| Entry |
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| Name |
Nitrogen metabolism - Sideroxydans lithotrophicus
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| 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.
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| Class |
Metabolism; Energy metabolism
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| Pathway map |

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| Module |
| Nitrogen fixation, nitrogen => ammonia [PATH: slt00910] | | Nitrification, ammonia => nitrite [PATH: slt00910] | | Denitrification, nitrate => nitrogen [PATH: slt00910] | | Dissimilatory nitrate reduction, nitrate => ammonia [PATH: slt00910] | | Assimilatory nitrate reduction, nitrate => ammonia [PATH: slt00910] | | |
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| Other DBs |
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| Organism |
Sideroxydans lithotrophicus [GN: slt]
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| Gene |
| | | | | | | molybdopterin oxidoreductase; K00372 nitrate reductase catalytic subunit [EC: 1.7.99.4] [KO: K00372] [EC: 1.7.99.4] | | 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] | | nitrite reductase (NAD(P)H); K00363 nitrite reductase (NAD(P)H) small subunit [EC: 1.7.1.4] [KO: K00363] [EC: 1.7.1.4] | | nitric-oxide reductase; K04561 nitric oxide reductase subunit B [EC: 1.7.2.5] [KO: K04561] [EC: 1.7.2.5] | | Cytochrome C class I; K02305 nitric oxide reductase subunit C [KO: K02305] | | nitrogenase molybdenum-iron protein alpha chain; K02586 nitrogenase molybdenum-iron protein alpha chain [EC: 1.18.6.1] [KO: K02586] [EC: 1.18.6.1] | | nitrogenase molybdenum-iron protein beta chain; K02591 nitrogenase molybdenum-iron protein beta chain [EC: 1.18.6.1] [KO: K02591] [EC: 1.18.6.1] | | | | nitrogen fixation protein NifW; K02595 nitrogenase-stabilizing/protective protein [KO: K02595] | | flavodoxin; K03839 flavodoxin I [KO: K03839] | | | | | | | | | | asparagine synthase family amidotransferase; K01953 asparagine synthase (glutamine-hydrolysing) [EC: 6.3.5.4] [KO: K01953] [EC: 6.3.5.4] | | nitrilase/cyanide hydratase and apolipoprotein N-acyltransferase; K01501 nitrilase [EC: 3.5.5.1] [KO: K01501] [EC: 3.5.5.1] | | ubiquinol-Cytochrome C reductase; K00411 ubiquinol-cytochrome c reductase iron-sulfur subunit [EC: 1.10.2.2] [KO: K00411] [EC: 1.10.2.2] | | cytochrome b/b6 domain protein; K00412 ubiquinol-cytochrome c reductase cytochrome b subunit [KO: K00412] | | Cytochrome C1; K00413 ubiquinol-cytochrome c reductase cytochrome c1 subunit [KO: K00413] | | nitrate transport ATP-binding protein; K15576 nitrate/nitrite transport system substrate-binding protein [KO: K15576] | | binding-protein-dependent transport systems inner membrane component; K15577 nitrate/nitrite transport system permease protein [KO: K15577] | | nitrate ABC transporter; K15578 nitrate/nitrite transport system ATP-binding protein [EC:3.6.3.-] [KO: K15578] [EC:3.6.3.-] | | NADH-ubiquinone/plastoquinone oxidoreductase chain 3; K00330 NADH-quinone oxidoreductase subunit A [EC: 1.6.5.3] [KO: K00330] [EC: 1.6.5.3] | | NADH-quinone oxidoreductase; K00331 NADH-quinone oxidoreductase subunit B [EC: 1.6.5.3] [KO: K00331] [EC: 1.6.5.3] | | NADH (or F420H2) dehydrogenase; K00332 NADH-quinone oxidoreductase subunit C [EC: 1.6.5.3] [KO: K00332] [EC: 1.6.5.3] | | NADH dehydrogenase I; K00333 NADH-quinone oxidoreductase subunit D [EC: 1.6.5.3] [KO: K00333] [EC: 1.6.5.3] | | NADH-quinone oxidoreductase; K00334 NADH-quinone oxidoreductase subunit E [EC: 1.6.5.3] [KO: K00334] [EC: 1.6.5.3] | | NADH-quinone oxidoreductase; K00335 NADH-quinone oxidoreductase subunit F [EC: 1.6.5.3] [KO: K00335] [EC: 1.6.5.3] | | NADH-quinone oxidoreductase; K00336 NADH-quinone oxidoreductase subunit G [EC: 1.6.5.3] [KO: K00336] [EC: 1.6.5.3] | | NADH dehydrogenase (quinone); K00337 NADH-quinone oxidoreductase subunit H [EC: 1.6.5.3] [KO: K00337] [EC: 1.6.5.3] | | NADH-quinone oxidoreductase; K00338 NADH-quinone oxidoreductase subunit I [EC: 1.6.5.3] [KO: K00338] [EC: 1.6.5.3] | | NADH-ubiquinone/plastoquinone oxidoreductase chain 6; K00339 NADH-quinone oxidoreductase subunit J [EC: 1.6.5.3] [KO: K00339] [EC: 1.6.5.3] | | NADH-ubiquinone oxidoreductase chain 4L; K00340 NADH-quinone oxidoreductase subunit K [EC: 1.6.5.3] [KO: K00340] [EC: 1.6.5.3] | | proton-translocating NADH-quinone oxidoreductase; K00341 NADH-quinone oxidoreductase subunit L [EC: 1.6.5.3] [KO: K00341] [EC: 1.6.5.3] | | proton-translocating NADH-quinone oxidoreductase; K00342 NADH-quinone oxidoreductase subunit M [EC: 1.6.5.3] [KO: K00342] [EC: 1.6.5.3] | | proton-translocating NADH-quinone oxidoreductase; K00343 NADH-quinone oxidoreductase subunit N [EC: 1.6.5.3] [KO: K00343] [EC: 1.6.5.3] | | NapC/NirT Cytochrome C domain protein; K02569 cytochrome c-type protein NapC [KO: K02569] | | pyruvate flavodoxin/ferredoxin oxidoreductase domain protein; K03737 putative pyruvate-flavodoxin oxidoreductase [EC:1.2.7.-] [KO: K03737] [EC:1.2.7.-] |
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| Compound |
| H2O | | ATP | | NAD+ | | NADH | | NADPH | | Oxygen | | ADP | | CO2 | | NH3 | | FAD | | Pyruvate | | L-Glutamate | | Glycine | | L-Aspartate | | Formate | | L-Glutamine | | Formaldehyde | | H+ | | Nitrite | | Methanol | | L-Asparagine | | Carbamoyl phosphate | | Hydroxylamine | | Nitrate | | Ubiquinol | | Ubiquinone | | Formamide | | Cytochrome c | | Nitric oxide | | Nitrogen | | Nitrile | | Menaquinone | | Nitrous oxide | | Cytochrome c-552 | | NH4+ | | Carbonic acid | | NH4OH | | Cyanate | | Methane | | Carbamate | | Ferredoxin | | Hydrazine | | Menaquinol | | Nitroalkane | | Cytochrome c-554 | | Cytochrome P-460 | | Membrane-associated cytochrome c-552 | | Cytochrome c-550 | | Pseudoazurin | | Cytochrome b | | Molybdopterin guanine dinucleotide | | Ferredoxin N | | FdI |
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| Reference |
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| 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 |
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| 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 |
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| 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 |
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| Authors |
Cabello P, Roldan MD, Moreno-Vivian C |
| Title |
Nitrate reduction and the nitrogen cycle in archaea. |
| Journal |
Microbiology 150:3527-46 (2004) |
| Reference |
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| 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 |
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| Authors |
Morozkina EV, Zvyagilskaya RA |
| Title |
Nitrate reductases: structure, functions, and effect of stress factors. |
| Journal |
Biochemistry (Mosc) 72:1151-60 (2007) |
| Reference |
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| 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 |
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| 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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