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ECOLI:NARI

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) narI (synonyms: chlI)
Protein Name(s) Respiratory nitrate reductase 1 gamma chain

Cytochrome B-NR Nitrate reductase A subunit gamma Quinol-nitrate oxidoreductase subunit gamma

External Links
UniProt P11350
EMBL M20147
U00096
AP009048
PIR C27737
RefSeq NP_415745.1
YP_489497.1
PDB 1Q16
1SIW
1Y4Z
1Y5I
1Y5L
1Y5N
3EGW
3IR5
3IR6
3IR7
PDBsum 1Q16
1SIW
1Y4Z
1Y5I
1Y5L
1Y5N
3EGW
3IR5
3IR6
3IR7
ProteinModelPortal P11350
SMR P11350
DIP DIP-10313N
IntAct P11350
MINT MINT-1262739
STRING 511145.b1227
TCDB 5.A.3.1.1
EnsemblBacteria AAC74311
BAA36097
GeneID 12933239
945808
KEGG ecj:Y75_p1202
eco:b1227
PATRIC 32117714
EchoBASE EB0634
EcoGene EG10640
eggNOG COG2181
HOGENOM HOG000237376
InParanoid P11350
KO K00374
OMA MVSGGFF
OrthoDB EOG6K13W6
PhylomeDB P11350
BioCyc EcoCyc:NARI-MONOMER
ECOL316407:JW1218-MONOMER
MetaCyc:NARI-MONOMER
EvolutionaryTrace P11350
PRO PR:P11350
Proteomes UP000000318
UP000000625
Genevestigator P11350
GO GO:0016021
GO:0031224
GO:0009325
GO:0005886
GO:0046872
GO:0008940
GO:0009061
GO:0017004
GO:0042128
InterPro IPR023234
IPR003816
Pfam PF02665
SUPFAM SSF103501
TIGRFAMs TIGR00351

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0009325

nitrate reductase complex

PMID:3053688[1]

ECO:0000314

C

Figure 4. Column 2 (0 min); Column 3 (2min) Column 4 (10min). As length of purification process increases, expression decreases - less expression in each consecutive column after column 2. Evidence that narJ is lost during lengthy purification process.

complete
CACAO 2300

part_of

GO:0009325

nitrate reductase complex

PMID:3053688[1]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0020037

heme binding

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10640
PANTHER:PTN002023632

F

Seeded From UniProt

complete

involved_in

GO:0019645

anaerobic electron transport chain

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10644
PANTHER:PTN002023632

P

Seeded From UniProt

complete

enables

GO:0009055

electron transfer activity

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10640
PANTHER:PTN002023632

F

Seeded From UniProt

complete

enables

GO:0008940

nitrate reductase activity

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10640
EcoGene:EG10644
PANTHER:PTN002023632

F

Seeded From UniProt

complete

part_of

GO:0044799

NarGHI complex

PMID:4151408[3]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0044799

NarGHI complex

PMID:12910261[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0020037

heme binding

PMID:9325288[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0020037

heme binding

PMID:12910261[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0020037

heme binding

PMID:10504245[6]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0009061

anaerobic respiration

PMID:2832376[7]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0009055

electron transfer activity

PMID:12910261[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0009055

electron transfer activity

PMID:10504245[6]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008940

nitrate reductase activity

PMID:7047497[8]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008940

nitrate reductase activity

PMID:4151408[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0005887

integral component of plasma membrane

PMID:12910261[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005887

integral component of plasma membrane

PMID:7746153[9]

ECO:0000255

match to sequence model evidence used in manual assertion

C

Seeded From UniProt

Missing: with/from

part_of

GO:0005886

plasma membrane

PMID:17309111[10]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

PMID:15919996[11]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0008940

nitrate reductase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003816

F

Seeded From UniProt

complete

part_of

GO:0009325

nitrate reductase complex

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003816

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:IPR003816

P

Seeded From UniProt

complete

part_of

GO:0016021

integral component of membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0812

C

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

GO_REF:0000037
GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0997
UniProtKB-KW:KW-1003
UniProtKB-SubCell:SL-0037

C

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:0016020

membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0472

C

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

involved_in

GO:0042128

nitrate assimilation

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0534

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

edit table

Notes

References

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

  1. ↑ 1.0 1.1 Sodergren, EJ et al. (1988) Roles of the narJ and narI gene products in the expression of nitrate reductase in Escherichia coli. J. Biol. Chem. 263 16156-62 PubMed GONUTS page
  2. ↑ 2.0 2.1 2.2 2.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  3. ↑ 3.0 3.1 Forget, P (1974) The bacterial nitrate reductases. Solubilization, purification and properties of the enzyme A of Escherichia coli K 12. Eur. J. Biochem. 42 325-32 PubMed GONUTS page
  4. ↑ 4.0 4.1 4.2 4.3 Bertero, MG et al. (2003) Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A. Nat. Struct. Biol. 10 681-7 PubMed GONUTS page
  5. ↑ Magalon, A et al. (1997) Heme axial ligation by the highly conserved His residues in helix II of cytochrome b (NarI) of Escherichia coli nitrate reductase A. J. Biol. Chem. 272 25652-8 PubMed GONUTS page
  6. ↑ 6.0 6.1 Rothery, RA et al. (1999) The hemes of Escherichia coli nitrate reductase A (NarGHI): potentiometric effects of inhibitor binding to narI. Biochemistry 38 12747-57 PubMed GONUTS page
  7. ↑ Sodergren, EJ & DeMoss, JA (1988) narI region of the Escherichia coli nitrate reductase (nar) operon contains two genes. J. Bacteriol. 170 1721-9 PubMed GONUTS page
  8. ↑ Stewart, V & MacGregor, CH (1982) Nitrate reductase in Escherichia coli K-12: involvement of chlC, chlE, and chlG loci. J. Bacteriol. 151 788-99 PubMed GONUTS page
  9. ↑ Berks, BC et al. (1995) Sequence analysis of subunits of the membrane-bound nitrate reductase from a denitrifying bacterium: the integral membrane subunit provides a prototype for the dihaem electron-carrying arm of a redox loop. Mol. Microbiol. 15 319-31 PubMed GONUTS page
  10. ↑ Zhang, N et al. (2007) Comparison of SDS- and methanol-assisted protein solubilization and digestion methods for Escherichia coli membrane proteome analysis by 2-D LC-MS/MS. Proteomics 7 484-93 PubMed GONUTS page
  11. ↑ Daley, DO et al. (2005) Global topology analysis of the Escherichia coli inner membrane proteome. Science 308 1321-3 PubMed GONUTS page
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