A0A3M7MC51 · A0A3M7MC51_9PLEO

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.

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 site195sulfate (UniProtKB | ChEBI)
Binding site195-198ATP (UniProtKB | ChEBI)
Active site196
Active site197
Binding site197sulfate (UniProtKB | ChEBI)
Active site198
Site201Transition state stabilizer
Site204Transition state stabilizer
Binding site289-292ATP (UniProtKB | ChEBI)
Binding site293sulfate (UniProtKB | ChEBI)
Site328Induces change in substrate recognition on ATP binding
Binding site331ATP (UniProtKB | ChEBI)
Binding site432-4353'-phosphoadenylyl sulfate (UniProtKB | ChEBI); allosteric inhibitor
Binding site5133'-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
      GMOD_00007075

Organism names

  • Taxonomic identifier
  • Strain
    • CCB06
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Dothideomycetes > Pleosporomycetidae > Pleosporales > Pleosporineae > Pleosporaceae > Pyrenophora

Accessions

  • Primary accession
    A0A3M7MC51

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homohexamer. Dimer of trimers.

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-167N-terminal
Domain4-162ATP-sulfurylase PUA-like
Domain172-385Sulphate adenylyltransferase catalytic
Region393-571Allosteric 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
    571
  • Mass (Da)
    63,973
  • Last updated
    2019-02-13 v1
  • MD5 Checksum
    D8C80D9673C03123F1447E548ED59714
MVSGILKDLIARDAPRRKELFDEAEKLPAIVLSERQLCDLELILNGGFSPLEGFMNQKDYDGVVAENRLADGNLFSIPITLDVSQQTIDEVGVKQGARIALRDFRDDRNLAILTVDDVYKPDKEREAREVFDKDGDVAHPAIKYLYETVKDFYVGGKLEAIDRLEHYDYVGLRYTPAELRLHFDKLGWSKVVAFQTRNPMHRAHRELTVRAARARQANVLIHPVVGLTKPGDIDHFTRVRVYQALMPRYPNGMAVLALLPLAMRMAGPREAIWHAIIRKNHGATHFIVGRDHAGPGKNSKGVDFYGPYDAQDAVEKYRSELGIEVVPFLQMTYLPDSDEYKPKNEVEQGVKTLDISGTELRKRLRTGQEIPEWFSYPEVVRVLRESHPPRNQQGFTVFLTGYQNSGKDSIARALNVTLNQQGGRSVSLLLGDTIRSELSSELGFSRSDRDKNIARIAFVASELTKAGAAAIVAPIAPFEDSRKAARQSVEKYGSFYLIHVATPLEHAEKTDKRGIYAKARAGEIKGFTGVDDPYEVPEKADLTVDLSVSNVRTAVHQIVLLLESEGLLTQL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KE747829
EMBL· GenBank· DDBJ
RMZ72081.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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