A0A9P9LV10 · A0A9P9LV10_9HELO

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 site197sulfate (UniProtKB | ChEBI)
Binding site197-200ATP (UniProtKB | ChEBI)
Active site198
Active site199
Binding site199sulfate (UniProtKB | ChEBI)
Active site200
Site203Transition state stabilizer
Site206Transition state stabilizer
Binding site291-294ATP (UniProtKB | ChEBI)
Binding site295sulfate (UniProtKB | ChEBI)
Site330Induces change in substrate recognition on ATP binding
Binding site333ATP (UniProtKB | ChEBI)
Binding site434-4373'-phosphoadenylyl sulfate (UniProtKB | ChEBI); allosteric inhibitor
Binding site5153'-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 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
      BKA65DRAFT_106197

Organism names

  • Taxonomic identifier
  • Strain
    • MPI-PUGE-AT-0058
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Leotiomycetes > Helotiales > Helotiales incertae sedis > Rhexocercosporidium

Accessions

  • Primary accession
    A0A9P9LV10

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homohexamer. Dimer of trimers.

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-169N-terminal
Domain4-164ATP-sulfurylase PUA-like
Domain174-387Sulphate adenylyltransferase catalytic
Region395-573Allosteric 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.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    573
  • Mass (Da)
    64,297
  • Last updated
    2023-09-13 v1
  • Checksum
    5DCEC670DD4DF895
MANSPHGGELKDLLARDLPRHNELAAEAETLPAVVLSERQLCDLELLLSGGFSPLEGFLNEKDYNGVVENNRLADGNLFSMPITLDVGEQQIKELGIKAGARLTLRDFRDDRNLAIITVDDVYQPDKTKEAKLVFGGDEEHPAVKYLNNTAREFYVGGKIDAIRRLEHYDYVALRYTPAELRLHFDKLGWSKVVAFQTRNPMHRAHRELTVRAARSRQANVLIHPVVGLTKPGDIDHFTRVRVYQALLPRYPNGMAVLGLLPLAMRMGGPREAIWHAIIRKNFGATHFIVGRDHAGPGKNSKGEEFYGPYDAQYAVEKYKDELGIEVVPFQMMTYLPDSDEYRPKDEVPAGIRTLDISGTELRNRLRTGREIPEWFSYPEVVRVLRESHPPRSEQGFTVFLTGYQNSGKDAIARALHVTLNQQGGRSVSLLLGETVRAELSSELGFSRADRTRNIGRIAFVASELTRSRAAVIAAPIAPYEDARQHARELVEKYGDFYLIHVATSLEHAEKTDKRGIYAKARSGEIKGFTGVDDPYETPKKADLTVDLEKTSVRSAVHQIVLLLESQGLLDRL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAGTJL010000017
EMBL· GenBank· DDBJ
KAH7317680.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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