HMM Summary Page: TIGR02039

Functionsulfate adenylyltransferase, small subunit
Gene SymbolcysD
Trusted Cutoff396.60
Domain Trusted Cutoff396.60
Noise Cutoff213.25
Domain Noise Cutoff213.25
Isology Typesubfamily
EC Number2.7.7.4
HMM Length294
Mainrole CategoryCentral intermediary metabolism
Subrole CategorySulfur metabolism
Gene Ontology TermGO:0000103: sulfate assimilation biological_process
GO:0000103: sulfate assimilation biological_process
GO:0004781: sulfate adenylyltransferase (ATP) activity molecular_function
GO:0004781: sulfate adenylyltransferase (ATP) activity molecular_function
AuthorBrinkac L
Entry DateOct 27 2003 1:45PM
Last ModifiedFeb 14 2011 3:27PM
CommentMetabolic assimilation of sulfur from inorganic sulfate, requires sulfate activation by coupling to a nucleoside, for the production of high-energy nucleoside phosphosulfates. This pathway appears to be similar in all prokaryotic organisms. Activation is first achieved through sulfation of sulfate with ATP by sulfate adenylyltransferase (ATP sulfurylase) to produce 5'-phosphosulfate (APS), coupled by GTP hydrolysis. Subsequently, APS is phosphorylated by an APS kinase to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS) [1]. In Escherichia coli, ATP sulfurylase is a heterodimer composed of two subunits encoded by cysD and cysN, with APS kinase encoded by cysC. These genes are located in a unidirectionally transcribed gene cluster, and have been shown to be required for the synthesis of sulfur-containing amino acids [1]. Homologous to this E.coli activation pathway are nodPQH gene products found among members of the Rhizobiaceae family. These gene products have been shown to exhibit ATP sulfurase and APS kinase activity, yet are involved in Nod factor sulfation, and sulfation of other macromolecules [2].
ReferencesRN [1] RM 2828368 RT The sulfate activation locus of Escherichia coli K12: cloning, genetic, and enzymatic characterization. RA Leyh TS, Taylor JC, Markham GD. RJ J Biol Chem. 1988 Feb 15;263(5):2409-16. RN [2] RM 12676676 RT Identification of a third sulfate activation system in Sinorhizobium sp. strain BR816: the CysDN sulfate activation complex. RA Snoeck C, Verreth C, Hernandez-Lucas I, Martinez-Romero E,Vanderleyden J. RL Appl Environ Microbiol. 2003 Apr;69(4):2006-14. DR EXPERIMENTAL; SP|P21156; Escherichia coli; correlation of enzymatic activity, complementation patterns, and polypeptides associated with subclones of cloned DNA. DR EXPERIMENTAL; SP|P52995; Rhizobium tropici; site-directed mutagenesis demonstrated inability to synthesize sulfated Nod factors by high-pressure liquid chromatography and thin-layer chromatography assays. DR EXPERIMENTAL; GP|5911360; Sinorhizobium meliloti; mutanogenesis measuring growth characteristics and Nod factor sulfation. DR EXPERIMETNAL; SP|P28603; Azospirillum brasilense; deletion and mutational analysis. DR PFAM; PF01507; Phosphoadenosine phosphosulfate reductase family DR OURGROUP; GP|22553030; Physcomitrella patens; phosphoadenosine-phosphosulphate reductase DR HAMAP; MF_00064; 145 of 151
Genome PropertyGenProp0149: sulfate reduction to sulfide, assimilatory (HMM)
GenProp0149: sulfate reduction to sulfide, assimilatory (HMM)