Identification
Name:Periplasmic nitrate reductase
Synonyms:Not Available
Gene Name:napA
Enzyme Class:
Biological Properties
General Function:Involved in oxidoreductase activity
Specific Function:Catalytic subunit of the periplasmic nitrate reductase (NAP). Only expressed at high levels during aerobic growth. NapAB complex receives electrons from the membrane-anchored tetraheme protein napC, thus allowing electron flow between membrane and periplasm. Essential function for nitrate assimilation and may have a role in anaerobic metabolism
Cellular Location:Periplasm
SMPDB Pathways:
KEGG Pathways:
  • Microbial metabolism in diverse environments ec01120
  • Nitrogen metabolism ec00910
KEGG Reactions:
1.0Thumb+1.0Acceptor+1.0Thumb+1.0Acceptor1.0Thumb+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+1.0Thumb1.0Thumb+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+1.0Thumb1.0Nitrite+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+2.0Electron1.0Thumb+1.0Thumb
1.0Selenate + 2.0Hydrogen ion + 2.0Electron → 1.0Selenite + 1.0Water
ReactionCard
1.0Thumb+2.0Thumb+1.0a menaquinol1.0Thumb+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+1.0Thumb1.0Thumb+1.0Thumb+1.0Thumb+2.0Thumb
2.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+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
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb+1.0Thumb
1.0Thumb+1.0Thumb1.0Menaquinone 8+1.0Thumb+1.0Thumb
1.0Menaquinol 8 + 1.0Nitrate → 1.0Menaquinone 8 + 1.0Water + 1.0Nitrite
ReactionCard
1.0Thumb+1.0acceptor1.0Thumb+1.0reduced acceptor
1.0Nitrite + 1.0acceptor → 1.0Nitrate + 1.0reduced acceptor
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB21652Ferricytochrome cMetaboCard
ECMDB23135Ferrocytochrome cMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB21245Menaquinol 8MetaboCard
ECMDB02878NitrateMetaboCard
ECMDB02786NitriteMetaboCard
ECMDB23788SelenateMetaboCard
ECMDB21355SeleniteMetaboCard
ECMDB01060Ubiquinol-8MetaboCard
ECMDB21296Ubiquinone-8MetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Component
cell part
periplasmic space
Function
4 iron, 4 sulfur cluster binding
binding
catalytic activity
cation binding
electron carrier activity
ion binding
iron-sulfur cluster binding
metal cluster binding
metal ion binding
molybdenum ion binding
nitrate reductase activity
oxidoreductase activity
oxidoreductase activity, acting on other nitrogenous compounds as donors
transition metal ion binding
Process
metabolic process
nitrate assimilation
nitrate metabolic process
nitrogen compound metabolic process
oxidation reduction
Gene Properties
Blattner:b2206
Gene OrientationCounterclockwise
Centisome Percentage:49.54
Left Sequence End2298289
Right Sequence End2300775
Gene Sequence:
>2487 bp
ATGAAACTCAGTCGTCGTAGCTTTATGAAAGCTAACGCCGTTGCGGCCGCTGCGGCGGCT
GCCGGTCTCAGCGTGCCGGGCGTTGCCCGCGCCGTTGTTGGTCAGCAGGAAGCCATCAAA
TGGGATAAAGCGCCGTGCCGTTTCTGCGGTACTGGTTGCGGCGTTCTGGTCGGAACGCAG
CAGGGACGTGTGGTGGCCTGTCAGGGCGACCCGGACGCACCGGTTAACCGTGGCCTGAAC
TGCATTAAGGGCTATTTCCTGCCCAAAATCATGTACGGTAAAGACCGTTTGACGCAGCCG
CTGCTGCGTATGAAAAACGGTAAATATGACAAAGAAGGCGAATTTACCCCAATCACCTGG
GATCAGGCCTTCGATGTGATGGAAGAGAAATTCAAAACCGCCCTGAAAGAAAAAGGGCCG
GAATCGATCGGTATGTTCGGTTCTGGTCAGTGGACTATCTGGGAAGGTTATGCCGCGTCC
AAGCTGTTTAAAGCGGGCTTCCGTTCGAACAACATCGACCCGAACGCGCGTCACTGTATG
GCGTCGGCAGTAGTTGGCTTTATGCGTACCTTTGGTATGGATGAGCCGATGGGCTGCTAT
GACGACATCGAGCAGGCTGACGCGTTTGTGCTGTGGGGCGCAAACATGGCGGAAATGCAC
CCGATCCTCTGGTCGCGCATCACTAACCGTCGTCTCTCTAACCAGAACGTCACCGTGGCG
GTGCTTTCTACCTACCAGCATCGTAGCTTCGAGCTGGCGGATAACGGCATCATCTTTACG
CCGCAATCTGACCTGGTGATCCTGAACTACATCGCCAACTATATCATTCAAAACAATGCG
ATAAATCAGGACTTCTTCAGCAAGCACGTTAACCTGCGCAAAGGGGCGACGGACATCGGC
TACGGTTTACGTCCGACCCATCCGCTGGAAAAAGCAGCGAAGAATCCGGGTTCTGACGCC
TCCGAACCGATGAGCTTTGAAGATTACAAAGCCTTCGTTGCCGAGTATACGCTGGAAAAA
ACTGCCGAAATGACCGGCGTGCCGAAAGACCAGTTAGAACAACTGGCGCAGCTGTATGCC
GATCCGAACAAGAAAGTCATCTCCTACTGGACGATGGGCTTCAACCAGCATACTCGTGGC
GTGTGGGCTAACAACCTGGTCTACAACCTGCACCTGCTGACCGGCAAAATTTCCCAGCCG
GGTTGCGGTCCGTTCTCCCTGACCGGGCAACCTTCTGCGTGTGGTACTGCGCGTGAAGTG
GGCACCTTTGCTCACCGTCTGCCTGCGGACATGGTGGTGACCAACGAGAAACACCGTGAT
ATCTGCGAGAAGAAGTGGAATATCCCGAGCGGCACCATTCCGGCGAAAATCGGTCTGCAC
GCGGTGGCACAAGACCGTGCGCTGAAAGACGGCAAACTGAATGTTTACTGGACCATGTGT
ACCAACAACATGCAGGCCGGGCCGAACATCAATGAAGAGCGTATGCCGGGCTGGCGCGAT
CCGCGCAACTTCATCATCGTCTCCGATCCGTATCCGACAGTCAGTGCGCTGGCCGCCGAC
TTGATCCTGCCGACCGCAATGTGGGTAGAGAAAGAGGGCGCTTACGGTAACGCCGAACGC
CGTACTCAGTTCTGGCGTCAACAGGTACAGGCACCGGGCGAAGCGAAATCGGATCTCTGG
CAGTTAGTCCAGTTCTCCCGCCGCTTCAAAACTGAAGAAGTATGGCCGGAAGATCTGCTG
GCGAAGAAACCGGAACTGCGTGGCAAAACGCTGTACGAAGTGCTGTATGCCACACCGGAA
GTGAGCAAATTCCCGGTATCCGAACTGGCGGAAGATCAGCTGAACGATGAATCCCGCGAG
CTGGGCTTCTATCTGCAAAAAGGGCTGTTCGAAGAGTACGCATGGTTTGGTCGCGGTCAC
GGTCACGATCTGGCACCGTTCGATGACTACCACAAAGCGCGCGGTCTGCGCTGGCCGGTG
GTGAACGGTAAAGAAACGCAGTGGCGTTACAGCGAAGGTAACGACCCGTACGTGAAAGCG
GGCGAAGGCTATAAGTTCTACGGTAAACCGGATGGCAAAGCGGTGATCTTCGCACTGCCA
TTCGAACCGGCGGCGGAAGCACCGGATGAAGAGTACGACCTGTGGCTCTCTACCGGACGC
GTTCTGGAGCACTGGCACACCGGCAGTATGACTCGCCGTGTACCAGAACTGCACCGCGCC
TTCCCGGAAGCGGTCCTGTTTATTCACCCGCTGGATGCGAAAGCGCGCGATCTGCGCCGT
GGCGACAAAGTGAAAGTGGTTTCTCGCCGTGGCGAAGTGATCTCGATTGTTGAAACGCGC
GGTCGTAACCGTCCGCCACAGGGCCTGGTGTACATGCCGTTCTTCGACGCCGCACAGTTG
GTTAACAAACTGACGCTGGATGCGACCGATCCGCTCTCGAAAGAGACGGACTTCAAGAAG
TGCGCGGTCAAACTGGAGAAGGTGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:828
Protein Molecular Weight:93041
Protein Theoretical pI:8
Signaling Regions:
  • 1-36
Transmembrane Regions:
  • None
Protein Sequence:
>Periplasmic nitrate reductase
MKLSRRSFMKANAVAAAAAAAGLSVPGVARAVVGQQEAIKWDKAPCRFCGTGCGVLVGTQ
QGRVVACQGDPDAPVNRGLNCIKGYFLPKIMYGKDRLTQPLLRMKNGKYDKEGEFTPITW
DQAFDVMEEKFKTALKEKGPESIGMFGSGQWTIWEGYAASKLFKAGFRSNNIDPNARHCM
ASAVVGFMRTFGMDEPMGCYDDIEQADAFVLWGANMAEMHPILWSRITNRRLSNQNVTVA
VLSTYQHRSFELADNGIIFTPQSDLVILNYIANYIIQNNAINQDFFSKHVNLRKGATDIG
YGLRPTHPLEKAAKNPGSDASEPMSFEDYKAFVAEYTLEKTAEMTGVPKDQLEQLAQLYA
DPNKKVISYWTMGFNQHTRGVWANNLVYNLHLLTGKISQPGCGPFSLTGQPSACGTAREV
GTFAHRLPADMVVTNEKHRDICEKKWNIPSGTIPAKIGLHAVAQDRALKDGKLNVYWTMC
TNNMQAGPNINEERMPGWRDPRNFIIVSDPYPTVSALAADLILPTAMWVEKEGAYGNAER
RTQFWRQQVQAPGEAKSDLWQLVQFSRRFKTEEVWPEDLLAKKPELRGKTLYEVLYATPE
VSKFPVSELAEDQLNDESRELGFYLQKGLFEEYAWFGRGHGHDLAPFDDYHKARGLRWPV
VNGKETQWRYSEGNDPYVKAGEGYKFYGKPDGKAVIFALPFEPAAEAPDEEYDLWLSTGR
VLEHWHTGSMTRRVPELHRAFPEAVLFIHPLDAKARDLRRGDKVKVVSRRGEVISIVETR
GRNRPPQGLVYMPFFDAAQLVNKLTLDATDPLSKETDFKKCAVKLEKV
References
External Links:
ResourceLink
Uniprot ID:P33937
Uniprot Name:NAPA_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85675313
Ecogene ID:EG12067
Ecocyc:EG12067
ColiBase:b2206
Kegg Gene:b2206
EchoBASE ID:EB1994
CCDB:NAPA_ECOLI
BacMap:16130143
General Reference:
  • 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
  • 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
  • Itoh, T., Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Kasai, H., Kimura, S., Kitakawa, M., Kitagawa, M., Makino, K., Miki, T., Mizobuchi, K., Mori, H., Mori, T., Motomura, K., Nakade, S., Nakamura, Y., Nashimoto, H., Nishio, Y., Oshima, T., Saito, N., Sampei, G., Seki, Y., Horiuchi, T., et, a. l. .. (1996). "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map." DNA Res 3:379-392. Pubmed: 9097040
  • Thomas, G., Potter, L., Cole, J. A. (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 174:167-171. Pubmed: 10234835
  • Tullman-Ercek, D., DeLisa, M. P., Kawarasaki, Y., Iranpour, P., Ribnicky, B., Palmer, T., Georgiou, G. (2007). "Export pathway selectivity of Escherichia coli twin arginine translocation signal peptides." J Biol Chem 282:8309-8316. Pubmed: 17218314