Sulfate adenylyltransferase (P08536)

Identification
NameSulfate adenylyltransferase
Synonyms
  • ATP-sulfurylase
  • Methionine-requiring protein 3
  • Sulfate adenylate transferase
  • SAT
Gene NameMET3
Enzyme Class
Biological Properties
General FunctionInvolved in sulfate adenylyltransferase (ATP) activity
Specific FunctionCatalyzes the first intracellular reaction of sulfate assimilation, forming adenosine-5'-phosphosulfate (APS) from inorganic sulfate and ATP. Plays an important role in sulfate activation as a component of the biosynthesis pathway of sulfur- containing amino acids
Cellular LocationCytoplasm
SMPDB Pathways
Selenocompound metabolismPW002472 ThumbThumb?image type=greyscaleThumb?image type=simple
Sulfur metabolismPW002483 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Purine metabolismec00230 Map00230
Selenocompound metabolismec00450 Map00450
Sulfur metabolismec00920 Map00920
SMPDB ReactionsNot Available
KEGG Reactions
Adenosine triphosphate + hydron + Sulfate → Pyrophosphate + Adenosine phosphosulfate
Metabolites
YMDB IDNameView
YMDB00005SulfateShow
YMDB00109Adenosine triphosphateShow
YMDB00219PyrophosphateShow
YMDB00256Adenosine phosphosulfateShow
YMDB00862hydronShow
GO Classification
Component
Not Available
Function
sulfate adenylyltransferase activity
sulfate adenylyltransferase (ATP) activity
catalytic activity
transferase activity
transferase activity, transferring phosphorus-containing groups
nucleotidyltransferase activity
adenylyltransferase activity
Process
sulfur metabolic process
sulfate assimilation
metabolic process
cellular metabolic process
Gene Properties
Chromosome Locationchromosome 10
LocusYJR010W
Gene Sequence>1536 bp ATGCCTGCTCCTCACGGTGGTATTCTACAAGACTTGATTGCTAGAGATGCGTTAAAGAAG AATGAATTGTTATCTGAAGCGCAATCTTCGGACATTTTAGTATGGAACTTGACTCCTAGA CAACTATGTGATATTGAATTGATTCTAAATGGTGGGTTTTCTCCTCTGACTGGGTTTTTG AACGAAAACGATTACTCCTCTGTTGTTACAGATTCGAGATTAGCAGACGGCACATTGTGG ACCATCCCTATTACATTAGATGTTGATGAAGCATTTGCTAACCAAATTAAACCAGACACA AGAATTGCCCTTTTCCAAGATGATGAAATTCCTATTGCTATACTTACTGTCCAGGATGTT TACAAGCCAAACAAAACTATCGAAGCCGAAAAAGTCTTCAGAGGTGACCCAGAACATCCA GCCATTAGCTATTTATTTAACGTTGCCGGTGATTATTACGTCGGCGGTTCTTTAGAAGCG ATTCAATTACCTCAACATTATGACTATCCAGGTTTGCGTAAGACACCTGCCCAACTAAGA CTTGAATTCCAATCAAGACAATGGGACCGTGTCGTAGCTTTCCAAACTCGTAATCCAATG CATAGAGCCCACAGGGAGTTGACTGTGAGAGCCGCCAGAGAAGCTAATGCTAAGGTGCTG ACCCATCCAGTTGTTGGACTAACCAAACCAGGTGATATAGACCATCACACTCGTGTTCGT GTCTACCAGGAAATTATTAAGCGTTATCCTAATGGTATTGCTTTCTTATCCCTGTTGCCA TTAGCAATGAGAATGAGTGGTGATAGAGAAGCCGTATGGCATGCTATTATTAGAAAGAAT TATGGTGCCTCCCACTTCATTGTTGGTAGAGACCATGCGGGCCCAGGTAAGAACTCCAAG GGTGTTGATTTCTACGGTCCATACGATGCTCAAGAATTGGTCGAATCCTACAAGCATGAA CTGGACATTGAAGTTGTTCCATTCAGAATGGTCACTTATTTGCCAGACGAAGACCGTTAT GCTCCAATTGATCAAATTGACACCACAAAGACGAGAACCTTGAACATTTCAGGTACAGAG TTGAGACGCCGTTTAAGAGTTGGTGGTGAGATTCCTGAATGGTTCTCATATCCTGAAGTG GTTAAAATCCTAAGAGAATCCAACCCACCAAGACCAAAACAAGGTTTTTCAATTGTTTTA GGTAATTCATTAACCGTTTCTCGTGAGCAATTATCCATTGCTTTGTTGTCAACATTCTTG CAATTCGGTGGTGGCAGGTATTACAAGATCTTTGAACACAATAATAAGACAGAGTTACTA TCTTTGATTCAAGATTTCATTGGTTCTGGTAGTGGACTAATTATTCCAAATCAATGGGAA GATGACAAGGACTCTGTTGTTGGCAAGCAAAACGTTTACTTATTAGATACCTCAAGCTCA GCCGATATTCAGCTAGAGTCAGCGGATGAACCTATTTCACATATTGTACAAAAAGTTGTC CTATTCTTGGAAGACAATGGCTTTTTTGTATTTTAA
Protein Properties
Pfam Domain Function
Protein Residues511
Protein Molecular Weight57724.0
Protein Theoretical pI5.62
PDB Fileshow
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Sulfate adenylyltransferase MPAPHGGILQDLIARDALKKNELLSEAQSSDILVWNLTPRQLCDIELILNGGFSPLTGFL NENDYSSVVTDSRLADGTLWTIPITLDVDEAFANQIKPDTRIALFQDDEIPIAILTVQDV YKPNKTIEAEKVFRGDPEHPAISYLFNVAGDYYVGGSLEAIQLPQHYDYPGLRKTPAQLR LEFQSRQWDRVVAFQTRNPMHRAHRELTVRAAREANAKVLIHPVVGLTKPGDIDHHTRVR VYQEIIKRYPNGIAFLSLLPLAMRMSGDREAVWHAIIRKNYGASHFIVGRDHAGPGKNSK GVDFYGPYDAQELVESYKHELDIEVVPFRMVTYLPDEDRYAPIDQIDTTKTRTLNISGTE LRRRLRVGGEIPEWFSYPEVVKILRESNPPRPKQGFSIVLGNSLTVSREQLSIALLSTFL QFGGGRYYKIFEHNNKTELLSLIQDFIGSGSGLIIPNQWEDDKDSVVGKQNVYLLDTSSS ADIQLESADEPISHIVQKVVLFLEDNGFFVF
References
External Links
ResourceLink
Saccharomyces Genome Database MET3
Uniprot IDP08536
Uniprot NameMET3_YEAST
GenBank Gene IDAY723835
Genebank Protein ID51830408
PDB ID
1J70
General Reference
  • Cherest, H., Kerjan, P., Surdin-Kerjan, Y. (1987). "The Saccharomyces cerevisiae MET3 gene: nucleotide sequence and relationship of the 5' non-coding region to that of MET25." Mol Gen Genet 210:307-313.3325778
  • Mountain, H. A., Korch, C. (1991). "TDH2 is linked to MET3 on chromosome X of Saccharomyces cerevisiae." Yeast 7:873-880.1789010
  • Galibert, F., Alexandraki, D., Baur, A., Boles, E., Chalwatzis, N., Chuat, J. C., Coster, F., Cziepluch, C., De Haan, M., Domdey, H., Durand, P., Entian, K. D., Gatius, M., Goffeau, A., Grivell, L. A., Hennemann, A., Herbert, C. J., Heumann, K., Hilger, F., Hollenberg, C. P., Huang, M. E., Jacq, C., Jauniaux, J. C., Katsoulou, C., Karpfinger-Hartl, L., et, a. l. .. (1996). "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X." EMBO J 15:2031-2049.8641269
  • Hu, Y., Rolfs, A., Bhullar, B., Murthy, T. V., Zhu, C., Berger, M. F., Camargo, A. A., Kelley, F., McCarron, S., Jepson, D., Richardson, A., Raphael, J., Moreira, D., Taycher, E., Zuo, D., Mohr, S., Kane, M. F., Williamson, J., Simpson, A., Bulyk, M. L., Harlow, E., Marsischky, G., Kolodner, R. D., LaBaer, J. (2007). "Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Genome Res 17:536-543.17322287
  • Blaiseau, P. L., Thomas, D. (1998). "Multiple transcriptional activation complexes tether the yeast activator Met4 to DNA." EMBO J 17:6327-6336.9799240
  • Huh, W. K., Falvo, J. V., Gerke, L. C., Carroll, A. S., Howson, R. W., Weissman, J. S., O'Shea, E. K. (2003). "Global analysis of protein localization in budding yeast." Nature 425:686-691.14562095
  • Ghaemmaghami, S., Huh, W. K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., Weissman, J. S. (2003). "Global analysis of protein expression in yeast." Nature 425:737-741.14562106
  • Gruhler, A., Olsen, J. V., Mohammed, S., Mortensen, P., Faergeman, N. J., Mann, M., Jensen, O. N. (2005). "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Mol Cell Proteomics 4:310-327.15665377
  • Albuquerque, C. P., Smolka, M. B., Payne, S. H., Bafna, V., Eng, J., Zhou, H. (2008). "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Mol Cell Proteomics 7:1389-1396.18407956
  • Ullrich, T. C., Blaesse, M., Huber, R. (2001). "Crystal structure of ATP sulfurylase from Saccharomyces cerevisiae, a key enzyme in sulfate activation." EMBO J 20:316-329.11157739
  • Lalor, D. J., Schnyder, T., Saridakis, V., Pilloff, D. E., Dong, A., Tang, H., Leyh, T. S., Pai, E. F. (2003). "Structural and functional analysis of a truncated form of Saccharomyces cerevisiae ATP sulfurylase: C-terminal domain essential for oligomer formation but not for activity." Protein Eng 16:1071-1079.14983089