Reviewed, UniProtKB/Swiss-Prot P08201 (NIRB_ECOLI)

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) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	847 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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
Gene Ontology (GO)
Biological process	nitrate assimilation Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW FAD binding Inferred from electronic annotation. Source: InterPro NADP or NADPH binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro nitrite reductase [NAD(P)H] activity Inferred from electronic annotation. Source: EC
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	36	FAD Potential
	Nucleotide binding	193 – 225	33	NAD or NADP Potential
Sites
	Metal binding	641	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	647	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	681	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	685	1	Iron (siroheme axial ligand) By similarity
	Metal binding	685	1	Iron-sulfur (4Fe-4S) By similarity
Experimental info
	Sequence conflict	442	1	G → A Ref.1
	Sequence conflict	442	1	G → A Ref.2
	Sequence conflict	835 – 847	13	YERIP…VEDNA → MNVSQ Ref.1
	Sequence conflict	835 – 847	13	YERIP…VEDNA → MNVSQ Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P08201-1 [UniParc]. Last modified November 1, 1995. Version 4. Checksum: 5265AD93FD390EB4	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

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: 2543955] [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: 2200672] [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: 9278503] [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: 16738553] [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: 2445993] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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	AP_004424.1. NP_417824.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	947868.
GenomeReviews	Gene locus JW3328 in contig AP009048_GR. Gene locus b3365 in contig U00096_GR.
KEGG	ecj:JW3328. eco:b3365.
Organism-specific databases
EchoBASE	EB0647.
EcoGene	EG10653. nirB.
CMR	Search...
Phylogenomic databases
HOGENOM	P08201.
OMA	P08201. NIQRNGT.
Enzyme and pathway databases
BioCyc	EcoCyc:NIRB-MON. MetaCyc:NIRB-MON.
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. IPR001327. Pyr_OxRdtase_NAD_bd. [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.
ProDom	PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain]
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:	June 16, 2009
This is version 90 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)