Warning: The NCBI web site requires JavaScript to function. more...
An official website of the United States government
The .gov means it's official. Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you're on a federal government site.
The site is secure. The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.
sulfate adenylyltransferase subunit CysD
sulfate adenylyltransferase subunit CysD (subunit 2) is the small subunit that with CysN, forms the ATP sulfurylase (ATPS) that catalyzes the conversion of ATP and sulfate to diphosphate and adenylyl sulfate
ATP-sulfurylase
This domain is the catalytic domain of ATP-sulfurylase or sulfate adenylyltransferase EC:2.7.7.4 some of which are part of a bifunctional polypeptide chain associated with adenosyl phosphosulphate (APS) kinase Pfam:PF01583. Both enzymes are required for PAPS (phosphoadenosine-phosphosulfate) synthesis from inorganic sulphate [2]. ATP sulfurylase catalyses the synthesis of adenosine-phosphosulfate APS from ATP and inorganic sulphate [1]. [1]. 9671738. A member of a family of sulfate-activating enzymes causes murine. brachymorphism [published erratum appears in Proc Natl Acad Sci. U S A 1998 Sep 29;95(20):12071]. Kurima K, Warman ML, Krishnan S, Domowicz M, Krueger RC Jr,. Deyrup A, Schwartz NB;. Proc Natl Acad Sci U S A 1998;95:8681-8685.. [2]. 8522184. A multifunctional Urechis caupo protein, PAPS synthetase, has. both ATP sulfurylase and APS kinase activities.. Rosenthal E, Leustek T;. Gene 1995;165:243-248. (from Pfam)
sulfate adenylyltransferase
sulfate adenylyltransferase converts ATP and sulfate to adenosine-5'-phosphosulfate (APS) and pyrophosphate
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase
bifunctional sulfate adenylyltransferase (SAT)/adenylyl-sulfate kinase; SAT catalyzes and couples the energy of GTP hydrolysis to the synthesis of adenosine 5'-phosphosulfate (APS); adenylyl-sulfate kinase catalyzes the ATP-dependent phosphorylation of APS to 3'-phosphoadenosine-5'-phosphosulfate (PAPS)
bifunctional sulfate adenylyltransferase subunit 1/adenylyl-sulfate kinase
bifunctional sulfate adenylyltransferase (SAT) subunit 1/adenylyl-sulfate kinase (CysN/CysC); SAT subunit 1 acts as a regulatory GTPase and is an essential component of ATP sulfurylase that catalyzes and couples the energy of GTP hydrolysis to the synthesis of adenosine 5'-phosphosulfate (APS); adenylyl-sulfate kinase catalyzes the ATP-dependent phosphorylation of APS to 3'-phosphoadenosine-5'-phosphosulfate (PAPS)
sulfate adenylyltransferase subunit 1
sulfate adenylyltransferase subunit 1 similar to CysN, which acts a regulatory GTPase and is an essential component of the ATP sulfurylase, which catalyzes and couples the energy of GTP hydrolysis to the synthesis of adenosine 5'-phosphosulfate (APS)
bifunctional sulfate adenylyltransferase/adenylyl-sulfate kinase NodQ
With CysN catalyzes the formation of adenylylsulfate from sulfate and ATP
sulfate adenylyltransferase subunit CysN
With CysD catalyzes the formation of adenylylsulfate from sulfate and ATP
sulfate adenylyltransferase, small subunit
Metabolic 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].
sulfate adenylyltransferase, large subunit
Metabolic 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].
adenylyl-sulfate kinase
adenylylsulfate kinase catalyzes the ATP-dependent phosphorylation of adenosine 5'-phosphosulfate (APS) to 3'-phosphoadenosine-5'-phosphosulfate (PAPS); it is often found as a fusion protein with sulphate adenylyltransferase. Both enzymes are required for PAPS (phosphoadenosine-phosphosulfate) synthesis from inorganic sulfate
sulfate adenylyltransferase; tryptophan--tRNA ligase
sulfate adenylyltransferase converts ATP and sulfate to adenosine-5'-phosphosulfate (APS) and pyrophosphate; tryptophan--tRNA ligase, a class I tRNA synthetase, aminoacylates the 2'-OH of the nucleotide at the 3' end of the tRNA
Filter your results:
Your browsing activity is empty.
Activity recording is turned off.
Turn recording back on