of the reductase.
CC {ECO:0000269|PubMed:1435259}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H2O + 3 NAD(+) + NH4(+) = 5 H(+) + 3 NADH + nitrite;
CC Xref=Rhea:RHEA:24628, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16301, ChEBI:CHEBI:28938, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.7.1.15;
CC -!- SUBUNIT: Associates with NirB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: To B.subtilis NasE. {ECO:0000305}.
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DR EMBL; X14202; CAA32417.1; ALT_SEQ; Genomic_DNA.
DR EMBL; U18997; AAA58163.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76391.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77924.1; -; Genomic_DNA.
DR PIR; A65131; A65131.
DR RefSeq; NP_417825.1; NC_000913.3.
DR RefSeq; WP_000084764.1; NZ_STEB01000004.1.
DR PDB; 2JO6; NMR; -; A=1-108.
DR PDBsum; 2JO6; -.
DR AlphaFoldDB; P0A9I8; -.
DR SMR; P0A9I8; -.
DR BioGRID; 4262476; 15.
DR STRING; 511145.b3366; -.
DR jPOST; P0A9I8; -.
DR PaxDb; P0A9I8; -.
DR PRIDE; P0A9I8; -.
DR DNASU; 947881; -.
DR EnsemblBacteria; AAC76391; AAC76391; b3366.
DR EnsemblBacteria; BAE77924; BAE77924; BAE77924.
DR GeneID; 67416998; -.
DR GeneID; 947881; -.
DR KEGG; ecj:JW3329; -.
DR KEGG; eco:b3366; -.
DR PATRIC; fig|1411691.4.peg.3363; -.
DR EchoBASE; EB0649; -.
DR eggNOG; COG2146; Bacteria.
DR HOGENOM; CLU_055690_3_0_6; -.
DR InParanoid; P0A9I8; -.
DR OMA; IDNRDPF; -.
DR PhylomeDB; P0A9I8; -.
DR BioCyc; EcoCyc:NIRD-MON; -.
DR BioCyc; MetaCyc:NIRD-MON; -.
DR BRENDA; 1.7.1.15; 2026.
DR EvolutionaryTrace; P0A9I8; -.
DR PRO; PR:P0A9I8; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009344; C:nitrite reductase complex [NAD(P)H]; IDA:EcoCyc.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0008942; F:nitrite reductase [NAD(P)H] activity; IDA:EcoCyc.
DR GO; GO:0106316; F:nitrite reductase NADH activity; IEA:RHEA.
DR GO; GO:0009061; P:anaerobic respiration; IEP:EcoCyc.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR CDD; cd03529; Rieske_NirD; 1.
DR Gene3D; 2.102.10.10; -; 1.
DR InterPro; IPR017881; NirD.
DR InterPro; IPR012748; Rieske-like_NirD.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR PANTHER; PTHR40562; PTHR40562; 1.
DR Pfam; PF13806; Rieske_2; 1.
DR SUPFAM; SSF50022; SSF50022; 1.
DR TIGRFAMs; TIGR02378; nirD_assim_sml; 1.
DR PROSITE; PS51300; NIRD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; NAD; Nitrate assimilation; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..108
FT /note="Nitrite reductase (NADH) small subunit"
FT /id="PRO_0000096855"
FT CONFLICT 102
FT /note="G -> D (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:2JO6"
FT TURN 10..12
FT /evidence="ECO:0007829|PDB:2JO6"
FT STRAND 17..23
FT /evidence="ECO:0007829|PDB:2JO6"
FT STRAND 26..32
FT /evidence="ECO:0007829|PDB:2JO6"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:2JO6"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:2JO6"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:2JO6"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:2JO6"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:2JO6"
FT TURN 71..74
FT /evidence="ECO:0007829|PDB:2JO6"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:2JO6"
FT TURN 79..82
FT /evidence="ECO:0007829|PDB:2JO6"
FT TURN 85..90
FT /evidence="ECO:0007829|PDB:2JO6"
FT STRAND 94..100
FT /evidence="ECO:0007829|PDB:2JO6"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:2JO6"
SQ SEQUENCE 108 AA; 12284 MW; 4B16AAE73EC4B786 CRC64;
MSQWKDICKI DDILPETGVC ALLGDEQVAI FRPYHSDQVF AISNIDPFFE SSVLSRGLIA
EHQGELWVAS PLKKQRFRLS DGLCMEDEQF SVKHYEARVK DGVVQLRG
