A0A166NK20 · A0A166NK20_9HYPO

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.

TypeIDPosition(s)Description
Binding site221sulfate (UniProtKB | ChEBI)
Binding site221-224ATP (UniProtKB | ChEBI)
Active site222
Active site223
Binding site223sulfate (UniProtKB | ChEBI)
Active site224
Site227Transition state stabilizer
Site230Transition state stabilizer
Binding site315-318ATP (UniProtKB | ChEBI)
Binding site319sulfate (UniProtKB | ChEBI)
Site354Induces change in substrate recognition on ATP binding
Binding site357ATP (UniProtKB | ChEBI)
Binding site458-4613'-phosphoadenylyl sulfate (UniProtKB | ChEBI); allosteric inhibitor
Binding site5403'-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
      AAL_07206

Organism names

  • Taxonomic identifier
  • Strain
    • RCEF 2490
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Hypocreales > Clavicipitaceae > Moelleriella

Accessions

  • Primary accession
    A0A166NK20

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homohexamer. Dimer of trimers.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-193N-terminal
Domain4-57ATP-sulfurylase PUA-like
Domain80-189ATP-sulfurylase PUA-like
Domain198-411Sulphate adenylyltransferase catalytic
Region419-598Allosteric 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
    598
  • Mass (Da)
    67,229
  • Last updated
    2016-07-06 v1
  • Checksum
    B00A8366FAB03D31
MANPPHGGVLKDLFARDLPRQAELLEESAKYPAIVLTDRHLCDLELILNGGFSPLQGEASRPLQLHHEPLTDASGFRRAGFMTQKDYNGVVEKNRLADGTLFSMPITLDVDQKQIEALGIKPGAKLTLRDSRDDRNLAIFTVDDVYRPDKTKEAKEVFGSDDDTHPGIKHLFSVAKDFYVGGQLEAVNRLEHYDFLDLRFTPAELRSHFNKLGWQKVVAFQTRNPMHRAHRELTVRAARSQQANVLIHPVVGMTKPGDIDHFTRVRVYKALLPRYPNGMAALALLPLAMRMGGPREALWHAIIRKNHGATHFIVGRDHAGPGKNKHGKDHYGPYDAQTLVQQYQEELGIKMVEFQEMIYIPDKDEYMPANEIPEGTRTMNISGTELRNRLRTGKEIPEWFSYPEVVRVLREQNPLPREKGFTVFLTGYQNCGKDQVARALQATLNQGGGRPVSMLLGETVRSELSSELGFSRQDRDLNISRIAFVASELTKAGAAVIAAPIAPFDQARIQARELIEKSGGPFFLVHVATPLEYCEKTDRRGIYRRARAGEIKGFTGVDDPYETPSRPDLTVDLSQQNVRSIVHEVILLLESRGLLDRV

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AZGY01000021
EMBL· GenBank· DDBJ
KZZ90520.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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