Sat

• Description: sulfate adenylyltransferase
  
  

Gene name	sat
Synonyms	ylnB
Essential	no
Product	sulfate adenylyltransferase
Function	sulfate activation
Gene expression levels in SubtiExpress: sat
Metabolic function and regulation of this protein in SubtiPathways: sat
MW, pI	42 kDa, 5.646
Gene length, protein length	1146 bp, 382 aa
Immediate neighbours	cysP, cysC
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

sulfur metabolism, most abundant proteins

This gene is a member of the following regulons

CymR regulon, S-box

The gene

Basic information

• Locus tag: BSU15590

Database entries

• BsubCyc: BSU15590

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: ATP + sulfate = diphosphate + adenylyl sulfate (according to Swiss-Prot)

• Protein family: sulfate adenylyltransferase family (according to Swiss-Prot)

• Paralogous protein(s): YitA

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactors:

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• BsubCyc: BSU15590

• Structure:

• UniProt: O34764

• KEGG entry: [3]

• E.C. number: 2.7.7.4

Expression and regulation

• Operon: cysH-cysP-sat-cysC-ylnD-ylnE-ylnF PubMed

• Expression browser: sat PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • repressed by casamino acids PubMed
  • repressed in the presence of cysteine (CymR)
  • induced by methionine starvation (S-box) PubMed

• Regulatory mechanism:
  • S-box: transcription termination/ antitermination, the S-box riboswitch binds S-adenosylmethionine resulting in termination PubMed
  • CymR: transcription repression

• Additional information:
  • belongs to the 100 most abundant proteins PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

Labs working on this gene/protein

Isabelle Martin-Verstraete, Institute Pasteur, Paris, France