Nitrate reductase molybdenum cofactor assembly chaperone NarJ (P0AF26)

Identification
Name:Nitrate reductase molybdenum cofactor assembly chaperone NarJ
Synonyms:
  • Redox enzyme maturation protein NarJ
Gene Name:narJ
Enzyme Class:Not Available
Biological Properties
General Function:Involved in unfolded protein binding
Specific Function:Chaperone required for proper molybdenum cofactor insertion and final assembly of the membrane-bound respiratory nitrate reductase 1. Required for the insertion of the molybdenum into the apo-NarG subunit, maybe by keeping NarG in an appropriate competent-open conformation for the molybdenum cofactor insertion to occur. NarJ maintains the apoNarGH complex in a soluble state. Upon insertion of the molybdenum cofactor, NarJ seems to dissociate from the activated soluble NarGH complex, before its association with the NarI subunit on the membrane
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Acceptor+1.0Thumb+1.0Acceptor ↔ 1.0Thumb+1.0Reduced acceptor+1.0Reduced acceptor
1.0Nitrite + 1.0Acceptor + 1.0Water + 1.0Acceptor ↔ 1.0Nitrate + 1.0Reduced acceptor + 1.0Reduced acceptor
ReactionCard
2.0Ferricytochrome c+1.0Thumb+1.0Thumb ↔ 1.0Thumb+2.0Ferrocytochrome c+2.0Thumb
2.0Ferricytochrome c + 1.0Nitrite + 1.0Water ↔ 1.0Nitrate + 2.0Ferrocytochrome c + 2.0Hydrogen ion
ReactionCard
SMPDB Reactions:
1.0Nitrate+1.0cytochrome c nitrite reductase+1.0Thumb ↔ 1.0Nitrite+1.0cytochrome c nitrite reductase+1.0Thumb+1.0Thumb
1.0Nitrate + 1.0cytochrome c nitrite reductase + 1.0Nitrate ↔ 1.0Nitrite + 1.0cytochrome c nitrite reductase + 1.0Water + 1.0Nitrite
ReactionCard
1.0Thumb+2.0Thumb+2.0Electron → 1.0Thumb+1.0Thumb
1.0Selenate + 2.0Hydrogen ion + 2.0Electron → 1.0Selenite + 1.0Water
ReactionCard
1.0Thumb+2.0Thumb+1.0a menaquinol → 1.0Thumb+1.0Thumb+1.0a menaquinone
1.0Nitrate + 2.0Hydrogen ion + 1.0a menaquinol → 1.0Nitrite + 1.0Water + 1.0a menaquinone
ReactionCard
Complex Reactions:
2.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+2.0Thumb
2.0Hydrogen ion + 1.0Nitrate + 1.0Ubiquinol-8 → 1.0Water + 1.0Nitrite + 1.0Ubiquinone-8 + 2.0Hydrogen ion
ReactionCard
2.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Menaquinone 8+1.0Thumb+2.0Thumb
2.0Hydrogen ion + 1.0Menaquinol 8 + 1.0Nitrate → 1.0Water + 1.0Menaquinone 8 + 1.0Nitrite + 2.0Hydrogen ion
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB21652Ferricytochrome cMetaboCard
ECMDB23135Ferrocytochrome cMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB21245Menaquinol 8MetaboCard
ECMDB02878NitrateMetaboCard
ECMDB02786NitriteMetaboCard
ECMDB23788SelenateMetaboCard
ECMDB21355SeleniteMetaboCard
ECMDB01060Ubiquinol-8MetaboCard
ECMDB21296Ubiquinone-8MetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
binding
protein binding
unfolded protein binding
Process
cellular component assembly
cellular component organization
cellular component organization or biogenesis
cellular protein complex assembly
chaperone-mediated protein complex assembly
macromolecular complex assembly
protein complex assembly
Gene Properties
Blattner:b1226
Gene OrientationClockwise
Centisome Percentage:27.68
Left Sequence End1284362
Right Sequence End1285072
Gene Sequence:
>711 bp
ATGGTGAAAAAAGCGATAGTGACAGCGATGGCTGTAATCAGCCTCTTTACTCTGATGGGA
TGTAATAATCGGGCCGAAGTCGATACGCTTTCTCCGGCGCAGGCTGCCGAACTGAAACCG
ATGCCGCAAAGTTGGCGCGGCGTGCTGCCGTGTGCCGATTGCGAAGGAATCGAAACCTCT
CTGTTCCTCGAAAAAGACGGAACATGGGTGATGAATGAGCGTTATCTCGGTGCTCGTGAA
GAACCTTCCTCCTTCGCTTCCTACGGTACATGGGCGCGAACCGCTGACAAGCTGGTATTA
ACCGACAGCAAAGGTGAAAAGTCATATTATCGGGCGAAAGGCGATGCGCTGGAGATGCTC
GATCGTGAAGGCAATCCGATTGAATCGCAGTTCAACTATACGCTGGAAGCGGCACAATCC
AGTTTACCTATGACGCCGATGACCCTGCGGGGCATGTATTTTTATATGGCTGATGCGGCG
ACCTTCACTGATTGCGCGACCGGAAAACGTTTCATGGTAGCGAATAACGCAGAGCTGGAG
CGTAGCTACCTGGCTGCGCGCGGTCACAGTGAAAAACCGGTGTTACTGTCAGTAGAAGGT
CACTTTACGCTTGAGGGTAATCCGGATACCGGTGCGCCGACTAAAGTATTGGCACCCGAT
ACGGCAGGGAAATTTTACCCCAACCAGGATTGCAGTAGTTTGGGGCAGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:236
Protein Molecular Weight:26449
Protein Theoretical pI:5
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Nitrate reductase molybdenum cofactor assembly chaperone NarJ
MIELVIVSRLLEYPDAALWQHQQEMFEAIAASKNLPKEDAHALGIFLRDLTTMDPLDAQA
QYSELFDRGRATSLLLFEHVHGESRDRGQAMVDLLAQYEQHGLQLNSRELPDHLPLYLEY
LAQLPQSEAVEGLKDIAPILALLSARLQQRESRYAVLFDLLLKLANTAIDSDKVAEKIAD
EARDDTPQALDAVWEEEQVKFFADKGCGDSAITAHQRRFAGAVAPQYLNITTGGQH
References
External Links:
ResourceLink
Uniprot ID:P0AF26
Uniprot Name:NARJ_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:4902934
Ecogene ID:EG10641
Ecocyc:EG10641
ColiBase:b1226
Kegg Gene:b1226
EchoBASE ID:EB0635
CCDB:NARJ_ECOLI
BacMap:16129189
General Reference:
  • Blasco, F., Dos Santos, J. P., Magalon, A., Frixon, C., Guigliarelli, B., Santini, C. L., Giordano, G. (1998). "NarJ is a specific chaperone required for molybdenum cofactor assembly in nitrate reductase A of Escherichia coli." Mol Microbiol 28:435-447. Pubmed: 9632249
  • Blasco, F., Iobbi, C., Giordano, G., Chippaux, M., Bonnefoy, V. (1989). "Nitrate reductase of Escherichia coli: completion of the nucleotide sequence of the nar operon and reassessment of the role of the alpha and beta subunits in iron binding and electron transfer." Mol Gen Genet 218:249-256. Pubmed: 2674654
  • Blattner, F. R., Plunkett, G. 3rd, 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. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Chan, C. S., Howell, J. M., Workentine, M. L., Turner, R. J. (2006). "Twin-arginine translocase may have a role in the chaperone function of NarJ from Escherichia coli." Biochem Biophys Res Commun 343:244-251. Pubmed: 16540088
  • Dubourdieu, M., DeMoss, J. A. (1992). "The narJ gene product is required for biogenesis of respiratory nitrate reductase in Escherichia coli." J Bacteriol 174:867-872. Pubmed: 1732220
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Liu, X., DeMoss, J. A. (1997). "Characterization of NarJ, a system-specific chaperone required for nitrate reductase biogenesis in Escherichia coli." J Biol Chem 272:24266-24271. Pubmed: 9305880
  • Oshima, T., Aiba, H., Baba, T., Fujita, K., Hayashi, K., Honjo, A., Ikemoto, K., Inada, T., Itoh, T., Kajihara, M., Kanai, K., Kashimoto, K., Kimura, S., Kitagawa, M., Makino, K., Masuda, S., Miki, T., Mizobuchi, K., Mori, H., Motomura, K., Nakamura, Y., Nashimoto, H., Nishio, Y., Saito, N., Horiuchi, T., et, a. l. .. (1996). "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." DNA Res 3:137-155. Pubmed: 8905232
  • Sodergren, E. J., DeMoss, J. A. (1988). "narI region of the Escherichia coli nitrate reductase (nar) operon contains two genes." J Bacteriol 170:1721-1729. Pubmed: 2832376
  • Vergnes, A., Pommier, J., Toci, R., Blasco, F., Giordano, G., Magalon, A. (2006). "NarJ chaperone binds on two distinct sites of the aponitrate reductase of Escherichia coli to coordinate molybdenum cofactor insertion and assembly." J Biol Chem 281:2170-2176. Pubmed: 16286471
  • Zakian, S., Lafitte, D., Vergnes, A., Pimentel, C., Sebban-Kreuzer, C., Toci, R., Claude, J. B., Guerlesquin, F., Magalon, A. (2010). "Basis of recognition between the NarJ chaperone and the N-terminus of the NarG subunit from Escherichia coli nitrate reductase." FEBS J 277:1886-1895. Pubmed: 20236317