Nitrite reductase [NAD(P)H] large subunit - Escherichia coli (strain K12)

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P08201 (NIRB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 129. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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

Gene names

Name:	nirB
Ordered Locus Names:	b3365, JW3328

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	847 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	Ammonium hydroxide + 3 NAD(P)⁺ + H₂O = nitrite + 3 NAD(P)H.
Cofactor	Binds 1 siroheme per subunit. Binds 1 4Fe-4S cluster per subunit. FAD.
Pathway	Nitrogen metabolism; nitrate reduction (assimilation).
Subunit structure	Homodimer which associates with NirD.
Sequence similarities	Belongs to the nitrite and sulfite reductase 4Fe-4S domain family.

Ontologies

Keywords
Biological process	Nitrate assimilation
Ligand	4Fe-4S FAD Flavoprotein Heme Iron Iron-sulfur Metal-binding NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	anaerobic respiration Inferred from expression pattern PubMed 2173895. Source: EcoCyc nitrate assimilation Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	nitrite reductase complex [NAD(P)H] Inferred from direct assay PubMed 217342 PubMed 6279095. Source: EcoCyc
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW NADP binding Inferred from direct assay PubMed 217342. Source: EcoCyc flavin adenine dinucleotide binding Inferred from direct assay PubMed 7030314. Source: EcoCyc heme binding Inferred from direct assay PubMed 7030314. Source: EcoCyc iron-sulfur cluster binding Inferred from direct assay PubMed 6297458. Source: EcoCyc metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW nitrite reductase [NAD(P)H] activity Inferred from direct assay PubMed 1435259 PubMed 217342. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 847

847

Nitrite reductase [NAD(P)H] large subunit

PRO_0000199962

Regions

Nucleotide binding

44 – 79

FAD Potential

Nucleotide binding

193 – 225

NAD or NADP Potential

Sites

Metal binding

641

Iron-sulfur (4Fe-4S) By similarity

Metal binding

647

Iron-sulfur (4Fe-4S) By similarity

Metal binding

681

Iron-sulfur (4Fe-4S) By similarity

Metal binding

685

Iron (siroheme axial ligand) By similarity

Metal binding

685

Iron-sulfur (4Fe-4S) By similarity

Experimental info

Sequence conflict

442

G → A Ref.1

Sequence conflict

442

G → A Ref.2

Sequence conflict

835 – 847

YERIP…VEDNA → MNVSQ Ref.1

Sequence conflict

835 – 847

YERIP…VEDNA → MNVSQ Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P08201 [UniParc].

Last modified November 1, 1995. Version 4.
Checksum: 5265AD93FD390EB4
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FASTA

847

93,121

        10         20         30         40         50         60 
MSKVRLAIIG NGMVGHRFIE DLLDKSDAAN FDITVFCEEP RIAYDRVHLS SYFSHHTAEE 

        70         80         90        100        110        120 
LSLVREGFYE KHGIKVLVGE RAITINRQEK VIHSSAGRTV FYDKLIMATG SYPWIPPIKG 

       130        140        150        160        170        180 
SDTQDCFVYR TIEDLNAIES CARRSKRGAV VGGGLLGLEA AGALKNLGIE THVIEFAPML 

       190        200        210        220        230        240 
MAEQLDQMGG EQLRRKIESM GVRVHTSKNT LEIVQEGVEA RKTMRFADGS ELEVDFIVFS 

       250        260        270        280        290        300 
TGIRPRDKLA TQCGLDVAPR GGIVINDSCQ TSDPDIYAIG ECASWNNRVF GLVAPGYKMA 

       310        320        330        340        350        360 
QVAVDHILGS ENAFEGADLS AKLKLLGVDV GGIGDAHGRT PGARSYVYLD ESKEIYKRLI 

       370        380        390        400        410        420 
VSEDNKTLLG AVLVGDTSDY GNLLQLVLNA IELPENPDSL ILPAHSGSGK PSIGVDKLPD 

       430        440        450        460        470        480 
SAQICSCFDV TKGDLIAAIN KGCHTVAALK AETKAGTGCG GCIPLVTQVL NAELAKQGIE 

       490        500        510        520        530        540 
VNNNLCEHFA YSRQELFHLI RVEGIKTFEE LLAKHGKGYG CEVCKPTVGS LLASCWNEYI 

       550        560        570        580        590        600 
LKPEHTPLQD SNDNFLANIQ KDGTYSVIPR SPGGEITPEG LMAVGRIARE FNLYTKITGS 

       610        620        630        640        650        660 
QRLAMFGAQK DDLPEIWRQL IEAGFETGHA YAKALRMAKT CVGSTWCRYG VGDSVGLGVE 

       670        680        690        700        710        720 
LENRYKGIRT PHKMKFGVSG CTRECSEAQG KDVGIIATEK GWNLYVCGNG GMKPRHADLL 

       730        740        750        760        770        780 
AADIDRETLI KYLDRFMMFY IRTADKLTRT APWLENLEGG IDYLKAVIID DKLGLNAHLE 

       790        800        810        820        830        840 
EEMARLREAV LCEWTETVNT PSAQTRFKHF INSDKRDPNV QMVPEREQHR PATPYERIPV 


TLVEDNA

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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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Location and sequence of the promoter of the gene for the NADH-dependent nitrite reductase of Escherichia coli and its regulation by oxygen, the Fnr protein and nitrite." Jayaraman P.S., Peakman T.C., Busby S.J.W., Quincey R.V., Cole J.A. J. Mol. Biol. 196:781-788(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X14202 Genomic DNA. Translation: CAA32416.1. U18997 Genomic DNA. Translation: AAA58162.1. U00096 Genomic DNA. Translation: AAC76390.1. AP009048 Genomic DNA. Translation: BAE77925.1.
PIR	H65130.
RefSeq	NP_417824.1. NC_000913.2. YP_492066.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P08201.
SMR	P08201. Positions 3-400.
ModBase	Search...
Protein-protein interaction databases
STRING	511145.b3365.
Proteomic databases
PaxDb	P08201.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC76390; AAC76390; b3365. BAE77925; BAE77925; BAE77925.
GeneID	12932093. 947868.
KEGG	ecj:Y75_p3810. eco:b3365.
PATRIC	32122164. VBIEscCol129921_3459.
Organism-specific databases
EchoBASE	EB0647.
EcoGene	EG10653. nirB.
Phylogenomic databases
eggNOG	COG1251.
HOGENOM	HOG000196164.
KO	K00362.
OMA	QRNGTFS.
ProtClustDB	PRK14989.
Enzyme and pathway databases
BioCyc	EcoCyc:NIRB-MONOMER. ECOL316407:JW3328-MONOMER. MetaCyc:NIRB-MONOMER.
UniPathway	UPA00653.
Gene expression databases
Genevestigator	P08201.
Family and domain databases
InterPro	IPR007419. BFD-like_2Fe2S-bd_dom. IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR005117. NiRdtase/SiRdtase_haem-b_fer. IPR012744. Nitri_red_NirB. IPR017121. Nitrite_Rdtase_lsu. IPR006067. NO2/SO3_Rdtase_4Fe4S_dom. IPR006066. NO2/SO3_Rdtase_FeS/sirohaem_BS. IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD. IPR001327. Pyr_OxRdtase_NAD-bd_dom. [Graphical view]
Pfam	PF04324. Fer2_BFD. 1 hit. PF01077. NIR_SIR. 1 hit. PF03460. NIR_SIR_ferr. 1 hit. PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. [Graphical view]
PIRSF	PIRSF037149. NirB. 1 hit.
PRINTS	PR00368. FADPNR. PR00397. SIROHAEM.
SUPFAM	SSF55124. NiR_SiRalpha_1/3. 1 hit.
TIGRFAMs	TIGR02374. nitri_red_nirB. 1 hit.
PROSITE	PS00365. NIR_SIR. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NIRB_ECOLI

Accession

Primary (citable) accession number: P08201
Secondary accession number(s): Q2M731

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	November 1, 1995
Last modified:	May 1, 2013
This is version 129 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents