Sulfate adenylyltransferase subunit 1 (P23845)

Identification
Name:Sulfate adenylyltransferase subunit 1
Synonyms:
  • ATP-sulfurylase large subunit
  • Sulfate adenylate transferase
  • SAT
Gene Name:cysN
Enzyme Class:
Biological Properties
General Function:Involved in GTPase activity
Specific Function:May be the GTPase, regulating ATP sulfurylase activity
Cellular Location:Cytoplasmic
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Sulfate ↔ 1.0Pyrophosphate + 1.0Adenosine phosphosulfate
ReactionCard
1.0Thumb+1.0Selenate ↔ 1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Selenate ↔ 1.0Pyrophosphate + 1.0Adenylylselenate
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb+1.0Sulfate+1.0Thumb → 1.0Thumb+1.0Pyrophosphate
1.0Adenosine triphosphate + 1.0Hydrogen ion + 1.0Sulfate + 1.0Sulfate → 1.0Adenosine phosphosulfate + 1.0Pyrophosphate
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Sulfate ↔ 1.0Pyrophosphate + 1.0Adenosine phosphosulfate
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Guanosine triphosphate + 1.0Water + 1.0Sulfate → 1.0Adenosine phosphosulfate + 1.0Guanosine diphosphate + 1.0Phosphate + 1.0Pyrophosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB01003Adenosine phosphosulfateMetaboCard
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB21003AdenylylselenateMetaboCard
ECMDB01201Guanosine diphosphateMetaboCard
ECMDB01273Guanosine triphosphateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB04142PyrophosphateMetaboCard
ECMDB23788SelenateMetaboCard
ECMDB01448SulfateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
binding
catalytic activity
GTP binding
GTPase activity
guanyl nucleotide binding
guanyl ribonucleotide binding
hydrolase activity
hydrolase activity, acting on acid anhydrides
hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
nucleoside-triphosphatase activity
nucleotide binding
purine nucleotide binding
pyrophosphatase activity
transferase activity
transferase activity, transferring phosphorus-containing groups
Gene Properties
Blattner:b2751
Gene OrientationCounterclockwise
Centisome Percentage:61.90
Left Sequence End2872014
Right Sequence End2873441
Gene Sequence:
>1428 bp
ATGTCGATCAAAACCAGTAATACAGATTTTAAGACACGCATCCGTCAGCAAATTGAAGAT
CCGATCATGCGCAAAGCGGTGGCAAACGCGCAGCAGCGTATTGGGGCAAATCGGCAAAAA
ATGGTCGATGAATTGGGGCACTGGGAGGAGTGGCGCGATCGGGCCGCCCAGATACGTGAT
CATGTTCTGAGTAATCTCGACGCTTATCTGTACCAGCTCTCAGAAAAAGTGACGCAAAAC
GGCGGTCACGTCTATTTTGCAAGAACCAAAGAAGACGCTACCCGCTACATTTTACAGGTT
GCCCAACGCAAAAATGCCCGGAAGGTGGTGAAATCTAAATCGATGGTGACCGAAGAGATT
GGTGTCAATCATGTGTTGCAGGATGCTGGCATTCAGGTGATTGAAACCGATCTGGGTGAA
TATATTCTCCAGCTGGATCAAGATCCGCCATCTCATGTTGTGGTCCCGGCAATTCATAAA
GATCGCCATCAGATCCGTCGAGTGCTACACGAACGTCTGGGCTATGAGGGGCCGGAAACG
CCTGAAGCGATGACCTTATTCATCCGGCAAAAAATCCGCGAAGATTTCCTCAGTGCTGAA
ATAGGTATTACCGGCTGTAATTTCGCGGTGGCAGAGACCGGTTCGGTATGCCTGGTGACC
AATGAAGGTAATGCGCGAATGTGTACCACGCTGCCTAAAACGCATATTGCAGTGATGGGA
ATGGAGCGTATTGCCCCCACGTTTGCCGAGGTAGATGTATTGATCACCATGCTGGCGCGC
AGTGCCGTTGGTGCACGTTTGACGGGATACAACACCTGGCTGACAGGACCGCGCGAAGCT
GGGCACGTTGATGGTCCTGAAGAGTTTCATCTGGTTATTGTCGATAACGGGCGTTCTGAG
GTGCTGGCCTCTGAATTTCGGGATGTGCTGCGCTGTATTCGCTGCGGGGCTTGTATGAAT
ACTTGTCCGGCATATCGCCATATTGGCGGTCATGGATATGGCTCTATTTATCCAGGGCCA
ATTGGTGCGGTGATTTCTCCGCTACTTGGCGGCTATAAAGATTTTAAAGATTTACCCTAC
GCCTGCTCTTTATGCACAGCTTGTGACAACGTGTGTCCGGTGCGTATTCCGCTGTCAAAA
CTGATTTTGCGTCATCGTCGGGTGATGGCTGAAAAAGGGATCACCGCAAAAGCAGAGCAA
CGGGCGATAAAAATGTTCGCTTATGCCAATAGTCATCCAGGATTGTGGAAAGTCGGGATG
ATGGCCGGTGCTCATGCGGCAAGCTGGTTTATCAATGGCGGCAAAACACCACTCAAATTT
GGCGCGATTAGCGACTGGATGGAAGCACGCGATCTTCCTGAAGCTGACGGAGAGAGTTTC
CGTAGTTGGTTTAAGAAACATCAGGCGCAGGAGAAAAAGAATGGATAA
Protein Properties
Pfam Domain Function:
Protein Residues:475
Protein Molecular Weight:52558
Protein Theoretical pI:5
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Sulfate adenylyltransferase subunit 1
MNTALAQQIANEGGVEAWMIAQQHKSLLRFLTCGSVDDGKSTLIGRLLHDTRQIYEDQLS
SLHNDSKRHGTQGEKLDLALLVDGLQAEREQGITIDVAYRYFSTEKRKFIIADTPGHEQY
TRNMATGASTCELAILLIDARKGVLDQTRRHSFISTLLGIKHLVVAINKMDLVDYSEETF
TRIREDYLTFAGQLPGNLDIRFVPLSALEGDNVASQSESMPWYSGPTLLEVLETVEIQRV
VDAQPMRFPVQYVNRPNLDFRGYAGTLASGRVEVGQRVKVLPSGVESNVARIVTFDGDRE
EAFAGEAITLVLTDEIDISRGDLLLAADEALPAVQSASVDVVWMAEQPLSPGQSYDIKIA
GKKTRARVDGIRYQVDINNLTQREVENLPLNGIGLVDLTFDEPLVLDRYQQNPVTGGLIF
IDRLSNVTVGAGMVHEPVSQATAAPSEFSAFELELNALVRRHFPHWGARDLLGDK
References
External Links:
ResourceLink
Uniprot ID:P23845
Uniprot Name:CYSN_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674451
Ecogene ID:EG10194
Ecocyc:EG10194
ColiBase:b2751
Kegg Gene:b2751
EchoBASE ID:EB0191
CCDB:CYSN_ECOLI
BacMap:16130658
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