A0A2J8BT29 · A0A2J8BT29_VERDA

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 site199sulfate (UniProtKB | ChEBI)
Binding site199-202ATP (UniProtKB | ChEBI)
Active site200
Active site201
Binding site201sulfate (UniProtKB | ChEBI)
Active site202
Site205Transition state stabilizer
Site208Transition state stabilizer
Binding site293-296ATP (UniProtKB | ChEBI)
Binding site297sulfate (UniProtKB | ChEBI)
Site332Induces change in substrate recognition on ATP binding
Binding site335ATP (UniProtKB | ChEBI)
Binding site436-4393'-phosphoadenylyl sulfate (UniProtKB | ChEBI); allosteric inhibitor
Binding site5173'-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

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
      BJF96_g8719
      , VDGE_02457

Organism names

  • Taxonomic identifier
  • Strains
    • 12008
    • Getta Getta
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Glomerellales > Plectosphaerellaceae > Verticillium

Accessions

  • Primary accession
    A0A2J8BT29

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homohexamer. Dimer of trimers.

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-171N-terminal
Domain4-167ATP-sulfurylase PUA-like
Domain175-389Sulphate adenylyltransferase catalytic
Region397-575Allosteric 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
    575
  • Mass (Da)
    64,127
  • Last updated
    2018-03-28 v1
  • Checksum
    EE5C61BFB4088134
MANTPHGGVLKDLFVRDAPRQAELLEESDKLPSLTLTERHLCDLELILNGGFSPLEGFLNEKDYNGVVKENRLADGSLFSMPINLDVSQQTIDEVGIKPGARITLRDLRDDRALAILTVEEVYKPNKNLEAQEVFGSPDDVTHPGIKHLLQVAQEFYVGGKLEAVQRLAHYDFVDLRYTPAELRQHFEKLGWNKVVAFQTRNPMHRAHRELTVRASRSQQANVLIHPVVGLTKPGDIDHFTRVRVYKALLPRYPNGMAALALLPLAMRMGGPREAIWHAIIRKNHGATHFIVGRDHAGPGKNKDGKDWYGAYDAQIAVQKYQEELGIKMVEFQEMIYIPDRDEYQPANEIAPGTHTANISGTELRNRLKTGKEIPAWFSYPEVVKVLREQNPLPAAKGFTIFLTGFQNSGKDQIARALQLILNQGGGRSVSLLLGETVRHELSAELGFSREDRSKNVARIAFVASELTRAGAAVIAAPIAPYEDARSQARELIEKAGPFFLVHVATSLEYSEKTDRRGVYQKARAGEIKGFTGVDDPYEVPAKADLTVDIEKQSVRSAVHQIILLLESQGLLDRI

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MPSH01000039
EMBL· GenBank· DDBJ
PNH27926.1
EMBL· GenBank· DDBJ
Genomic DNA
RSDZ01000157
EMBL· GenBank· DDBJ
RXG41967.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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