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P08201

- NIRB_ECOLI

UniProt

P08201 - NIRB_ECOLI

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Protein

Nitrite reductase (NADH) large subunit

Gene

nirB

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi

Functioni

Catalytic activityi

Ammonia + 3 NAD+ + 2 H2O = nitrite + 3 NADH.

Cofactori

Binds 1 siroheme per subunit.
Binds 1 4Fe-4S cluster per subunit.
FAD.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi641 – 6411Iron-sulfur (4Fe-4S)By similarity
Metal bindingi647 – 6471Iron-sulfur (4Fe-4S)By similarity
Metal bindingi681 – 6811Iron-sulfur (4Fe-4S)By similarity
Metal bindingi685 – 6851Iron (siroheme axial ligand)By similarity
Metal bindingi685 – 6851Iron-sulfur (4Fe-4S)By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi44 – 7936FADSequence AnalysisAdd
BLAST
Nucleotide bindingi193 – 22533NAD or NADPSequence AnalysisAdd
BLAST

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  2. flavin adenine dinucleotide binding Source: EcoCyc
  3. heme binding Source: EcoCyc
  4. iron-sulfur cluster binding Source: EcoCyc
  5. metal ion binding Source: UniProtKB-KW
  6. NADP binding Source: EcoCyc
  7. nitrite reductase [NAD(P)H] activity Source: EcoCyc

GO - Biological processi

  1. anaerobic respiration Source: EcoCyc
  2. nitrate assimilation Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Nitrate assimilation

Keywords - Ligandi

4Fe-4S, FAD, Flavoprotein, Heme, Iron, Iron-sulfur, Metal-binding, NAD

Enzyme and pathway databases

BioCyciEcoCyc:NIRB-MONOMER.
ECOL316407:JW3328-MONOMER.
MetaCyc:NIRB-MONOMER.
UniPathwayiUPA00653.

Names & Taxonomyi

Protein namesi
Recommended name:
Nitrite reductase (NADH) large subunit (EC:1.7.1.15)
Gene namesi
Name:nirB
Ordered Locus Names:b3365, JW3328
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10653. nirB.

Subcellular locationi

GO - Cellular componenti

  1. nitrite reductase complex [NAD(P)H] Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 847847Nitrite reductase (NADH) large subunitPRO_0000199962Add
BLAST

Proteomic databases

PaxDbiP08201.

Expressioni

Gene expression databases

GenevestigatoriP08201.

Interactioni

Subunit structurei

Homodimer which associates with NirD.

Protein-protein interaction databases

IntActiP08201. 1 interaction.
STRINGi511145.b3365.

Structurei

3D structure databases

ProteinModelPortaliP08201.
SMRiP08201. Positions 3-400.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1251.
HOGENOMiHOG000196164.
InParanoidiP08201.
KOiK00362.
OMAiIRSPHKI.
OrthoDBiEOG6G4VT5.
PhylomeDBiP08201.

Family and domain databases

InterProiIPR007419. 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]
PfamiPF04324. 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]
PIRSFiPIRSF037149. NirB. 1 hit.
PRINTSiPR00368. FADPNR.
PR00397. SIROHAEM.
SUPFAMiSSF55124. SSF55124. 1 hit.
TIGRFAMsiTIGR02374. nitri_red_nirB. 1 hit.
PROSITEiPS00365. NIR_SIR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P08201-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSKVRLAIIG NGMVGHRFIE DLLDKSDAAN FDITVFCEEP RIAYDRVHLS
60 70 80 90 100
SYFSHHTAEE LSLVREGFYE KHGIKVLVGE RAITINRQEK VIHSSAGRTV
110 120 130 140 150
FYDKLIMATG SYPWIPPIKG SDTQDCFVYR TIEDLNAIES CARRSKRGAV
160 170 180 190 200
VGGGLLGLEA AGALKNLGIE THVIEFAPML MAEQLDQMGG EQLRRKIESM
210 220 230 240 250
GVRVHTSKNT LEIVQEGVEA RKTMRFADGS ELEVDFIVFS TGIRPRDKLA
260 270 280 290 300
TQCGLDVAPR GGIVINDSCQ TSDPDIYAIG ECASWNNRVF GLVAPGYKMA
310 320 330 340 350
QVAVDHILGS ENAFEGADLS AKLKLLGVDV GGIGDAHGRT PGARSYVYLD
360 370 380 390 400
ESKEIYKRLI VSEDNKTLLG AVLVGDTSDY GNLLQLVLNA IELPENPDSL
410 420 430 440 450
ILPAHSGSGK PSIGVDKLPD SAQICSCFDV TKGDLIAAIN KGCHTVAALK
460 470 480 490 500
AETKAGTGCG GCIPLVTQVL NAELAKQGIE VNNNLCEHFA YSRQELFHLI
510 520 530 540 550
RVEGIKTFEE LLAKHGKGYG CEVCKPTVGS LLASCWNEYI LKPEHTPLQD
560 570 580 590 600
SNDNFLANIQ KDGTYSVIPR SPGGEITPEG LMAVGRIARE FNLYTKITGS
610 620 630 640 650
QRLAMFGAQK DDLPEIWRQL IEAGFETGHA YAKALRMAKT CVGSTWCRYG
660 670 680 690 700
VGDSVGLGVE LENRYKGIRT PHKMKFGVSG CTRECSEAQG KDVGIIATEK
710 720 730 740 750
GWNLYVCGNG GMKPRHADLL AADIDRETLI KYLDRFMMFY IRTADKLTRT
760 770 780 790 800
APWLENLEGG IDYLKAVIID DKLGLNAHLE EEMARLREAV LCEWTETVNT
810 820 830 840
PSAQTRFKHF INSDKRDPNV QMVPEREQHR PATPYERIPV TLVEDNA
Length:847
Mass (Da):93,121
Last modified:November 1, 1995 - v4
Checksum:i5265AD93FD390EB4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti442 – 4421G → A(PubMed:2543955)Curated
Sequence conflicti442 – 4421G → A(PubMed:2200672)Curated
Sequence conflicti835 – 84713YERIP…VEDNA → MNVSQ(PubMed:2543955)CuratedAdd
BLAST
Sequence conflicti835 – 84713YERIP…VEDNA → MNVSQ(PubMed:2200672)CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X14202 Genomic DNA. Translation: CAA32416.1.
U18997 Genomic DNA. Translation: AAA58162.1.
U00096 Genomic DNA. Translation: AAC76390.1.
AP009048 Genomic DNA. Translation: BAE77925.1.
PIRiH65130.
RefSeqiNP_417824.1. NC_000913.3.
YP_492066.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76390; AAC76390; b3365.
BAE77925; BAE77925; BAE77925.
GeneIDi12932093.
947868.
KEGGiecj:Y75_p3810.
eco:b3365.
PATRICi32122164. VBIEscCol129921_3459.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X14202 Genomic DNA. Translation: CAA32416.1 .
U18997 Genomic DNA. Translation: AAA58162.1 .
U00096 Genomic DNA. Translation: AAC76390.1 .
AP009048 Genomic DNA. Translation: BAE77925.1 .
PIRi H65130.
RefSeqi NP_417824.1. NC_000913.3.
YP_492066.1. NC_007779.1.

3D structure databases

ProteinModelPortali P08201.
SMRi P08201. Positions 3-400.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P08201. 1 interaction.
STRINGi 511145.b3365.

Proteomic databases

PaxDbi P08201.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76390 ; AAC76390 ; b3365 .
BAE77925 ; BAE77925 ; BAE77925 .
GeneIDi 12932093.
947868.
KEGGi ecj:Y75_p3810.
eco:b3365.
PATRICi 32122164. VBIEscCol129921_3459.

Organism-specific databases

EchoBASEi EB0647.
EcoGenei EG10653. nirB.

Phylogenomic databases

eggNOGi COG1251.
HOGENOMi HOG000196164.
InParanoidi P08201.
KOi K00362.
OMAi IRSPHKI.
OrthoDBi EOG6G4VT5.
PhylomeDBi P08201.

Enzyme and pathway databases

UniPathwayi UPA00653 .
BioCyci EcoCyc:NIRB-MONOMER.
ECOL316407:JW3328-MONOMER.
MetaCyc:NIRB-MONOMER.

Miscellaneous databases

PROi P08201.

Gene expression databases

Genevestigatori P08201.

Family and domain databases

InterProi 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 ]
Pfami 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 ]
PIRSFi PIRSF037149. NirB. 1 hit.
PRINTSi PR00368. FADPNR.
PR00397. SIROHAEM.
SUPFAMi SSF55124. SSF55124. 1 hit.
TIGRFAMsi TIGR02374. nitri_red_nirB. 1 hit.
PROSITEi PS00365. NIR_SIR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiNIRB_ECOLI
AccessioniPrimary (citable) accession number: P08201
Secondary accession number(s): Q2M731
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: November 1, 1995
Last modified: October 29, 2014
This is version 140 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3