KEGG   PATHWAY: paq00920Help
Entry
paq00920                    Pathway                                

Name
Sulfur metabolism - Pantoea ananatis PA13
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
Sulfur metabolism
paq00920

All organismsOrtholog table
Module
Assimilatory sulfate reduction, sulfate => H2S [PATH:paq00920]
Other DBs
BSID: 
GO: 
Organism
Pantoea ananatis PA13 [GN:paq]
Gene
thiosulfate-binding protein CysP; K02048 sulfate transport system substrate-binding protein [KO:K02048]
sulfate-binding protein precursor Sbp; K02048 sulfate transport system substrate-binding protein [KO:K02048]
sulfate transport system permease protein CysU; K02046 sulfate transport system permease protein [KO:K02046]
sulfate transport system permease CysW; K02047 sulfate transport system permease protein [KO:K02047]
sulfate/thiosulfate import ATP-binding protein CysA; K02045 sulfate transport system ATP-binding protein [EC:3.6.3.25] [KO:K02045] [EC:3.6.3.25]
taurine-binding periplasmic protein precursor TauA; K15551 taurine transport system substrate-binding protein [KO:K15551]
taurine transport system permease TauC; K15552 taurine transport system permease protein [KO:K15552]
taurine import ATP-binding protein TauB; K10831 taurine transport system ATP-binding protein [EC:3.6.3.36] [KO:K10831] [EC:3.6.3.36]
alpha-ketoglutarate-dependent taurine dioxygenase TauD; K03119 taurine dioxygenase [EC:1.14.11.17] [KO:K03119] [EC:1.14.11.17]
alkanesulfonate transporter substrate-binding subunit SsuA; K15553 sulfonate transport system substrate-binding protein [KO:K15553]
aliphatic sulfonates-binding protein SsuA; K15553 sulfonate transport system substrate-binding protein [KO:K15553]
aliphatic sulfonate transport permease protein SsuC; K15554 sulfonate transport system permease protein [KO:K15554]
aliphatic sulfonate transport ATP-binding protein SsuB; K15555 sulfonate transport system ATP-binding protein [EC:3.6.3.-] [KO:K15555] [EC:3.6.3.-]
alkanesulfonate monooxygenase SsuD; K04091 alkanesulfonate monooxygenase [EC:1.14.14.5] [KO:K04091] [EC:1.14.14.5]
alkanesulfonate monooxygenase 1 SsuD1; K04091 alkanesulfonate monooxygenase [EC:1.14.14.5] [KO:K04091] [EC:1.14.14.5]
FMN reductase SsuE; K00299 FMN reductase [EC:1.5.1.38] [KO:K00299] [EC:1.5.1.38]
sulfate adenylyltransferase subunit 1 CysN; K00956 sulfate adenylyltransferase subunit 1 [EC:2.7.7.4] [KO:K00956] [EC:2.7.7.4]
sulfate adenylyltransferase subunit 2 CysD; K00957 sulfate adenylyltransferase subunit 2 [EC:2.7.7.4] [KO:K00957] [EC:2.7.7.4]
adenylyl-sulfate kinase CysC; K00860 adenylylsulfate kinase [EC:2.7.1.25] [KO:K00860] [EC:2.7.1.25]
adenosine-3'(2'); K01082 3'(2'), 5'-bisphosphate nucleotidase [EC:3.1.3.7] [KO:K01082] [EC:3.1.3.7]
phosphoadenosine phosphosulfate reductase; K00390 phosphoadenosine phosphosulfate reductase [EC:1.8.4.8] [KO:K00390] [EC:1.8.4.8]
sulfite reductase flavoprotein alpha-component CysJ; K00380 sulfite reductase (NADPH) flavoprotein alpha-component [EC:1.8.1.2] [KO:K00380] [EC:1.8.1.2]
flavodoxin/nitric oxide synthase CysJ; K00380 sulfite reductase (NADPH) flavoprotein alpha-component [EC:1.8.1.2] [KO:K00380] [EC:1.8.1.2]
sulfite reductase hemoprotein beta-component CysI; K00381 sulfite reductase (NADPH) hemoprotein beta-component [EC:1.8.1.2] [KO:K00381] [EC:1.8.1.2]
3-mercaptopyruvate sulfurtransferase; K01011 thiosulfate/3-mercaptopyruvate sulfurtransferase [EC:2.8.1.1 2.8.1.2] [KO:K01011] [EC:2.8.1.2 2.8.1.1]
thiosulfate sulfurtransferase GlpE; K02439 thiosulfate sulfurtransferase [EC:2.8.1.1] [KO:K02439] [EC:2.8.1.1]
serine acetyltransferase CysE; K00640 serine O-acetyltransferase [EC:2.3.1.30] [KO:K00640] [EC:2.3.1.30]
cysteine synthase A Cys; K01738 cysteine synthase A [EC:2.5.1.47] [KO:K01738] [EC:2.5.1.47]
cysteine synthase 1 Cys11; K01738 cysteine synthase A [EC:2.5.1.47] [KO:K01738] [EC:2.5.1.47]
cysteine synthase B; K12339 cysteine synthase B [EC:2.5.1.47] [KO:K12339] [EC:2.5.1.47]
homoserine O-succinyltransferase MetA; K00651 homoserine O-succinyltransferase [EC:2.3.1.46] [KO:K00651] [EC:2.3.1.46]
cystathionine gamma-synthase; K01739 cystathionine gamma-synthase [EC:2.5.1.48] [KO:K01739] [EC:2.5.1.48]
FAD-dependent pyridine nucleotide-disulfide oxidoreductase; K17218 sulfide:quinone oxidoreductase [EC:1.8.5.-] [KO:K17218] [EC:1.8.5.-]
Compound
C00033  
Acetate
C00042  
Succinate
C00053  
3'-Phosphoadenylyl sulfate
C00054  
Adenosine 3',5'-bisphosphate
C00059  
Sulfate
C00065  
L-Serine
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)propionic acid
C11142  
Dimethyl sulfone
C11143  
Dimethyl sulfoxide
C11145  
Methanesulfonic acid
C15521  
Alkanesulfonate
C19692  
Polysulfide
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)
Reference
  Authors
Fauque GD, Barton LL
  Title
Hemoproteins in dissimilatory sulfate- and sulfur-reducing prokaryotes.
  Journal
Adv Microb Physiol 60:1-90 (2012)
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)
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)
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)
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)
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)
Reference
  Authors
Frigaard NU, Dahl C
  Title
Sulfur metabolism in phototrophic sulfur bacteria.
  Journal
Adv Microb Physiol 54:103-200 (2009)
KO pathway
 

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