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A0A0L0N0U0 · A0A0L0N0U0_TOLOC

Function

function

Catalyzes 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.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Activity regulation

Allosterically inhibited by 3'-phosphoadenosine 5'-phosphosulfate (PAPS).

Pathway

Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 1/3.

Features

Showing features for binding site, active site, site.

Type
IDPosition(s)Description
Binding site202sulfate (UniProtKB | ChEBI)
Binding site202-205ATP (UniProtKB | ChEBI)
Active site203
Active site204
Binding site204sulfate (UniProtKB | ChEBI)
Active site205
Site208Transition state stabilizer
Site211Transition state stabilizer
Binding site296-299ATP (UniProtKB | ChEBI)
Binding site300sulfate (UniProtKB | ChEBI)
Site335Induces change in substrate recognition on ATP binding
Binding site338ATP (UniProtKB | ChEBI)
Binding site439-4423'-phosphoadenylyl sulfate (UniProtKB | ChEBI); allosteric inhibitor
Binding site5203'-phosphoadenylyl sulfate (UniProtKB | ChEBI); allosteric inhibitor

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionadenylylsulfate kinase activity
Molecular FunctionATP binding
Molecular Functionsulfate adenylyltransferase (ATP) activity
Biological Processcysteine biosynthetic process
Biological Processhydrogen sulfide biosynthetic process
Biological Processmethionine biosynthetic process
Biological Processsulfate assimilation via adenylyl sulfate reduction
Biological Processsulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin)

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Sulfate adenylyltransferase
  • EC number
  • Alternative names
    • ATP-sulfurylase
    • Sulfate adenylate transferase
      (SAT
      )

Gene names

    • Name
      MET3
    • ORF names
      TOPH_07955

Organism names

Accessions

  • Primary accession
    A0A0L0N0U0

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homohexamer. Dimer of trimers.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-174N-terminal
Domain4-170ATP-sulfurylase PUA-like
Domain179-392Sulphate adenylyltransferase catalytic
Region294-313Disordered
Region400-578Allosteric regulation domain; adenylyl-sulfate kinase-like

Domain

The adenylyl-sulfate kinase (APS kinase) is non-functional. It is involved in allosteric regulation by PAPS. PAPS binding induces a large rotational rearrangement of domains lowering the substrate affinity of the enzyme.

Sequence similarities

In the C-terminal section; belongs to the APS kinase family.
In the N-terminal section; belongs to the sulfate adenylyltransferase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    578
  • Mass (Da)
    64,993
  • Last updated
    2015-11-11 v1
  • MD5 Checksum
    90860E26F0B630303CF1E2F5FAE02D83
MANTPHGGVLKDLFARDLPRHAELRDESEKLPALVLTERHLCDLELILNGGFSPLEGFMIEKDYNGVVDNNRLADGALFSMPITLDVDQGQLDHLGIKAGARITLRDSRDDRNLAILAVEDVYRPDNTSNRVKEAKEVFGSDDDTHPGVKHLFNTAKEFYVGGKLEAINRLEHYDFLDLRFTPAELRSHFNKLGWQKVVAFQTRNPMHRAHRELTVRAARSQQANVLIHPVVGMTKPGDIDHFTRVRVYKALLARYPNGMAALALLPLAMRMGGPREALWHAVIRKNHGATHFIVGRDHAGPGKNKNGKDHYGPYDAQELVQKYQDELGIKMVEFQEMIYIPDKDEYMPANEIPEGTRTMNISGTELRNRLKTGKEIPEWFSYPEVVKVLREQNPLPREKGFTVFMTGYQNSGKDQIARALQTTLNQGGGRPVSMLVGETVRHELSSELGFSRQDRDLNISRIAFVASELTKAGAAVIAAPIAPFDDARKQARELIEKSGSFFLIHVATPLEYCEKTDRRGIYQAARAGKIKGFTGVDDPYEAPHKPDLVVDLEKQNVRSIVHEIILLLXSRGLLDRL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LFRF01000037
EMBL· GenBank· DDBJ
KND87405.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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