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ECOLI:NAPA

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) napA (synonyms: yojC, yojD, yojE)
Protein Name(s) Periplasmic nitrate reductase
External Links
UniProt P33937
EMBL U00008
U00096
AP009048
PIR D64990
RefSeq NP_416710.1
YP_490444.1
PDB 2NYA
2PQ4
PDBsum 2NYA
2PQ4
ProteinModelPortal P33937
SMR P33937
DIP DIP-10304N
IntAct P33937
MINT MINT-1243254
STRING 511145.b2206
PaxDb P33937
PRIDE P33937
EnsemblBacteria AAC75266
BAA15989
GeneID 12933227
947093
KEGG ecj:Y75_p2167
eco:b2206
PATRIC 32119771
EchoBASE EB1994
EcoGene EG12067
eggNOG COG0243
HOGENOM HOG000031441
InParanoid P33937
KO K02567
OMA REYTPKM
OrthoDB EOG6CVV7G
PhylomeDB P33937
BioCyc EcoCyc:NAPA-MONOMER
ECOL316407:JW2194-MONOMER
MetaCyc:NAPA-MONOMER
EvolutionaryTrace P33937
PRO PR:P33937
Proteomes UP000000318
UP000000625
Genevestigator P33937
GO GO:0030288
GO:0042597
GO:0051539
GO:0009055
GO:0005506
GO:0030151
GO:0008940
GO:0016651
GO:0009061
GO:0045333
GO:0006777
GO:0042128
HAMAP MF_01630
InterPro IPR009010
IPR006657
IPR006656
IPR006963
IPR027467
IPR010051
IPR006311
IPR019546
Pfam PF04879
PF00384
PF01568
SMART SM00926
SUPFAM SSF50692
TIGRFAMs TIGR01706
TIGR01409
PROSITE PS51669
PS00551
PS51318

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0030288

outer membrane-bounded periplasmic space

PMID:10234835[1]

ECO:0000314

C

Figure 1. Periplasmic proteins separated and stained for nitrate reductase activity. Banding seen is due to the reduction of nitrite formed as the product of NapA activity by periplasmic nitrite reductase [20].

complete
CACAO 2458

GO:0008940

nitrate reductase activity

PMID:10234835[1]

ECO:0000314

F

Nap activity was detected, but associated with a band of decreased electrophoretic mobility which lacks c-type cytochrome, implying that NapA is active with the artificial electron donor, methyl viologen, in the absence of NapB (Fig. 1, track 2).

complete
CACAO 2467

part_of

GO:0030288

outer membrane-bounded periplasmic space

PMID:10234835[1]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0008940

nitrate reductase activity

PMID:10234835[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0051539

4 iron, 4 sulfur cluster binding

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10285
EcoGene:EG12067
EcoGene:EG12087
PANTHER:PTN000177493

F

Seeded From UniProt

complete

enables

GO:0030151

molybdenum ion binding

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG12067
PANTHER:PTN000177407

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:EG12067
PANTHER:PTN000177407

F

Seeded From UniProt

complete

involved_in

GO:0009061

anaerobic respiration

PMID:11844760[3]

ECO:0000316

genetic interaction evidence used in manual assertion

EcoliWiki:narG

P

Seeded From UniProt

complete

enables

GO:0008940

nitrate reductase activity

PMID:11844760[3]

ECO:0000316

genetic interaction evidence used in manual assertion

EcoliWiki:narG

F

Seeded From UniProt

complete

enables

GO:0051539

4 iron, 4 sulfur cluster binding

PMID:17130127[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0042597

periplasmic space

PMID:8830238[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0030288

outer membrane-bounded periplasmic space

PMID:24140104[6]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0030288

outer membrane-bounded periplasmic space

PMID:10234835[1]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0030151

molybdenum ion binding

PMID:17130127[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008940

nitrate reductase activity

PMID:8830238[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0022900

electron transport chain

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0009055

P

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:IPR010051

F

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR006656
InterPro:IPR006657
InterPro:IPR006963

F

Seeded From UniProt

complete

enables

GO:0030151

molybdenum ion binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR010051

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:IPR010051

C

Seeded From UniProt

complete

enables

GO:0043546

molybdopterin cofactor binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR006657

F

Seeded From UniProt

complete

enables

GO:0051539

4 iron, 4 sulfur cluster binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR027467

F

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:IPR006656
InterPro:IPR006657
InterPro:IPR006963
InterPro:IPR010051

P

Seeded From UniProt

complete

enables

GO:0050140

nitrate reductase (cytochrome) activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:1.9.6.1

F

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:UR000080092

F

Seeded From UniProt

complete

involved_in

GO:0042128

nitrate assimilation

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000080092

P

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:UR000080092

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:UR000080092

P

Seeded From UniProt

complete

enables

GO:0008940

nitrate reductase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000080092

F

Seeded From UniProt

complete

involved_in

GO:0006777

Mo-molybdopterin cofactor biosynthetic process

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000080092

P

Seeded From UniProt

complete

enables

GO:0009055

electron transfer activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000080092

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:0055114

oxidation-reduction process

GO_REF:0000037
GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

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

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

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: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

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: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

Notes

References

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

  1. 1.0 1.1 1.2 1.3 1.4 Thomas, G et al. (1999) The periplasmic nitrate reductase from Escherichia coli: a heterodimeric molybdoprotein with a double-arginine signal sequence and an unusual leader peptide cleavage site. FEMS Microbiol. Lett. 174 167-71 PubMed GONUTS page
  2. 2.0 2.1 2.2 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 Stewart, V et al. (2002) Periplasmic nitrate reductase (NapABC enzyme) supports anaerobic respiration by Escherichia coli K-12. J. Bacteriol. 184 1314-23 PubMed GONUTS page
  4. 4.0 4.1 Jepson, BJ et al. (2007) Spectropotentiometric and structural analysis of the periplasmic nitrate reductase from Escherichia coli. J. Biol. Chem. 282 6425-37 PubMed GONUTS page
  5. 5.0 5.1 Grove, J et al. (1996) Escherichia coli K-12 genes essential for the synthesis of c-type cytochromes and a third nitrate reductase located in the periplasm. Mol. Microbiol. 19 467-81 PubMed GONUTS page
  6. Han, MJ et al. (2014) Comparison of the large-scale periplasmic proteomes of the Escherichia coli K-12 and B strains. J. Biosci. Bioeng. 117 437-42 PubMed GONUTS page