ENTRY       zma00920                    Pathway
NAME        Sulfur metabolism - Zea mays (maize)
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 zma00920  Sulfur metabolism
MODULE      zma_M00021  Cysteine biosynthesis, serine => cysteine [PATH:zma00920]
DBLINKS     GO: 0006790
ORGANISM    Zea mays (maize) [GN:zma]
GENE        100281036  bifunctional 3-phosphoadenosine 5-phosphosulfate synthetase 2 [KO:K13811] [EC:2.7.7.4 2.7.1.25]
            103643994  ATP-sulfurylase 3, chloroplastic-like [KO:K13811] [EC:2.7.7.4 2.7.1.25]
            103625889  ATP-sulfurylase 3, chloroplastic-like [KO:K13811] [EC:2.7.7.4 2.7.1.25]
            100284636  aprataxin [KO:K22966] [EC:2.7.7.5 3.6.2.1]
            100217102  adenylyl-sulfate kinase [KO:K00860] [EC:2.7.1.25]
            100276991  adenylyl-sulfate kinase [KO:K00860] [EC:2.7.1.25]
            100193315  uncharacterized protein LOC100193315 isoform 1 [KO:K00860] [EC:2.7.1.25]
            100857009  uncharacterized protein LOC100857009 [KO:K00860] [EC:2.7.1.25]
            100285812  uncharacterized protein LOC100285812 [KO:K01082] [EC:3.1.3.7]
            100192833  uncharacterized protein LOC100192833 [KO:K01082] [EC:3.1.3.7]
            100276170  uncharacterized protein LOC100276170 [KO:K15422] [EC:3.1.3.7 3.1.3.57]
            542492  diphosphonucleotide phosphatase 1 [KO:K15422] [EC:3.1.3.7 3.1.3.57]
            103647705  uncharacterized protein LOC103647705 [KO:K05907] [EC:1.8.4.9]
            606419  adenosine 5'-phosphosulfate reductase-like 1 [KO:K05907] [EC:1.8.4.9]
            103642918  sulfite oxidase [KO:K00387] [EC:1.8.3.1]
            542221  sulfite reductase [ferredoxin], chloroplastic [KO:K00392] [EC:1.8.7.1]
            100283164  uncharacterized protein LOC100283164 [KO:K17725] [EC:1.13.11.18]
            100272428  uncharacterized protein LOC100272428 [KO:K01011] [EC:2.8.1.1 2.8.1.2]
            100275494  uncharacterized protein LOC100275494 [KO:K01011] [EC:2.8.1.1 2.8.1.2]
            541958  serine acetyltransferase 1 [KO:K00640] [EC:2.3.1.30]
            541959  serine acetyltransferase 2 [KO:K00640] [EC:2.3.1.30]
            542499  serine acetyltransferase 3 [KO:K00640] [EC:2.3.1.30]
            103631673  probable serine acetyltransferase 2 [KO:K00640] [EC:2.3.1.30]
            542438  cysteine synthase [KO:K01738] [EC:2.5.1.47]
            100272829  uncharacterized protein LOC100272829 [KO:K01738] [EC:2.5.1.47]
            100280321  cysteine synthase 1 [KO:K01738] [EC:2.5.1.47]
            100216991  uncharacterized protein LOC100216991 [KO:K01738] [EC:2.5.1.47]
            100502310  cysteine synthase [KO:K01738] [EC:2.5.1.47]
            103646469  cysteine synthase [KO:K01738] [EC:2.5.1.47]
            100193476  uncharacterized protein LOC100193476 isoform 1 [KO:K01738] [EC:2.5.1.47]
            109939155  putative inactive cysteine synthase 2 [KO:K01738] [EC:2.5.1.47]
            103638079  cysteine synthase [KO:K01738] [EC:2.5.1.47]
            109942192  putative inactive cysteine synthase 2 [KO:K01738] [EC:2.5.1.47]
            100216722  cysteine synthase [KO:K13034] [EC:2.5.1.47 4.4.1.9]
            100191523  uncharacterized protein LOC100191523 [KO:K01739] [EC:2.5.1.48]
            541650  cystathionine gamma-synthase 1 [KO:K01739] [EC:2.5.1.48]
            103645417  probable cystathionine gamma-synthase 2 [KO:K01739] [EC:2.5.1.48]
            103645418  probable cystathionine gamma-synthase 2 [KO:K01739] [EC:2.5.1.48]
            103639836  selenium-binding protein 2 [KO:K17285] [EC:1.8.3.4]
            100192654  uncharacterized protein LOC100192654 [KO:K17285] [EC:1.8.3.4]
            118473198  selenium-binding protein 2-like [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 zma00260  Glycine, serine and threonine metabolism
            zma00270  Cysteine and methionine metabolism
KO_PATHWAY  ko00920
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