HMM Summary Page: TIGR02034

Functionsulfate adenylyltransferase, large subunit
Gene SymbolcysN
Trusted Cutoff336.10
Domain Trusted Cutoff336.10
Noise Cutoff327.65
Domain Noise Cutoff327.65
Isology Typesubfamily
EC Number2.7.7.4
HMM Length406
Mainrole CategoryCentral intermediary metabolism
Subrole CategorySulfur metabolism
Gene Ontology TermGO:0000103: sulfate assimilation biological_process
GO:0004781: sulfate adenylyltransferase (ATP) activity molecular_function
AuthorBrinkac L
Entry DateOct 22 2003 3:00PM
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]. With members of the Rhizobiaceae family, nodQ often appears as a fusion of cysN (large subunit of ATP sulfurase) and cysC (APS kinase) [2,3].
ReferencesRN [1] RM 2828368 RA Leyh TS, Taylor JC, Markham GD. RT The sulfate activation locus of Escherichia coli K12: cloning, genetic, and enzymatic characterization. RL J Biol Chem. 1988 Feb 15;263(5):2409-16. RN [2] RM 12676676 RA Snoeck C, Verreth C, Hernandez-Lucas I, Martinez-Romero E, Vanderleyden J. RT Identification of a third sulfate activation system in Sinorhizobium sp. strain BR816: the CysDN sulfate activation complex. RL Appl Environ Microbiol. 2003 Apr;69(4):2006-14. RN [3] RM 7961471 RA Schwedock JS, Liu C, Leyh TS, Long SR. RT Rhizobium meliloti NodP and NodQ form a multifunctional sulfate-activating complex requiring GTP for activity. RL J Bacteriol. 1994 Nov;176(22):7055-64. DR PFAM; PF00009; Elongation factor Tu GTP binding domain DR PFAM; PF03144; Elongation factor Tu domain 2 DR EXPERIMENTAL; SP|Q8FEJ1; Escherichia coli; correlation of enzymatic activity, complementation patterns, and polypeptides associated with subclones of cloned DNA DR EXPERIMENTAL; GP|2110525; Xanthomonas oryzae; DR EXPERIMENTAL; GP|24528411; Sinorhizobium sp. BR8160; mutanogenesis measuring growth characteristics and Nod factor sulfation. DR OUTGROUP; SP|P48863; Halobacterium halobium; Elongation factor 1-alpha (EF-1-alpha) (Elongation factor Tu) (EF-Tu). DR HAMAP; MF_00062; 38 of 39
Genome PropertyGenProp0149: sulfate reduction to sulfide, assimilatory (HMM)