[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=K12; DOI=10.1093/nar/17.10.3865; PubMed=2543955 [NCBI, ExPASy, EBI, Israel, Japan] Bell A.I., Gaston K.L., Cole J.A., Busby S.J.W.; "Cloning of binding sequences for the Escherichia coli transcription activators, FNR and CRP: location of bases involved in discrimination between FNR and CRP."; Nucleic Acids Res. 17:3865-3874(1989).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=K12; PubMed=2200672 [NCBI, ExPASy, EBI, Israel, Japan] Peakman T., Crouzet J., Mayaux J.F., Busby S.J.W., Mohan S., Harborne N., Wootton J., Nicolson R., Cole J.A.; "Nucleotide sequence, organisation and structural analysis of the products of genes in the nirB-cysG region of the Escherichia coli K-12 chromosome."; Eur. J. Biochem. 191:315-323(1990).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "The complete genome sequence of Escherichia coli K-12."; Science 277:1453-1474(1997).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."; Mol. Syst. Biol. 2:E1-E5(2006).
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21. DOI=10.1016/0022-2836(87)90404-9; PubMed=2445993 [NCBI, ExPASy, EBI, Israel, Japan] Jayaraman P.S., Peakman T.C., Busby S.J.W., Quincey R.V., Cole J.A.; "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."; J. Mol. Biol. 196:781-788(1987).

Comments

CATALYTIC ACTIVITY: Ammonium hydroxide + 3 NAD(P)⁺ + H₂O = nitrite + 3 NAD(P)H.
COFACTOR: Binds 1 siroheme per subunit.
COFACTOR: Binds 1 4Fe-4S cluster per subunit.
COFACTOR: FAD.
PATHWAY: Nitrogen metabolism; nitrate reduction (assimilation).
SUBUNIT: Homodimer which associates with nirD.
SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X14202; CAA32416.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U18997; AAA58162.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC76390.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE77925.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

H65130; H65130.

RefSeq

AP_004424.1; -.
NP_417824.1; -.

3D structure databases

ModBase

P08201.

Enzyme and pathway databases

BioCyc

EcoCyc:NIRB-MON; -.
MetaCyc:NIRB-MON; -.

Organism-specific databases

EchoBASE

EB0647; -.

EcoGene

EG10653; nirB.

Ontologies

GO:0051539;	Molecular function: 4 iron, 4 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050660;	Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0020037;	Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0050661;	Molecular function: NADP binding (inferred from electronic annotation from InterPro).
GO:0008942;	Molecular function: nitrite reductase [NAD(P)H] activity (inferred from electronic annotation from InterPro).
GO:0042128;	Biological process: nitrate assimilation (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR007419; BFD_Fer2_bd.
IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR006066; Nir_Si_BS.
IPR006067; Nir_Sir_4Fe4S.
IPR005117; NiRdtase/SiRdtase_haem-b_fer.
IPR012744; Nitri_red_NirB.
IPR017121; Nitrite_Rdtase_lsu.
IPR001100; Pyr_nuc-diS_OxRdtase.
IPR001327; Pyr_OxRdtase_NAD_bd.
Graphical view of domain structure.

Pfam

PF04324; Fer2_BFD; 1.
PF01077; NIR_SIR; 1.
PF03460; NIR_SIR_ferr; 1.
PF00070; Pyr_redox; 1.
PF07992; Pyr_redox_2; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF037149; NirB; 1.

PRINTS

PR00368; FADPNR.
PR00411; PNDRDTASEI.
PR00397; SIROHAEM.

ProDom

PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR02374; nitri_red_nirB; 1.

PROSITE

PS00365; NIR_SIR; 1.

Genome annotation databases

GeneID

947868; -.

GenomeReviews

AP009048_GR; JW3328.
U00096_GR; b3365.

KEGG

ecj:JW3328; -.
eco:b3365; -.

Phylogenomic databases

HOGENOM

P08201; -.

Genome annotation databases

CMR

P08201; b3365.

Other

ProtoNet

P08201.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

4Fe-4S; Complete proteome; FAD; Flavoprotein; Heme; Iron; Iron-sulfur; Metal-binding; NADP; Nitrate assimilation; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 847`	`847`	`Nitrite reductase [NAD(P)H] large subunit.`	`PRO_0000199962`
`NP_BIND`	`44 79`	`36`	`FAD (Potential).`
`NP_BIND`	`193 225`	`33`	`NAD or NADP (Potential).`
`METAL`	`641 641`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`647 647`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`681 681`		`Iron-sulfur (4Fe-4S) (By similarity).`
`METAL`	`685 685`		`Iron (siroheme axial ligand) (By similarity).`
`METAL`	`685 685`		`Iron-sulfur (4Fe-4S) (By similarity).`
`CONFLICT`	`442 442`		`G -> A (in Ref. 1 and 2).`
`CONFLICT`	`835 847`		`YERIPVTLVEDNA -> MNVSQ (in Ref. 1 and 2).`

Sequence information

Length: 847 AA [This is the length of the unprocessed precursor]

Molecular weight: 93121 Da [This is the MW of the unprocessed precursor]

CRC64: 5265AD93FD390EB4 [This is a checksum on the sequence]

        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

P08201 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools