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Entry
rhi00910                    Pathway                                

Name
Nitrogen metabolism - Sinorhizobium fredii NGR234
Description
The biological process of the nitrogen cycle is a complex interplay among many microorganisms catalyzing different reactions. In biological world, nitrogen is found in varying oxidation states from nitrate (the most oxidized form) to ammonia (the most reduced form). Gaseous nitrogen cannot be absorbed and used as a nutrient by plants and animals. It must first be converted to ammonia by microorganisms, so that it can enter the ecological chain as part of the nitrogen cycle. The core nitrogen cycle involves four reduction pathways and two oxidation pathways. Nitrogen fixation [MD:M00175] is the process of reducing atmospheric molecular nitrogen to ammonia, a biologically useful reduced form incorporated into the amino acids and other vital compounds. The ability of fixing atmospheric nitrogen by the nitrogenase enzyme complex is present in restricted prokaryotes (diazotroph). Assimilatory nitrate reduction [MD:M00531] is the biological conversion of nitrite or nitrate to ammonia. Dissimilatory nitrate reduction includes two different processes: denitrification [MD:M00529] and dissimilatory nitrate reduction to ammonium [MD:M00530]. Denitrification is a respiration in which nitrate or nitrite is reduced as a terminal electron acceptor under low oxygen or anoxic conditions. As a consequence, gaseous nitrogen compounds (N2, NO and N2O) are produced to the atmosphere. Denitrifying organisms are found among bacteria, archaea and eukaryotes, but mainly in heterotrophic microorganism. The two oxidation pathways are anammox and nitrification [MD:M00528]. Anammox (anaerobic ammonium oxidation) is a recently discovered biochemical process of oxidizing ammonium into dinitrogen gas using nitrite as an electron acceptor. It is catabolized in the anammoxosome that is a membrane bound compartment inside the cytoplasm. Planctomycetes (e.g., K. stuttgartiensis), known chemolithoautotroph, performs this anammox process. Nitrification is the biological conversion of ammonia to nitrite or nitrate. Ammonia-oxidizing microorganisms (e.g., Nitrosomonas and Nitrosococcus) oxidize ammonia with oxygen into nitrite and, following this metabolic process, nitrite-oxidizing microorganisms (e.g., Nitrobacter) oxidize nitrite into nitrate under an aerobic condition. These chemolithoautotrophic microorganisms use ammonia or nitrite as a respiratory substance and use electrons from the oxidation of compounds to produce energy.
Class
Metabolism; Energy metabolism
BRITE hierarchy
Pathway map
Nitrogen metabolism
rhi00910

All organismsOrtholog table
Module
Nitrogen fixation, nitrogen => ammonia [PATH:rhi00910]
Nitrification, ammonia => nitrite [PATH:rhi00910]
Denitrification, nitrate => nitrogen [PATH:rhi00910]
Dissimilatory nitrate reduction, nitrate => ammonia [PATH:rhi00910]
Assimilatory nitrate reduction, nitrate => ammonia [PATH:rhi00910]
Ammonia oxidation [PATH:rhi00910]
Other DBs
BSID: 
GO: 
Organism
Sinorhizobium fredii NGR234 [GN:rhi]
Gene
carbonic anhydrase; K01673 carbonic anhydrase [EC:4.2.1.1] [KO:K01673] [EC:4.2.1.1]
cah; carbonic anhydrase, Cah [KO:K01674] [EC:4.2.1.1]
aspA; aspartate ammonia-lyase [KO:K01744] [EC:4.3.1.1]
2-nitropropane dioxygenase-like dioxygenase; K00459 nitronate monooxygenase [EC:1.13.12.16] [KO:K00459] [EC:1.13.12.16]
narB; assimilatory nitrate reductase [KO:K00372] [EC:1.7.99.4]
napA; nitrate reductase catalytic subunit [KO:K02567] [EC:1.7.99.4]
napB; NapB periplasmic nitrate reductase [KO:K02568]
nitrite reductase [NAD(P)H]; K00362 nitrite reductase (NAD(P)H) large subunit [EC:1.7.1.4] [KO:K00362] [EC:1.7.1.4]
nirD; nitrite reductase small subunit [KO:K00363] [EC:1.7.1.4]
nirK; copper-containing nitrite reductase [KO:K00368] [EC:1.7.2.1]
norB; nitric-oxide reductase subunit B [KO:K04561] [EC:1.7.2.5]
norC; nitric-oxide reductase subunit C [KO:K02305]
nifD2; nitrogenase molybdenum-iron protein subunit alpha NifD2 [KO:K02586] [EC:1.18.6.1]
nifD1; nitrogenase molybdenum-iron protein subunit alpha NifD1 [KO:K02586] [EC:1.18.6.1]
nifK2; nitrogenase molybdenum-iron protein subunit beta NifK2 [KO:K02591] [EC:1.18.6.1]
nifK1; nitrogenase molybdenum-iron protein subunit beta NifK1 [KO:K02591] [EC:1.18.6.1]
nifH; nitrogenase reductase [KO:K02588] [EC:1.18.6.1]
nifH; nitrogenase reductase [KO:K02588] [EC:1.18.6.1]
nifW; nitrogenase stabilizing/protective protein [KO:K02595]
NAD-glutamate dehydrogenase; K15371 glutamate dehydrogenase [EC:1.4.1.2] [KO:K15371] [EC:1.4.1.2]
glutamate dehydrogenase; K00261 glutamate dehydrogenase (NAD(P)+) [EC:1.4.1.3] [KO:K00261] [EC:1.4.1.3]
gdh; glutamate dehydrogenase [KO:K00261] [EC:1.4.1.3]
glnA2; glutamine synthetase [KO:K01915] [EC:6.3.1.2]
glnA1; glutamine synthetase [KO:K01915] [EC:6.3.1.2]
glnT; glutamine synthetase [KO:K01915] [EC:6.3.1.2]
glnA3; glutamine synthetase [KO:K01915] [EC:6.3.1.2]
glnII; glutamine synthetase [KO:K01915] [EC:6.3.1.2]
glsA; glutaminase [KO:K01425] [EC:3.5.1.2]
gltB1; glutamate synthase [NADPH] large subunit [KO:K00265] [EC:1.4.1.14 1.4.1.13]
gltB2; oxidoreductase [KO:K00266] [EC:1.4.1.14 1.4.1.13]
gltD; glutamate synthase subunit beta [KO:K00266] [EC:1.4.1.14 1.4.1.13]
asparagine synthase; K01953 asparagine synthase (glutamine-hydrolysing) [EC:6.3.5.4] [KO:K01953] [EC:6.3.5.4]
asparagine synthetase AsnB; K01953 asparagine synthase (glutamine-hydrolysing) [EC:6.3.5.4] [KO:K01953] [EC:6.3.5.4]
fbcF3; ubiquinol-cytochrome C reductase iron-sulfur subunit [KO:K00411] [EC:1.10.2.2]
fbcB; cytochrome B subunit of cytochrome bc1 [KO:K00412]
fbcC; cytochrome c1 [KO:K00413]
ctaD; cytochrome o ubiquinol oxidase subunit I [KO:K02274] [EC:1.9.3.1]
coxN; cytochrome c oxidase polypeptide I/III [KO:K02274] [EC:1.9.3.1]
ctaC; cytochrome c oxidase subunit II [KO:K02275] [EC:1.9.3.1]
coxM; cytochrome-c oxidase subunit II protein [KO:K02275] [EC:1.9.3.1]
coxO; cytochrome c oxidase subunit III [KO:K02276] [EC:1.9.3.1]
coxP; cytochrome c oxidase subunit III [KO:K02276] [EC:1.9.3.1]
ctaE; cytochrome c oxidase subunit III [KO:K02276] [EC:1.9.3.1]
nrtA; nitrate ABC transporter substrate-binding protein NrtA [KO:K15576]
nrtB; Nitrate transport permease NrtB [KO:K15577]
nrtC; nitrate ABC transporter ATPase [KO:K15578] [EC:3.6.3.-]
nuoA1; NADH-quinone oxidoreductase subunit A1 [KO:K00330] [EC:1.6.5.3]
nuoA2; NADH dehydrogenase subunit A [KO:K00330] [EC:1.6.5.3]
nuoB1; NADH dehydrogenase subunit B [KO:K00331] [EC:1.6.5.3]
nuoB2; NADH dehydrogenase subunit B [KO:K00331] [EC:1.6.5.3]
nuoC1; NADH dehydrogenase subunit C1 [KO:K00332] [EC:1.6.5.3]
nuoC2; NADH dehydrogenase subunit C [KO:K00332] [EC:1.6.5.3]
nuoD1; NADH-quinone oxidoreductase subunit D1 [KO:K00333] [EC:1.6.5.3]
nuoD2; NADH dehydrogenase subunit D [KO:K00333] [EC:1.6.5.3]
nuoE1; NADH dehydrogenase I subunit E1 [KO:K00334] [EC:1.6.5.3]
nuoE2; NADH dehydrogenase subunit E [KO:K00334] [EC:1.6.5.3]
nuoF1; NADH dehydrogenase I subunit F1 [KO:K00335] [EC:1.6.5.3]
nuoF2; NADH dehydrogenase I subunit F [KO:K00335] [EC:1.6.5.3]
nuoG2; NADH dehydrogenase subunit G [KO:K00336] [EC:1.6.5.3]
nuoH1; NADH dehydrogenase I subunit H1 [KO:K00337] [EC:1.6.5.3]
nuoH2; NADH dehydrogenase subunit H [KO:K00337] [EC:1.6.5.3]
nuoI2; NADH-quinone oxidoreductase subunit I2 [KO:K00338] [EC:1.6.5.3]
nuoI1; NADH dehydrogenase subunit I [KO:K00338] [EC:1.6.5.3]
NADH-ubiquinone oxidoreductase subunit J; K00339 NADH-quinone oxidoreductase subunit J [EC:1.6.5.3] [KO:K00339] [EC:1.6.5.3]
nuoJ; NADH dehydrogenase subunit J [KO:K00339] [EC:1.6.5.3]
NADH-ubiquinone oxidoreductase; K00340 NADH-quinone oxidoreductase subunit K [EC:1.6.5.3] [KO:K00340] [EC:1.6.5.3]
nuoK; NADH dehydrogenase subunit K [KO:K00340] [EC:1.6.5.3]
nuoL; NADH dehydrogenase subunit L [KO:K00341] [EC:1.6.5.3]
nuoM3; NADH-ubiquinone oxidoreductase subunit M3 [KO:K00342] [EC:1.6.5.3]
nuoM1; NADH dehydrogenase subunit M [KO:K00342] [EC:1.6.5.3]
nuoN1; NADH-quinone oxidoreductase subunit N1 [KO:K00343] [EC:1.6.5.3]
nuoN2; NADH dehydrogenase subunit N [KO:K00343] [EC:1.6.5.3]
napC; NapC membrane protein, e-donor to periplasmic nitrate reductase [KO:K02569]
electron transfer flavoprotein subunit beta; K03521 electron transfer flavoprotein beta subunit [KO:K03521]
fixA; nitrogen fixation protein FixA [KO:K03521]
electron transfer flavoprotein subunit beta; K03521 electron transfer flavoprotein beta subunit [KO:K03521]
electron transfer flavoprotein subunit alpha; K03522 electron transfer flavoprotein alpha subunit [KO:K03522]
fixB; nitrogen fixation protein FixB [KO:K03522]
fixC; nitrogen fixation protein FixC [KO:K00313] [EC:1.5.5.-]
Compound
C00001  
H2O
C00002  
ATP
C00003  
NAD+
C00004  
NADH
C00005  
NADPH
C00007  
Oxygen
C00008  
ADP
C00011  
CO2
C00014  
NH3
C00016  
FAD
C00022  
Pyruvate
C00025  
L-Glutamate
C00037  
Glycine
C00049  
L-Aspartate
C00058  
Formate
C00064  
L-Glutamine
C00067  
Formaldehyde
C00080  
H+
C00088  
Nitrite
C00132  
Methanol
C00152  
L-Asparagine
C00169  
Carbamoyl phosphate
C00192  
Hydroxylamine
C00244  
Nitrate
C00390  
Ubiquinol
C00399  
Ubiquinone
C00488  
Formamide
C00524  
Cytochrome c
C00533  
Nitric oxide
C00697  
Nitrogen
C00726  
Nitrile
C00828  
Menaquinone
C00887  
Nitrous oxide
C00949  
Cytochrome c-552
C01342  
NH4+
C01353  
Carbonic acid
C01358  
NH4OH
C01417  
Cyanate
C01438  
Methane
C01563  
Carbamate
C01695  
Ferredoxin
C05361  
Hydrazine
C05819  
Menaquinol
C06058  
Nitroalkane
C19922  
Cytochrome c-554
C19923  
Cytochrome P-460
C19924  
Membrane-associated cytochrome c-552
C19925  
Cytochrome c-550
C19926  
Pseudoazurin
C19927  
Cytochrome b
C19928  
Molybdopterin guanine dinucleotide
C19940  
Ferredoxin N
C19941  
FdI
Reference
  Authors
Scott JD, Ludwig RA
  Title
Azorhizobium caulinodans electron-transferring flavoprotein N electrochemically couples pyruvate dehydrogenase complex activity to N2 fixation.
  Journal
Microbiology 150:117-26 (2004)
Reference
  Authors
Kneip C, Lockhart P, Voss C, Maier UG
  Title
Nitrogen fixation in eukaryotes--new models for symbiosis.
  Journal
BMC Evol Biol 7:55 (2007)
Reference
  Authors
Whittaker M, Bergmann D, Arciero D, Hooper AB
  Title
Electron transfer during the oxidation of ammonia by the chemolithotrophic bacterium Nitrosomonas europaea.
  Journal
Biochim Biophys Acta 1459:346-55 (2000)
Reference
  Authors
Cabello P, Roldan MD, Moreno-Vivian C
  Title
Nitrate reduction and the nitrogen cycle in archaea.
  Journal
Microbiology 150:3527-46 (2004)
Reference
  Authors
Stolz JF, Basu P
  Title
Evolution of nitrate reductase: molecular and structural variations on a common function.
  Journal
Chembiochem 3:198-206 (2002)
Reference
  Authors
Morozkina EV, Zvyagilskaya RA
  Title
Nitrate reductases: structure, functions, and effect of stress factors.
  Journal
Biochemistry (Mosc) 72:1151-60 (2007)
Reference
  Authors
Jetten MS, Niftrik L, Strous M, Kartal B, Keltjens JT, Op den Camp HJ
  Title
Biochemistry and molecular biology of anammox bacteria.
  Journal
Crit Rev Biochem Mol Biol 44:65-84 (2009)
Reference
  Authors
Luesken FA, Wu ML, Op den Camp HJ, Keltjens JT, Stunnenberg H, Francoijs KJ, Strous M, Jetten MS
  Title
Effect of oxygen on the anaerobic methanotroph 'Candidatus Methylomirabilis oxyfera': kinetic and transcriptional analysis.
  Journal
Environ Microbiol 14:1024-34 (2012)
KO pathway
 

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