KEGG   PATHWAY: atu00920Help
Entry
atu00920                    Pathway                                

Name
Sulfur metabolism - Agrobacterium fabrum
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
BRITE hierarchy
Pathway map
atu00920  Sulfur metabolism
atu00920

Ortholog table
Other DBs
BSID: 7062
GO: 0006790
Organism
Agrobacterium fabrum [GN:atu]
Gene
Atu3504  sulfate ABC transporter substrate-binding protein [KO:K02048]
Atu0820  ABC transporter, substrate binding protein (sulfate) [KO:K02048]
Atu3503  ABC transporter permease [KO:K02046]
Atu0821  cysT; ABC transporter, membrane spanning protein [KO:K02046]
Atu3502  ABC transporter permease [KO:K02047]
Atu0822  ABC transporter, membrane spanning protein [KO:K02047]
Atu3501  ABC transporter permease [KO:K02045] [EC:3.6.3.25]
Atu0823  ABC transporter, nucleotide binding/ATPase protein [KO:K02045] [EC:3.6.3.25]
Atu1884  ssuA; ABC transporter, substrate binding protein (aliphatic sulfonate) [KO:K15553]
Atu6085  ABC transporter, substrate binding protein (nitrate/sulfonate) [KO:K15553]
Atu4154  aliphatic sulfonate ABC transporter substrate-binding protein [KO:K15553]
Atu6059  ssuA; ABC transporter, substrate binding protein (nitrate/sulfonate) [KO:K15553]
Atu6086  nrtB; ABC transporter, membrane spanning protein (nitrate/sulfonate) [KO:K15554]
Atu6057  ssuC; ABC transporter, membrane spanning protein (nitrate/sulfonates) [KO:K15554]
Atu4155  aliphatic sulfonate ABC transporter permease [KO:K15554]
Atu4156  aliphatic sulfonate ABC transporter ATPase [KO:K15555] [EC:3.6.3.-]
Atu6087  nrtC; ABC transporter, nucleotide binding/ATPase protein (nitrate/sulfonate) [KO:K15555] [EC:3.6.3.-]
Atu6058  ssuB; ABC transporter, nucleotide binding/ATPase protein (nitrate/sulfonates) [KO:K15555] [EC:3.6.3.-]
Atu3426  sulfonate monooxygenase [KO:K04091] [EC:1.14.14.5]
Atu3279  methanesulfonate sulfonatase [KO:K04091] [EC:1.14.14.5]
Atu3430  alkanesulfonate monooxygenase [KO:K04091] [EC:1.14.14.5]
Atu5527  NADH-dependent FMN reductase [KO:K00299] [EC:1.5.1.38]
Atu0816  cysN; sulfate adenylate transferase, subunit 1 [KO:K00956] [EC:2.7.7.4]
Atu0817  sulfate adenylate transferase, subunit 2 [KO:K00957] [EC:2.7.7.4]
Atu2428  pssB; 3'(2'),5'-bisphosphate nucleotidase CysQ [KO:K01082] [EC:3.1.3.7]
Atu0818  cysH; phosphoadenosine phosphosulfate reductase [KO:K00390] [EC:1.8.4.10 1.8.4.8]
Atu0146  cysJ; sulfite reductase (NADPH) flavoprotein alpha-component [KO:K00380] [EC:1.8.1.2]
Atu1456  cysI; sulfite reductase (NADPH) hemoprotein beta-component [KO:K00381] [EC:1.8.1.2]
Atu1215  thiosulfate sulfurtransferase [KO:K01011] [EC:2.8.1.2 2.8.1.1]
Atu1571  cysE; serine acetyltransferase [KO:K00640] [EC:2.3.1.30]
Atu0312  cysK; cysteine synthase [KO:K01738] [EC:2.5.1.47]
Atu1217  cysK; cysteine synthase [KO:K01738] [EC:2.5.1.47]
Atu2718  metA; homoserine O-succinyltransferase [KO:K00651] [EC:2.3.1.46]
Atu0432  O-succinylhomoserine sulfhydrylase [KO:K10764] [EC:2.5.1.-]
Atu3446  monooxygenase [KO:K17228] [EC:1.14.14.35]
Atu6078  hypothetical protein [KO:K17228] [EC:1.14.14.35]
Atu5526  monooxygenase [KO:K17228] [EC:1.14.14.35]
Atu1417  fad; enoyl-CoA hydratase [KO:K20036] [EC:4.2.1.155]
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
  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
  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
  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
  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
  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
  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
  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
KO pathway
ko00920   

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