| Identification |
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| Name: | Adenylyl-sulfate kinase |
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| Synonyms: | - APS kinase
- ATP adenosine-5'-phosphosulfate 3'-phosphotransferase
- Adenosine-5'-phosphosulfate kinase
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| Gene Name: | cysC |
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| Enzyme Class: | |
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| Biological Properties |
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| General Function: | Involved in adenylylsulfate kinase activity |
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| Specific Function: | Catalyzes the synthesis of activated sulfate |
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| Cellular Location: | Not Available |
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| SMPDB Pathways: | - Sulfur metabolism PW000922
- cysteine biosynthesis PW000800
- sulfur metabolism (butanesulfonate) PW000923
- sulfur metabolism (ethanesulfonate) PW000925
- sulfur metabolism (isethionate) PW000926
- sulfur metabolism (methanesulfonate) PW000927
- sulfur metabolism (propanesulfonate) PW000924
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| KEGG Pathways: | |
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| KEGG Reactions: | |
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| SMPDB Reactions: | |
1.0 | + | 1.0 | → | 1.0 | + | 1.0Adenosine diphosphate | + | 1.0 | + | 1.0 |
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| EcoCyc Reactions: | |
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| Complex Reactions: | |
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| Metabolites: | |
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| GO Classification: | | Function |
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| adenyl nucleotide binding | | adenyl ribonucleotide binding | | ATP binding | | binding | | catalytic activity | | kinase activity | | nucleoside binding | | purine nucleoside binding | | transferase activity | | transferase activity, transferring phosphorus-containing groups | | Process |
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| cellular metabolic process | | metabolic process | | sulfate assimilation | | sulfur metabolic process |
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| Gene Properties |
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| Blattner: | b2750 |
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| Gene Orientation | Counterclockwise |
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| Centisome Percentage: | 61.89 |
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| Left Sequence End | 2871409 |
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| Right Sequence End | 2872014 |
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| Gene Sequence: | >606 bp
ATGAGTATAAAAAATCTACCTGCCGACTATTTATTGGCTGCACAACAGGGTGATATCGAT
AAAGTAAAAACCTGCCTTGCGCTGGGTGTCGATATTAATACCTGCGATCGTCAGGGGAAA
ACGGCAATTACGCTGGCAAGTTTATATCAGCAATATGCTTGCGTTCAGGCATTAATTGAT
GCCGGAGCGGATATTAATAAGCAAGATCATACCTGTTTAAATCCTTTTTTAATTAGCTGT
CTGAACGATGATTTAACGCTACTACGAATTATTTTACCGGCTAAACCCGATCTTAATTGC
GTAACCCGTTTTGGCGGTGTCGGCCTGACGCCTGCCTGTGAAAAAGGCCATTTAAGTATT
GTAAAAGAGCTTTTGGCGCATACGGAGATTAACGTTAACCAGACCAACCATGTAGGCTGG
ACGCCGCTACTGGAAGCGATTGTGCTTAATGATGGTGGTATTAAACAGCAGGCGATTGTG
CAGTTATTGCTGGAACACGGTGCCAGCCCGCATCTGACCGATAAATATGGCAAAACGCCA
CTGGAACTGGCGCGGGAACGGGGCTTTGAAGAGATTGCGCAGTTACTGATTGCCGCAGGT
GCATAA |
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| Protein Properties |
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| Pfam Domain Function: | |
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| Protein Residues: | 201 |
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| Protein Molecular Weight: | 22321 |
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| Protein Theoretical pI: | 6 |
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| Signaling Regions: | |
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| Transmembrane Regions: | |
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| Protein Sequence: | >Adenylyl-sulfate kinase
MALHDENVVWHSHPVTVQQRELHHGHRGVVLWFTGLSGSGKSTVAGALEEALHKLGVSTY
LLDGDNVRHGLCSDLGFSDADRKENIRRVGEVANLMVEAGLVVLTAFISPHRAERQMVRE
RVGEGRFIEVFVDTPLAICEARDPKGLYKKARAGELRNFTGIDSVYEAPESAEIHLNGEQ
LVTNLVQQLLDLLRQNDIIRS |
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| References |
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| External Links: | |
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| General Reference: | - Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
- Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
- Leyh, T. S., Taylor, J. C., Markham, G. D. (1988). "The sulfate activation locus of Escherichia coli K12: cloning, genetic, and enzymatic characterization." J Biol Chem 263:2409-2416. Pubmed: 2828368
- Leyh, T. S., Vogt, T. F., Suo, Y. (1992). "The DNA sequence of the sulfate activation locus from Escherichia coli K-12." J Biol Chem 267:10405-10410. Pubmed: 1316900
- Satishchandran, C., Hickman, Y. N., Markham, G. D. (1992). "Characterization of the phosphorylated enzyme intermediate formed in the adenosine 5'-phosphosulfate kinase reaction." Biochemistry 31:11684-11688. Pubmed: 1332767
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