ECOLI:FNR

Species (Taxon ID)	Escherichia coli (strain K12). (83333)
Gene Name(s)	fnr (synonyms: nirR)
Protein Name(s)	Fumarate and nitrate reduction regulatory protein
External Links
UniProt	P0A9E5
EMBL	J01608 U00096 AP009048
PIR	A64883
RefSeq	NP_415850.1 YP_489604.1
ProteinModelPortal	P0A9E5
SMR	P0A9E5
DIP	DIP-9669N
IntAct	P0A9E5
MINT	MINT-1237977
STRING	511145.b1334
PaxDb	P0A9E5
PRIDE	P0A9E5
EnsemblBacteria	AAC74416 BAA14927
GeneID	12932858 945908
KEGG	ecj:Y75_p1311 eco:b1334
PATRIC	32117944
EchoBASE	EB0321
EcoGene	EG10325
eggNOG	COG0664
HOGENOM	HOG000186461
InParanoid	P0A9E5
KO	K01420
OMA	AIRTGFF
OrthoDB	EOG6RVFWF
PhylomeDB	P0A9E5
BioCyc	EcoCyc:PD00197 ECOL316407:JW1328-MONOMER
PRO	PR:P0A9E5
Proteomes	UP000000318 UP000000625
Genevestigator	P0A9E5
GO	GO:0005737 GO:0051539 GO:0003677 GO:0051536 GO:0046872 GO:0003700 GO:0009061 GO:0006355 GO:0071731 GO:0006351
Gene3D	1.10.10.10 2.60.120.10
InterPro	IPR018490 IPR000595 IPR012318 IPR014710 IPR001808 IPR018335 IPR011991
Pfam	PF00027 PF00325
PRINTS	PR00034
SMART	SM00100 SM00419
SUPFAM	SSF51206
PROSITE	PS50042 PS00042 PS51063

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
	0051539		PMID:22029434^[1]						Missing: evidence
	GO:0005737	cytoplasm	PMID:22029434^[1]	ECO:0000314			C	Fig 1: The FNR protein regulates transitions between aerobic and anaerobic growth and also a physiologically relevant sensor of NO	complete CACAO 10728
involved_in	GO:0045893	positive regulation of transcription, DNA-templated	PMID:18227264^[2]	ECO:0005660	quantitative polymerase chain reaction evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0045893	positive regulation of transcription, DNA-templated	PMID:16199562^[3]	ECO:0005660	quantitative polymerase chain reaction evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0045893	positive regulation of transcription, DNA-templated	PMID:9696769^[4]	ECO:0001204	in vitro transcription assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0045893	positive regulation of transcription, DNA-templated	PMID:16199562^[3]	ECO:0001204	in vitro transcription assay evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0032993	protein-DNA complex	PMID:18683632^[5]	ECO:0005667	site-directed mutagenesis phenotypic evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0032993	protein-DNA complex	PMID:9696769^[4]	ECO:0005631	DNAse footprinting evidence used in manual assertion	RefSeq:NC_000913.2	C	Seeded From UniProt	complete
part_of	GO:0032993	protein-DNA complex	PMID:19251855^[6]	ECO:0005631	DNAse footprinting evidence used in manual assertion	RefSeq:NC_000913.2	C	Seeded From UniProt	complete
part_of	GO:0032993	protein-DNA complex	PMID:18227264^[2]	ECO:0005631	DNAse footprinting evidence used in manual assertion	RefSeq:NC_000913.2	C	Seeded From UniProt	complete
part_of	GO:0032993	protein-DNA complex	PMID:16199562^[3]	ECO:0005631	DNAse footprinting evidence used in manual assertion	RefSeq:NC_000913.2	C	Seeded From UniProt	complete
part_of	GO:0032993	protein-DNA complex	PMID:19251855^[6]	ECO:0001807	electrophoretic mobility shift assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0032993	protein-DNA complex	PMID:18683632^[5]	ECO:0001807	electrophoretic mobility shift assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0001216	DNA-binding transcription activator activity	PMID:18683632^[5]	ECO:0005667	site-directed mutagenesis phenotypic evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0001216	DNA-binding transcription activator activity	PMID:9696769^[4]	ECO:0005631	DNAse footprinting evidence used in manual assertion	RefSeq:NC_000913.2	F	Seeded From UniProt	complete
enables	GO:0001216	DNA-binding transcription activator activity	PMID:19251855^[6]	ECO:0005631	DNAse footprinting evidence used in manual assertion	RefSeq:NC_000913.2	F	Seeded From UniProt	complete
enables	GO:0001216	DNA-binding transcription activator activity	PMID:18227264^[2]	ECO:0005631	DNAse footprinting evidence used in manual assertion	RefSeq:NC_000913.2	F	Seeded From UniProt	complete
enables	GO:0001216	DNA-binding transcription activator activity	PMID:16199562^[3]	ECO:0005631	DNAse footprinting evidence used in manual assertion	RefSeq:NC_000913.2	F	Seeded From UniProt	complete
enables	GO:0001216	DNA-binding transcription activator activity	PMID:19251855^[6]	ECO:0001807	electrophoretic mobility shift assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0001216	DNA-binding transcription activator activity	PMID:18683632^[5]	ECO:0001807	electrophoretic mobility shift assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0000976	transcription regulatory region sequence-specific DNA binding	PMID:18683632^[5]	ECO:0005667	site-directed mutagenesis phenotypic evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0000976	transcription regulatory region sequence-specific DNA binding	PMID:9696769^[4]	ECO:0005631	DNAse footprinting evidence used in manual assertion	RefSeq:NC_000913.2	F	Seeded From UniProt	complete
enables	GO:0000976	transcription regulatory region sequence-specific DNA binding	PMID:19251855^[6]	ECO:0005631	DNAse footprinting evidence used in manual assertion	RefSeq:NC_000913.2	F	Seeded From UniProt	complete
enables	GO:0000976	transcription regulatory region sequence-specific DNA binding	PMID:18227264^[2]	ECO:0005631	DNAse footprinting evidence used in manual assertion	RefSeq:NC_000913.2	F	Seeded From UniProt	complete
enables	GO:0000976	transcription regulatory region sequence-specific DNA binding	PMID:16199562^[3]	ECO:0005631	DNAse footprinting evidence used in manual assertion	RefSeq:NC_000913.2	F	Seeded From UniProt	complete
enables	GO:0000976	transcription regulatory region sequence-specific DNA binding	PMID:19251855^[6]	ECO:0001807	electrophoretic mobility shift assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0000976	transcription regulatory region sequence-specific DNA binding	PMID:18683632^[5]	ECO:0001807	electrophoretic mobility shift assay evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:21873635^[7]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10164 EcoGene:EG10325 PANTHER:PTN000705815	C	Seeded From UniProt	complete
enables	GO:0003700	DNA-binding transcription factor activity	PMID:21873635^[7]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10325 PANTHER:PTN000705815 UniProtKB:P22260 UniProtKB:P46148 UniProtKB:P9WMH3	F	Seeded From UniProt	complete
involved_in	GO:0071731	response to nitric oxide	PMID:20714851^[8]	ECO:0000270	expression pattern evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0051539	4 iron, 4 sulfur cluster binding	PMID:9177174^[9]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0051536	iron-sulfur cluster binding	PMID:8576252^[10]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0009061	anaerobic respiration	PMID:12754220^[11]	ECO:0000270	expression pattern evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006355	regulation of transcription, DNA-templated	PMID:12754220^[11]	ECO:0000270	expression pattern evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:18304323^[12]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0003700	DNA-binding transcription factor activity	PMID:9168602^[13]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003677	DNA binding	PMID:9168602^[13]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR012318	F	Seeded From UniProt	complete
enables	GO:0003700	DNA-binding transcription factor activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR018335	F	Seeded From UniProt	complete
involved_in	GO:0006355	regulation of transcription, DNA-templated	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR012318 InterPro:IPR018335	P	Seeded From UniProt	complete
enables	GO:0051536	iron-sulfur cluster binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0411	F	Seeded From UniProt	complete
enables	GO:0051539	4 iron, 4 sulfur cluster binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0004	F	Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0238	F	Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C	Seeded From UniProt	complete
edit table

Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 Vine, CE & Cole, JA (2011) Unresolved sources, sinks, and pathways for the recovery of enteric bacteria from nitrosative stress. FEMS Microbiol. Lett. 325 99-107 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 Partridge, JD et al. (2008) Characterization of the Escherichia coli K-12 ydhYVWXUT operon: regulation by FNR, NarL and NarP. Microbiology (Reading, Engl.) 154 608-18 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 ^3.4 Stewart, V & Bledsoe, PJ (2005) Fnr-, NarP- and NarL-dependent regulation of transcription initiation from the Haemophilus influenzae Rd napF (periplasmic nitrate reductase) promoter in Escherichia coli K-12. J. Bacteriol. 187 6928-35 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 ^4.3 Darwin, AJ et al. (1998) Fnr, NarP, and NarL regulation of Escherichia coli K-12 napF (periplasmic nitrate reductase) operon transcription in vitro. J. Bacteriol. 180 4192-8 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 ^5.3 ^5.4 ^5.5 Roca, I et al. (2008) Fumarate and nitrate reduction (FNR) dependent activation of the Escherichia coli anaerobic ribonucleotide reductase nrdDG promoter. Int. Microbiol. 11 49-56 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 ^6.3 ^6.4 ^6.5 Xu, M et al. (2009) Activation and repression at the Escherichia coli ynfEFGHI operon promoter. J. Bacteriol. 191 3172-6 PubMed GONUTS page
↑ ^7.0 ^7.1 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Vasilieva, SV et al. () Fnr[4Fe-4S](2+) protein regulates the aidB gene expression in Escherichia coli cultured under anaerobic conditions. Dokl. Biochem. Biophys. 433 179-82 PubMed GONUTS page
↑ Khoroshilova, N et al. (1997) Iron-sulfur cluster disassembly in the FNR protein of Escherichia coli by O2: [4Fe-4S] to [2Fe-2S] conversion with loss of biological activity. Proc. Natl. Acad. Sci. U.S.A. 94 6087-92 PubMed GONUTS page
↑ Lazazzera, BA et al. (1996) DNA binding and dimerization of the Fe-S-containing FNR protein from Escherichia coli are regulated by oxygen. J. Biol. Chem. 271 2762-8 PubMed GONUTS page
↑ ^11.0 ^11.1 Salmon, K et al. (2003) Global gene expression profiling in Escherichia coli K12. The effects of oxygen availability and FNR. J. Biol. Chem. 278 29837-55 PubMed GONUTS page
↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
↑ ^13.0 ^13.1 Meng, W et al. (1997) FNR-dependent repression of ndh gene expression requires two upstream FNR-binding sites. Microbiology (Reading, Engl.) 143 ( Pt 5) 1521-32 PubMed GONUTS page

[PMID:22029434-1] 1.0 ^1.1 Vine, CE & Cole, JA (2011) Unresolved sources, sinks, and pathways for the recovery of enteric bacteria from nitrosative stress. FEMS Microbiol. Lett. 325 99-107 PubMed GONUTS page

[PMID:18227264-2] 2.0 ^2.1 ^2.2 ^2.3 Partridge, JD et al. (2008) Characterization of the Escherichia coli K-12 ydhYVWXUT operon: regulation by FNR, NarL and NarP. Microbiology (Reading, Engl.) 154 608-18 PubMed GONUTS page

[PMID:16199562-3] 3.0 ^3.1 ^3.2 ^3.3 ^3.4 Stewart, V & Bledsoe, PJ (2005) Fnr-, NarP- and NarL-dependent regulation of transcription initiation from the Haemophilus influenzae Rd napF (periplasmic nitrate reductase) promoter in Escherichia coli K-12. J. Bacteriol. 187 6928-35 PubMed GONUTS page

[PMID:9696769-4] 4.0 ^4.1 ^4.2 ^4.3 Darwin, AJ et al. (1998) Fnr, NarP, and NarL regulation of Escherichia coli K-12 napF (periplasmic nitrate reductase) operon transcription in vitro. J. Bacteriol. 180 4192-8 PubMed GONUTS page

[PMID:18683632-5] 5.0 ^5.1 ^5.2 ^5.3 ^5.4 ^5.5 Roca, I et al. (2008) Fumarate and nitrate reduction (FNR) dependent activation of the Escherichia coli anaerobic ribonucleotide reductase nrdDG promoter. Int. Microbiol. 11 49-56 PubMed GONUTS page

[PMID:19251855-6] 6.0 ^6.1 ^6.2 ^6.3 ^6.4 ^6.5 Xu, M et al. (2009) Activation and repression at the Escherichia coli ynfEFGHI operon promoter. J. Bacteriol. 191 3172-6 PubMed GONUTS page

[PMID:21873635-7] 7.0 ^7.1 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:20714851-8] Vasilieva, SV et al. () Fnr[4Fe-4S](2+) protein regulates the aidB gene expression in Escherichia coli cultured under anaerobic conditions. Dokl. Biochem. Biophys. 433 179-82 PubMed GONUTS page

[PMID:9177174-9] Khoroshilova, N et al. (1997) Iron-sulfur cluster disassembly in the FNR protein of Escherichia coli by O2: [4Fe-4S] to [2Fe-2S] conversion with loss of biological activity. Proc. Natl. Acad. Sci. U.S.A. 94 6087-92 PubMed GONUTS page

[PMID:8576252-10] Lazazzera, BA et al. (1996) DNA binding and dimerization of the Fe-S-containing FNR protein from Escherichia coli are regulated by oxygen. J. Biol. Chem. 271 2762-8 PubMed GONUTS page

[PMID:12754220-11] 11.0 ^11.1 Salmon, K et al. (2003) Global gene expression profiling in Escherichia coli K12. The effects of oxygen availability and FNR. J. Biol. Chem. 278 29837-55 PubMed GONUTS page

[PMID:18304323-12] Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page

[PMID:9168602-13] 13.0 ^13.1 Meng, W et al. (1997) FNR-dependent repression of ndh gene expression requires two upstream FNR-binding sites. Microbiology (Reading, Engl.) 143 ( Pt 5) 1521-32 PubMed GONUTS page

[1]

[2]

[3]

[4]

[5]

[6]

[7]

[8]

[9]

[10]

[11]

[12]

[13]

ECOLI:FNR

Contents

Annotations

Notes

References

4

a

b

c

d

e

g

i

m

p

r

t

Navigation menu

Personal tools

Namespaces

Variants

Views

More

Search

Navigation

Cacao

Links

Tools