ENTRY       sly00920                    Pathway
NAME        Sulfur metabolism - Solanum lycopersicum (tomato)
DESCRIPTION Sulfur is an essential element for life and the metabolism of organic sulfur compounds plays an important role in the global sulfur cycle. Sulfur occurs in various oxidation states ranging from +6 in sulfate to -2 in sulfide (H2S). Sulfate reduction can occur in both an energy consuming assimilatory pathway and an energy producing dissimilatory pathway. The assimilatory pathway, which is found in a wide range of organisms, produces reduced sulfur compounds for the biosynthesis of S-containing amino acids and does not lead to direct excretion of sulfide. In the dissimilatory pathway, which is restricted to obligatory anaerobic bacterial and archaeal lineages, sulfate (or sulfur) is the terminal electron acceptor of the respiratory chain producing large quantities of inorganic sulfide. Both pathways start from the activation of sulfate by reaction with ATP to form adenylyl sulfate (APS). In the assimilatory pathway [MD:M00176] APS is converted to 3'-phosphoadenylyl sulfate (PAPS) and then reduced to sulfite, and sulfite is further reduced to sulfide by the assimilatory sulfite reductase. In the dissimilatory pathway [MD:M00596] APS is directly reduced to sulfite, and sulfite is further reduced to sulfide by the dissimilatory sulfite reductase. The capacity for oxidation of sulfur is quite widespread among bacteria and archaea, comprising phototrophs and chemolithoautotrophs. The SOX (sulfur-oxidation) system [MD:M00595] is a well-known sulfur oxidation pathway and is found in both photosynthetic and non-photosynthetic sulfur-oxidizing bacteria. Green sulfur bacteria and purple sulfur bacteria carry out anoxygenic photosynthesis with reduced sulfur compounds such as sulfide and elemental sulfur, as well as thiosulfate (in some species with the SOX system), as the electron donor for photoautotrophic growth. In some chemolithoautotrophic sulfur oxidizers (such as Thiobacillus denitrificans), it has been suggested that dissimilatory sulfur reduction enzymes operate in the reverse direction, forming a sulfur oxidation pathway from sulfite to APS and then to sulfate.
CLASS       Metabolism; Energy metabolism
PATHWAY_MAP sly00920  Sulfur metabolism
MODULE      sly_M00021  Cysteine biosynthesis, serine => cysteine [PATH:sly00920]
DBLINKS     GO: 0006790
ORGANISM    Solanum lycopersicum (tomato) [GN:sly]
GENE        101256557  ATP sulfurylase 1, chloroplastic [KO:K13811] [EC:2.7.7.4 2.7.1.25]
            101259979  ATP sulfurylase 1, chloroplastic-like [KO:K13811] [EC:2.7.7.4 2.7.1.25]
            101256255  ATP sulfurylase 1, chloroplastic-like [KO:K13811] [EC:2.7.7.4 2.7.1.25]
            101265563  bifunctional adenosine 5'-phosphosulfate phosphorylase/adenylylsulfatase HINT4 [KO:K22966] [EC:2.7.7.5 3.6.2.1]
            101247286  adenylyl-sulfate kinase 3 [KO:K00860] [EC:2.7.1.25]
            101267663  adenylyl-sulfate kinase 3 [KO:K00860] [EC:2.7.1.25]
            101262973  adenylyl-sulfate kinase 3 [KO:K00860] [EC:2.7.1.25]
            101259503  PAP-specific phosphatase HAL2-like [KO:K01082] [EC:3.1.3.7]
            101251056  putative PAP-specific phosphatase, mitochondrial [KO:K01082] [EC:3.1.3.7]
            101246318  PAP-specific phosphatase HAL2-like [KO:K01082] [EC:3.1.3.7]
            101251352  putative PAP-specific phosphatase, mitochondrial [KO:K01082] [EC:3.1.3.7]
            101267407  SAL1 phosphatase [KO:K15422] [EC:3.1.3.7 3.1.3.57]
            101257319  5'-adenylylsulfate reductase 3, chloroplastic [KO:K05907] [EC:1.8.4.9]
            101252466  5'-adenylylsulfate reductase 3, chloroplastic-like [KO:K05907] [EC:1.8.4.9]
            544267  adenylyl-sulfate reductase [KO:K05907] [EC:1.8.4.9]
            100134877  SO; sulfite oxidase [KO:K00387] [EC:1.8.3.1]
            101055609  sulfite reductase [KO:K00392] [EC:1.8.7.1]
            101254405  persulfide dioxygenase ETHE1 homolog, mitochondrial isoform X1 [KO:K17725] [EC:1.13.11.18]
            101268552  persulfide dioxygenase ETHE1 homolog, mitochondrial-like [KO:K17725] [EC:1.13.11.18]
            100301939  MST1; mercaptopyruvate sulfurtransferase-like protein [KO:K01011] [EC:2.8.1.1 2.8.1.2]
            100301940  MST2; thiosulfate sulfurtransferase [KO:K01011] [EC:2.8.1.1 2.8.1.2]
            101253958  serine acetyltransferase 2 [KO:K00640] [EC:2.3.1.30]
            101245503  serine acetyltransferase 1, chloroplastic [KO:K00640] [EC:2.3.1.30]
            101266998  serine acetyltransferase 5 [KO:K00640] [EC:2.3.1.30]
            101257583  serine acetyltransferase 1, chloroplastic-like [KO:K00640] [EC:2.3.1.30]
            101246283  cysteine synthase [KO:K01738] [EC:2.5.1.47]
            101245992  cysteine synthase-like isoform X1 [KO:K01738] [EC:2.5.1.47]
            101246567  cysteine synthase [KO:K01738] [EC:2.5.1.47]
            101256331  cysteine synthase-like [KO:K01738] [EC:2.5.1.47]
            101244415  cysteine synthase [KO:K01738] [EC:2.5.1.47]
            101253301  cysteine synthase 2 isoform X1 [KO:K01738] [EC:2.5.1.47]
            101254617  cysteine synthase, chloroplastic/chromoplastic isoform X1 [KO:K01738] [EC:2.5.1.47]
            101253940  bifunctional L-3-cyanoalanine synthase/cysteine synthase 1, mitochondrial [KO:K13034] [EC:2.5.1.47 4.4.1.9]
            101255033  bifunctional L-3-cyanoalanine synthase/cysteine synthase 2, mitochondrial [KO:K13034] [EC:2.5.1.47 4.4.1.9]
            543920  CGS; cystathionine gamma synthase [KO:K01739] [EC:2.5.1.48]
            101249583  selenium-binding protein 2 [KO:K17285] [EC:1.8.3.4]
COMPOUND    C00033  Acetate
            C00042  Succinate
            C00053  3'-Phosphoadenylyl sulfate
            C00054  Adenosine 3',5'-bisphosphate
            C00059  Sulfate
            C00065  L-Serine
            C00084  Acetaldehyde
            C00087  Sulfur
            C00094  Sulfite
            C00097  L-Cysteine
            C00155  L-Homocysteine
            C00224  Adenylyl sulfate
            C00245  Taurine
            C00263  L-Homoserine
            C00283  Hydrogen sulfide
            C00320  Thiosulfate
            C00409  Methanethiol
            C00580  Dimethyl sulfide
            C00979  O-Acetyl-L-serine
            C01118  O-Succinyl-L-homoserine
            C01861  Trithionate
            C02084  Tetrathionate
            C03920  2-(Methylthio)ethanesulfonate
            C04022  S,S-Dimethyl-beta-propiothetin
            C08276  3-(Methylthio)propanoate
            C11142  Dimethyl sulfone
            C11143  Dimethyl sulfoxide
            C11145  Methanesulfonic acid
            C15521  Alkanesulfonate
            C17267  S-Sulfanylglutathione
            C19692  Polysulfide
            C20870  3-(Methylthio)propanoyl-CoA
            C20955  3-(Methylthio)acryloyl-CoA
REFERENCE   PMID:22982583
  AUTHORS   Grein F, Ramos AR, Venceslau SS, Pereira IA
  TITLE     Unifying concepts in anaerobic respiration: Insights from dissimilatory sulfur metabolism.
  JOURNAL   Biochim Biophys Acta 1827:145-60 (2013)
            DOI:10.1016/j.bbabio.2012.09.001
REFERENCE   PMID:22633058
  AUTHORS   Fauque GD, Barton LL
  TITLE     Hemoproteins in dissimilatory sulfate- and sulfur-reducing prokaryotes.
  JOURNAL   Adv Microb Physiol 60:1-90 (2012)
            DOI:10.1016/B978-0-12-398264-3.00001-2
REFERENCE   PMID:20143161
  AUTHORS   Sakurai H, Ogawa T, Shiga M, Inoue K
  TITLE     Inorganic sulfur oxidizing system in green sulfur bacteria.
  JOURNAL   Photosynth Res 104:163-76 (2010)
            DOI:10.1007/s11120-010-9531-2
REFERENCE   PMID:22092713
  AUTHORS   Falkenby LG, Szymanska M, Holkenbrink C, Habicht KS, Andersen JS, Miller M, Frigaard NU
  TITLE     Quantitative proteomics of Chlorobaculum tepidum: insights into the sulfur metabolism of a phototrophic green sulfur bacterium.
  JOURNAL   FEMS Microbiol Lett 323:142-50 (2011)
            DOI:10.1111/j.1574-6968.2011.02370.x
REFERENCE   PMID:21833341
  AUTHORS   Gregersen LH, Bryant DA, Frigaard NU
  TITLE     Mechanisms and evolution of oxidative sulfur metabolism in green sulfur bacteria.
  JOURNAL   Front Microbiol 2:116 (2011)
            DOI:10.3389/fmicb.2011.00116
REFERENCE   PMID:16452431
  AUTHORS   Beller HR, Chain PS, Letain TE, Chakicherla A, Larimer FW, Richardson PM, Coleman MA, Wood AP, Kelly DP.
  TITLE     The genome sequence of the obligately chemolithoautotrophic, facultatively anaerobic bacterium Thiobacillus denitrificans.
  JOURNAL   J Bacteriol 188:1473-88 (2006)
            DOI:10.1128/JB.188.4.1473-1488.2006
REFERENCE   PMID:9695921
  AUTHORS   Pott AS, Dahl C
  TITLE     Sirohaem sulfite reductase and other proteins encoded by genes at the dsr locus of Chromatium vinosum are involved in the oxidation of intracellular sulfur.
  JOURNAL   Microbiology 144 ( Pt 7):1881-94 (1998)
            DOI:10.1099/00221287-144-7-1881
REFERENCE   PMID:18929068
  AUTHORS   Frigaard NU, Dahl C
  TITLE     Sulfur metabolism in phototrophic sulfur bacteria.
  JOURNAL   Adv Microb Physiol 54:103-200 (2009)
            DOI:10.1016/S0065-2911(08)00002-7
REL_PATHWAY sly00260  Glycine, serine and threonine metabolism
            sly00270  Cysteine and methionine metabolism
KO_PATHWAY  ko00920
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