KEGG   PATHWAY: soh00680
Entry
soh00680                    Pathway                                
Name
Methane metabolism - Sulfurisphaera ohwakuensis
Description
Methane is metabolized principally by methanotrophs and methanogens in the global carbon cycle. Methanotrophs consume methane as the only source of carbon, while methanogens produce methane as a metabolic byproduct. Methylotrophs, which are microorganisms that can obtain energy for growth by oxidizing one-carbon compounds, such as methanol and methane, are situated between methanotrophs and methanogens. Methanogens can obtain energy for growth by converting a limited number of substrates to methane under anaerobic conditions. Three types of methanogenic pathways are known: CO2 to methane [MD:M00567], methanol to methane [MD:M00356], and acetate to methane [MD:M00357]. Methanogens use 2-mercaptoethanesulfonate (CoM; coenzyme M) as the terminal methyl carrier in methanogenesis and have four enzymes for CoM biosynthesis [MD:M00358]. Coenzyme B-Coenzyme M heterodisulfide reductase (Hdr), requiring for the final reaction steps of methanogenic pathway, is divided into two types: cytoplasmic HdrABC in most methanogens and membrane-bound HdrED in Methanosarcina species. In methanotrophs and methyltrophs methane is oxidized to form formaldehyde, which is at the diverging point for further oxidation to CO2 for energy source and assimilation for biosynthesis. There are three pathways that convert formaldehyde to C2 or C3 compounds: serine pathway [MD:M00346], ribulose monophosphate pathway [MD:M00345], and xylulose monophosphate pathway [MD:M00344]. The first two pathways are found in prokaryotes and the third is found in yeast. As a special case of methylotrophs, various amines can be used as carbon sources in trimethylamine metabolism [MD:M00563].
Class
Metabolism; Energy metabolism
Pathway map
soh00680  Methane metabolism
soh00680

Other DBs
GO: 0015947
Organism
Sulfurisphaera ohwakuensis [GN:soh]
Gene
D1869_01445  formate dehydrogenase subunit alpha [KO:K00123] [EC:1.17.1.9]
D1869_14815  formate dehydrogenase subunit alpha [KO:K00123] [EC:1.17.1.9]
D1869_07620  aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme [KO:K00600] [EC:2.1.2.1]
D1869_11170  DUF4147 domain-containing protein [KO:K11529] [EC:2.7.1.165]
D1869_07055  phosphopyruvate hydratase [KO:K01689] [EC:4.2.1.11]
D1869_11525  phosphoenolpyruvate carboxylase [KO:K01595] [EC:4.1.1.31]
D1869_10235  malate dehydrogenase [KO:K00024] [EC:1.1.1.37]
D1869_12880  aldolase [KO:K11645] [EC:4.1.2.13]
D1869_01185  fructose 1,6-bisphosphatase [KO:K01622] [EC:4.1.2.13 3.1.3.11]
D1869_00465  hxlB; 6-phospho-3-hexuloisomerase [KO:K08094] [EC:5.3.1.27]
D1869_00695  hxlA; 3-hexulose-6-phosphate synthase [KO:K08093] [EC:4.1.2.43]
D1869_10555  FAD-binding protein [KO:K03388] [EC:1.8.7.3 1.8.98.4 1.8.98.5 1.8.98.6]
D1869_10540  disulfide reductase [KO:K03389] [EC:1.8.7.3 1.8.98.4 1.8.98.5 1.8.98.6]
D1869_10560  heterodisulfide reductase subunit B [KO:K03389] [EC:1.8.7.3 1.8.98.4 1.8.98.5 1.8.98.6]
D1869_10545  4Fe-4S dicluster domain-containing protein [KO:K03390] [EC:1.8.7.3 1.8.98.4 1.8.98.5 1.8.98.6]
D1869_10565  4Fe-4S dicluster domain-containing protein [KO:K03390] [EC:1.8.7.3 1.8.98.4 1.8.98.5 1.8.98.6]
D1869_11095  acs; acetate--CoA ligase [KO:K01895] [EC:6.2.1.1]
D1869_03560  acs; acetate--CoA ligase [KO:K01895] [EC:6.2.1.1]
D1869_11715  AMP-binding protein [KO:K01895] [EC:6.2.1.1]
D1869_10175  AMP-binding protein [KO:K01895] [EC:6.2.1.1]
D1869_10205  AMP-binding protein [KO:K01895] [EC:6.2.1.1]
D1869_06930  AMP-binding protein [KO:K01895] [EC:6.2.1.1]
D1869_14680  AMP-binding protein [KO:K01895] [EC:6.2.1.1]
D1869_10120  pyruvate ferredoxin oxidoreductase [KO:K00169] [EC:1.2.7.1]
D1869_10115  pyruvate synthase subunit beta [KO:K00170] [EC:1.2.7.1]
D1869_08600  3-methyl-2-oxobutanoate dehydrogenase subunit beta [KO:K00170] [EC:1.2.7.1]
D1869_10130  pyruvate synthase [KO:K00172] [EC:1.2.7.1]
D1869_08585  pyruvate synthase [KO:K00172] [EC:1.2.7.1]
D1869_10125  4Fe-4S dicluster domain-containing protein [KO:K00171] [EC:1.2.7.1]
D1869_08590  4Fe-4S dicluster domain-containing protein [KO:K00171] [EC:1.2.7.1]
D1869_07190  ppsA; pyruvate, water dikinase [KO:K01007] [EC:2.7.9.2]
D1869_11620  histidine phosphatase family protein [KO:K15634] [EC:5.4.2.11]
D1869_01610  2,3-bisphosphoglycerate-independent phosphoglycerate mutase [KO:K15635] [EC:5.4.2.12]
D1869_07095  3-phosphoglycerate dehydrogenase [KO:K00058] [EC:1.1.1.95 1.1.1.399]
D1869_11455  Ldh family oxidoreductase [KO:K05884] [EC:1.1.1.337]
Compound
C00011  CO2
C00022  Pyruvate
C00024  Acetyl-CoA
C00033  Acetate
C00036  Oxaloacetate
C00037  Glycine
C00048  Glyoxylate
C00058  Formate
C00065  L-Serine
C00067  Formaldehyde
C00074  Phosphoenolpyruvate
C00082  L-Tyrosine
C00085  D-Fructose 6-phosphate
C00101  Tetrahydrofolate
C00111  Glycerone phosphate
C00118  D-Glyceraldehyde 3-phosphate
C00132  Methanol
C00143  5,10-Methylenetetrahydrofolate
C00149  (S)-Malate
C00168  Hydroxypyruvate
C00184  Glycerone
C00197  3-Phospho-D-glycerate
C00199  D-Ribulose 5-phosphate
C00218  Methylamine
C00227  Acetyl phosphate
C00231  D-Xylulose 5-phosphate
C00237  CO
C00258  D-Glycerate
C00322  2-Oxoadipate
C00354  D-Fructose 1,6-bisphosphate
C00483  Tyramine
C00543  Dimethylamine
C00565  Trimethylamine
C00593  Sulfoacetaldehyde
C00631  2-Phospho-D-glycerate
C00862  Methanofuran
C00876  Coenzyme F420
C01001  Formylmethanofuran
C01005  O-Phospho-L-serine
C01031  S-Formylglutathione
C01046  N-Methyl-L-glutamate
C01080  Reduced coenzyme F420
C01104  Trimethylamine N-oxide
C01217  5,6,7,8-Tetrahydromethanopterin
C01274  5-Formyl-5,6,7,8-tetrahydromethanopterin
C01438  Methane
C03232  3-Phosphonooxypyruvate
C03576  Coenzyme M
C03920  2-(Methylthio)ethanesulfonate
C04330  5,10-Methenyltetrahydromethanopterin
C04348  L-Malyl-CoA
C04377  5,10-Methylenetetrahydromethanopterin
C04488  5-Methyl-5,6,7,8-tetrahydromethanopterin
C04628  Coenzyme B
C04732  5-Amino-6-(1-D-ribitylamino)uracil
C04832  Coenzyme M 7-mercaptoheptanoylthreonine-phosphate heterodisulfide
C05528  3-Sulfopyruvate
C06019  D-arabino-Hex-3-ulose 6-phosphate
C11536  (2R)-O-Phospho-3-sulfolactate
C11537  (2R)-3-Sulfolactate
C14180  S-(Hydroxymethyl)glutathione
C16583  (R)-(Homo)2-citrate
C16588  2-Oxopimelate
C16589  2-Oxosuberate
C16590  7-Oxoheptanoic acid
C16593  7-Mercaptoheptanoic acid
C16594  7-Mercaptoheptanoylthreonine
C16597  (-)-threo-Iso(homo)2-citrate
C16598  (R)-(Homo)3-citrate
C16600  (-)-threo-Iso(homo)3-citrate
C18799  5-Methyl-H4SPT
C18802  Tetrahydrosarcinapterin
C19151  Coenzyme F420-3
C19152  Coenzyme F420-1
C19153  Coenzyme F420-0
C19154  7,8-Didemethyl-8-hydroxy-5-deazariboflavin
C19155  (2S)-Lactyl-2-diphospho-5'-guanosine
C19156  (2S)-2-Phospholactate
C20581  cis-(Homo)2-aconitate
C20582  cis-(Homo)3-aconitate
C20926  gamma-Glutamyltyramine
C20954  (5-Formylfuran-3-yl)methyl phosphate
C21068  [5-(Aminomethyl)furan-3-yl]methyl phosphate
C21069  [5-(Aminomethyl)furan-3-yl]methyl diphosphate
C21070  (4-{4-[2-(gamma-L-Glutamylamino)ethyl]phenoxymethyl}furan-2-yl)methanamine
C21971  5-Amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil
C22277  Dehydro coenzyme F420-0
C22297  Enolpyruvoyl-2-diphospho-5'-guanosine
Reference
  Authors
Graham DE, Xu H, White RH
  Title
Identification of coenzyme M biosynthetic phosphosulfolactate synthase: a new family of sulfonate-biosynthesizing enzymes.
  Journal
J Biol Chem 277:13421-9 (2002)
DOI:10.1074/jbc.M201011200
Reference
  Authors
Deppenmeier U
  Title
The membrane-bound electron transport system of Methanosarcina species.
  Journal
J Bioenerg Biomembr 36:55-64 (2004)
DOI:10.1023/B:JOBB.0000019598.64642.97
Reference
  Authors
Hallam SJ, Putnam N, Preston CM, Detter JC, Rokhsar D, Richardson PM, DeLong EF
  Title
Reverse methanogenesis: testing the hypothesis with environmental genomics.
  Journal
Science 305:1457-62 (2004)
DOI:10.1126/science.1100025
Reference
  Authors
Welander PV, Metcalf WW
  Title
Loss of the mtr operon in Methanosarcina blocks growth on methanol, but not methanogenesis, and reveals an unknown methanogenic pathway.
  Journal
Proc Natl Acad Sci U S A 102:10664-9 (2005)
DOI:10.1073/pnas.0502623102
Reference
  Authors
Yurimoto H, Kato N, Sakai Y
  Title
Assimilation, dissimilation, and detoxification of formaldehyde, a central metabolic intermediate of methylotrophic metabolism.
  Journal
Chem Rec 5:367-75 (2005)
DOI:10.1002/tcr.20056
Reference
  Authors
Fricke WF, Seedorf H, Henne A, Kruer M, Liesegang H, Hedderich R, Gottschalk G, Thauer RK.
  Title
The genome sequence of Methanosphaera stadtmanae reveals why this human intestinal archaeon is restricted to methanol and H2 for methane formation and ATP synthesis.
  Journal
J Bacteriol 188:642-58 (2006)
DOI:10.1128/JB.188.2.642-658.2006
Reference
  Authors
Kato N, Yurimoto H, Thauer RK
  Title
The physiological role of the ribulose monophosphate pathway in bacteria and archaea.
  Journal
Biosci Biotechnol Biochem 70:10-21 (2006)
DOI:10.1271/bbb.70.10
Reference
  Authors
Thauer RK, Kaster AK, Seedorf H, Buckel W, Hedderich R
  Title
Methanogenic archaea: ecologically relevant differences in energy conservation.
  Journal
Nat Rev Microbiol 6:579-91 (2008)
DOI:10.1038/nrmicro1931
Reference
  Authors
Liffourrena AS, Salvano MA, Lucchesi GI
  Title
Pseudomonas putida A ATCC 12633 oxidizes trimethylamine aerobically via two different pathways.
  Journal
Arch Microbiol 192:471-6 (2010)
DOI:10.1007/s00203-010-0577-5
Related
pathway
soh00010  Glycolysis / Gluconeogenesis
soh00030  Pentose phosphate pathway
soh00260  Glycine, serine and threonine metabolism
soh00300  Lysine biosynthesis
soh00630  Glyoxylate and dicarboxylate metabolism
soh00720  Other carbon fixation pathways
soh00740  Riboflavin metabolism
soh00790  Folate biosynthesis
soh00910  Nitrogen metabolism
soh00920  Sulfur metabolism
KO pathway
ko00680   
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