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ECOLI:NRFA

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) nrfA
Protein Name(s) Cytochrome c-552

Ammonia-forming cytochrome c nitrite reductase Cytochrome c nitrite reductase

External Links
UniProt P0ABK9
EMBL X72298
U00006
U00096
AP009048
PIR S39590
RefSeq NP_418494.1
YP_492213.1
PDB 1GU6
2RDZ
2RF7
3L1T
3TOR
PDBsum 1GU6
2RDZ
2RF7
3L1T
3TOR
ProteinModelPortal P0ABK9
SMR P0ABK9
DIP DIP-36021N
IntAct P0ABK9
STRING 511145.b4070
PaxDb P0ABK9
PRIDE P0ABK9
EnsemblBacteria AAC77040
BAE78072
GeneID 12930411
948571
KEGG ecj:Y75_p3957
eco:b4070
PATRIC 32123689
EchoBASE EB1729
EcoGene EG11781
eggNOG COG3303
HOGENOM HOG000278511
InParanoid P0ABK9
KO K03385
OMA CHEKGKS
OrthoDB EOG6K3ZWZ
PhylomeDB P0ABK9
BioCyc EcoCyc:CYTOCHROMEC552-MONOMER
ECOL316407:JW4031-MONOMER
MetaCyc:CYTOCHROMEC552-MONOMER
UniPathway UPA00653
EvolutionaryTrace P0ABK9
PRO PR:P0ABK9
Proteomes UP000000318
UP000000625
Genevestigator P0ABK9
GO GO:0030288
GO:0005509
GO:0020037
GO:0005506
GO:0042279
GO:0019645
GO:0042128
Gene3D 1.10.710.10
HAMAP MF_01182
InterPro IPR023155
IPR003321
IPR017570
IPR011031
Pfam PF02335
PIRSF PIRSF000243
TIGRFAMs TIGR03152
PROSITE PS51008

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0016966

nitric oxide reductase activity

PMID:18245085[1]

ECO:0000314

F

Protein film voltammetry (PFV) was used to analyze the catalytic activity of the E. coli nrfA gene in reducing NO. Figure 3 shows data for NO reduction for varying concentration of NO by nfrA. Table 1 compares nrfA activity between NO and other substrates.

complete
CACAO 9553

GO:0003028

regulation of systemic arterial blood pressure by aortic body chemoreceptor signaling

PMID:18375814[2]

ECO:0000314

P

Figure 1&2: activity assays and measurements of NO consumption showing that the increased nitrite reductase activity correlates with an elevated capacity for NO reduction by intact cells.

complete
CACAO 10735

enables

GO:0016966

nitric oxide reductase activity

PMID:18245085[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0042279

nitrite reductase (cytochrome, ammonia-forming) activity

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11781
PANTHER:PTN000771929

F

Seeded From UniProt

complete

part_of

GO:0030288

outer membrane-bounded periplasmic space

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11781
PANTHER:PTN000771929

C

Seeded From UniProt

complete

enables

GO:0020037

heme binding

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11781
PANTHER:PTN000771929

F

Seeded From UniProt

complete

involved_in

GO:0019645

anaerobic electron transport chain

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11781
PANTHER:PTN000771929

P

Seeded From UniProt

complete

enables

GO:0042279

nitrite reductase (cytochrome, ammonia-forming) activity

PMID:5338848[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0042279

nitrite reductase (cytochrome, ammonia-forming) activity

PMID:3002798[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0030288

outer membrane-bounded periplasmic space

PMID:5338848[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0020037

heme binding

PMID:9593308[6]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0019645

anaerobic electron transport chain

PMID:8057835[7]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0005509

calcium ion binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR017570

F

Seeded From UniProt

complete

involved_in

GO:0006807

nitrogen compound metabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003321
InterPro:IPR017570

P

Seeded From UniProt

complete

enables

GO:0020037

heme binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR017570

F

Seeded From UniProt

complete

enables

GO:0042279

nitrite reductase (cytochrome, ammonia-forming) activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003321
InterPro:IPR017570

F

Seeded From UniProt

complete

part_of

GO:0042597

periplasmic space

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003321
InterPro:IPR017570

C

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003321
InterPro:IPR017570

P

Seeded From UniProt

complete

enables

GO:0042279

nitrite reductase (cytochrome, ammonia-forming) activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:1.7.2.2

F

Seeded From UniProt

complete

involved_in

GO:0006807

nitrogen compound metabolic process

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000100881

P

Seeded From UniProt

complete

enables

GO:0005506

iron ion binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000100881

F

Seeded From UniProt

complete

part_of

GO:0042597

periplasmic space

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000100881

C

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000100881

P

Seeded From UniProt

complete

enables

GO:0042279

nitrite reductase (cytochrome, ammonia-forming) activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000100881

F

Seeded From UniProt

complete

enables

GO:0005509

calcium ion binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000100881

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

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000037
GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560
UniProtKB-KW:KW-0249

P

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

F

Seeded From UniProt

complete

part_of

GO:0042597

periplasmic space

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0574
UniProtKB-SubCell:SL-0200

C

Seeded From UniProt

complete

involved_in

GO:0042128

nitrate assimilation

GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniPathway:UPA00653

P

Seeded From UniProt

complete

edit table

Notes

References

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

  1. ↑ 1.0 1.1 van Wonderen, JH et al. (2008) The nitric oxide reductase activity of cytochrome c nitrite reductase from Escherichia coli. J. Biol. Chem. 283 9587-94 PubMed GONUTS page
  2. ↑ Mills, PC et al. (2008) A combination of cytochrome c nitrite reductase (NrfA) and flavorubredoxin (NorV) protects Salmonella enterica serovar Typhimurium against killing by NO in anoxic environments. Microbiology (Reading, Engl.) 154 1218-28 PubMed GONUTS page
  3. ↑ 3.0 3.1 3.2 3.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  4. ↑ 4.0 4.1 Fujita, T (1966) Studies on soluble cytochromes in Enterobacteriaceae. I. Detection, purification, and properties of cytochrome c-552 in anaerobically grown cells. J. Biochem. 60 204-15 PubMed GONUTS page
  5. ↑ Kajie, S & Anraku, Y (1986) Purification of a hexaheme cytochrome c552 from Escherichia coli K 12 and its properties as a nitrite reductase. Eur. J. Biochem. 154 457-63 PubMed GONUTS page
  6. ↑ Eaves, DJ et al. (1998) Involvement of products of the nrfEFG genes in the covalent attachment of haem c to a novel cysteine-lysine motif in the cytochrome c552 nitrite reductase from Escherichia coli. Mol. Microbiol. 28 205-16 PubMed GONUTS page
  7. ↑ Hussain, H et al. (1994) A seven-gene operon essential for formate-dependent nitrite reduction to ammonia by enteric bacteria. Mol. Microbiol. 12 153-63 PubMed GONUTS page
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