ID NIRB_ECOLI Reviewed; 847 AA.
AC P08201; Q2M731;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 4.
DT 27-MAR-2024, entry version 193.
DE RecName: Full=Nitrite reductase (NADH) large subunit;
DE EC=1.7.1.15;
GN Name=nirB; OrderedLocusNames=b3365, JW3328;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; 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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RX PubMed=2445993; DOI=10.1016/0022-2836(87)90404-9;
RA Jayaraman P.S., Peakman T.C., Busby S.J.W., Quincey R.V., Cole J.A.;
RT "Location and sequence of the promoter of the gene for the NADH-dependent
RT nitrite reductase of Escherichia coli and its regulation by oxygen, the Fnr
RT protein and nitrite.";
RL J. Mol. Biol. 196:781-788(1987).
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 -!- COFACTOR:
CC Name=siroheme; Xref=ChEBI:CHEBI:60052;
CC Note=Binds 1 siroheme per subunit.;
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Note=Binds 1 [4Fe-4S] cluster per subunit.;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC -!- PATHWAY: Nitrogen metabolism; nitrate reduction (assimilation).
CC -!- SUBUNIT: Homodimer which associates with NirD.
CC -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain
CC family. {ECO:0000305}.
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DR EMBL; X14202; CAA32416.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58162.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76390.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77925.1; -; Genomic_DNA.
DR PIR; H65130; H65130.
DR RefSeq; NP_417824.1; NC_000913.3.
DR RefSeq; WP_000049208.1; NZ_SSZK01000008.1.
DR AlphaFoldDB; P08201; -.
DR SMR; P08201; -.
DR BioGRID; 4261087; 21.
DR BioGRID; 852179; 1.
DR IntAct; P08201; 1.
DR STRING; 511145.b3365; -.
DR jPOST; P08201; -.
DR PaxDb; 511145-b3365; -.
DR EnsemblBacteria; AAC76390; AAC76390; b3365.
DR GeneID; 947868; -.
DR KEGG; ecj:JW3328; -.
DR KEGG; eco:b3365; -.
DR PATRIC; fig|1411691.4.peg.3364; -.
DR EchoBASE; EB0647; -.
DR eggNOG; COG1251; Bacteria.
DR HOGENOM; CLU_003291_0_0_6; -.
DR InParanoid; P08201; -.
DR OMA; MWGGVTN; -.
DR OrthoDB; 9768666at2; -.
DR PhylomeDB; P08201; -.
DR BioCyc; EcoCyc:NIRB-MONOMER; -.
DR BioCyc; MetaCyc:NIRB-MONOMER; -.
DR UniPathway; UPA00653; -.
DR PRO; PR:P08201; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009344; C:nitrite reductase complex [NAD(P)H]; IDA:EcoCyc.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:EcoCyc.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:EcoCyc.
DR GO; GO:0020037; F:heme binding; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0106316; F:nitrite reductase NADH activity; IDA:EcoCyc.
DR GO; GO:0006113; P:fermentation; IMP:EcoCyc.
DR GO; GO:0006116; P:NADH oxidation; IMP:EcoCyc.
DR GO; GO:0042128; P:nitrate assimilation; IMP:EcoCyc.
DR CDD; cd19943; NirB_Fer2_BFD-like_1; 1.
DR CDD; cd19944; NirB_Fer2_BFD-like_2; 1.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.90.480.20; -; 1.
DR Gene3D; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 3.30.413.10; Sulfite Reductase Hemoprotein, domain 1; 1.
DR InterPro; IPR007419; BFD-like_2Fe2S-bd_dom.
DR InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR005117; NiRdtase/SiRdtase_haem-b_fer.
DR InterPro; IPR036136; Nit/Sulf_reduc_fer-like_dom_sf.
DR InterPro; IPR012744; Nitri_red_NirB.
DR InterPro; IPR017121; Nitrite_Rdtase_lsu.
DR InterPro; IPR006067; NO2/SO3_Rdtase_4Fe4S_dom.
DR InterPro; IPR045854; NO2/SO3_Rdtase_4Fe4S_sf.
DR InterPro; IPR006066; NO2/SO3_Rdtase_FeS/sirohaem_BS.
DR InterPro; IPR041575; Rubredoxin_C.
DR NCBIfam; TIGR02374; nitri_red_nirB; 1.
DR PANTHER; PTHR43809; NITRITE REDUCTASE (NADH) LARGE SUBUNIT; 1.
DR PANTHER; PTHR43809:SF1; NITRITE REDUCTASE (NADH) LARGE SUBUNIT; 1.
DR Pfam; PF04324; Fer2_BFD; 1.
DR Pfam; PF01077; NIR_SIR; 1.
DR Pfam; PF03460; NIR_SIR_ferr; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF18267; Rubredoxin_C; 1.
DR PIRSF; PIRSF037149; NirB; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR PRINTS; PR00397; SIROHAEM.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR SUPFAM; SSF56014; Nitrite and sulphite reductase 4Fe-4S domain-like; 1.
DR SUPFAM; SSF55124; Nitrite/Sulfite reductase N-terminal domain-like; 1.
DR PROSITE; PS00365; NIR_SIR; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; FAD; Flavoprotein; Heme; Iron; Iron-sulfur; Metal-binding; NAD;
KW Nitrate assimilation; Oxidoreductase; Reference proteome.
FT CHAIN 1..847
FT /note="Nitrite reductase (NADH) large subunit"
FT /id="PRO_0000199962"
FT BINDING 44..79
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 193..225
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT BINDING 641
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 647
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 681
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 685
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 685
FT /ligand="siroheme"
FT /ligand_id="ChEBI:CHEBI:60052"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT CONFLICT 442
FT /note="G -> A (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 835..847
FT /note="YERIPVTLVEDNA -> MNVSQ (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 847 AA; 93121 MW; 5265AD93FD390EB4 CRC64;
MSKVRLAIIG NGMVGHRFIE DLLDKSDAAN FDITVFCEEP RIAYDRVHLS SYFSHHTAEE
LSLVREGFYE KHGIKVLVGE RAITINRQEK VIHSSAGRTV FYDKLIMATG SYPWIPPIKG
SDTQDCFVYR TIEDLNAIES CARRSKRGAV VGGGLLGLEA AGALKNLGIE THVIEFAPML
MAEQLDQMGG EQLRRKIESM GVRVHTSKNT LEIVQEGVEA RKTMRFADGS ELEVDFIVFS
TGIRPRDKLA TQCGLDVAPR GGIVINDSCQ TSDPDIYAIG ECASWNNRVF GLVAPGYKMA
QVAVDHILGS ENAFEGADLS AKLKLLGVDV GGIGDAHGRT PGARSYVYLD ESKEIYKRLI
VSEDNKTLLG AVLVGDTSDY GNLLQLVLNA IELPENPDSL ILPAHSGSGK PSIGVDKLPD
SAQICSCFDV TKGDLIAAIN KGCHTVAALK AETKAGTGCG GCIPLVTQVL NAELAKQGIE
VNNNLCEHFA YSRQELFHLI RVEGIKTFEE LLAKHGKGYG CEVCKPTVGS LLASCWNEYI
LKPEHTPLQD SNDNFLANIQ KDGTYSVIPR SPGGEITPEG LMAVGRIARE FNLYTKITGS
QRLAMFGAQK DDLPEIWRQL IEAGFETGHA YAKALRMAKT CVGSTWCRYG VGDSVGLGVE
LENRYKGIRT PHKMKFGVSG CTRECSEAQG KDVGIIATEK GWNLYVCGNG GMKPRHADLL
AADIDRETLI KYLDRFMMFY IRTADKLTRT APWLENLEGG IDYLKAVIID DKLGLNAHLE
EEMARLREAV LCEWTETVNT PSAQTRFKHF INSDKRDPNV QMVPEREQHR PATPYERIPV
TLVEDNA
//
