A0A1Y2CVM9 · A0A1Y2CVM9_9FUNG

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 site189sulfate (UniProtKB | ChEBI)
Binding site189-192ATP (UniProtKB | ChEBI)
Active site190
Active site191
Binding site191sulfate (UniProtKB | ChEBI)
Active site192
Site195Transition state stabilizer
Site198Transition state stabilizer
Binding site271-274ATP (UniProtKB | ChEBI)
Binding site275sulfate (UniProtKB | ChEBI)
Site310Induces change in substrate recognition on ATP binding
Binding site313ATP (UniProtKB | ChEBI)
Binding site414-4173'-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
      BCR33DRAFT_713004

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • JEL800
  • Taxonomic lineage
    Eukaryota > Fungi > Fungi incertae sedis > Chytridiomycota > Chytridiomycota incertae sedis > Chytridiomycetes > Chytridiales > Chytriomycetaceae > Rhizoclosmatium

Accessions

  • Primary accession
    A0A1Y2CVM9

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
Region1-161N-terminal
Domain4-158ATP-sulfurylase PUA-like
Domain166-367Sulphate adenylyltransferase catalytic
Region375-553Allosteric 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
    553
  • Mass (Da)
    61,818
  • Last updated
    2017-08-30 v1
  • Checksum
    D4CEC4FF8F2C87E8
MSNPPHGGVLKDLIARDAPRQASLKLAAAGLPSITLTERNICDLELILNGGFSPLEGFLNQRDYESVVSNMRLADGSLWPMPINLDVSQEQINSLGLKSGARVALRDPIDDSALAILTIEDIYQPDKHREAVFVFGDDDLAHPAVDYLHKQIKAFYLSAHYDYVENRYTPSELRAHFKKLNWSRVVAFQTRNPMHRAHRELTVRAARDRQCNVLIHPVVGMTKPGDIDHYTRVREWHPLLLPLAMRMAGPREALWHAIIRKNYGCTHFIVGRDHAGPGKNSKGVDFYGPYDAQDLVAKYKDELHIEVVPFQMVAYVPDTDEYIPQDELPAGTKTLNISGTELRRRLKTGAAIPDWFTYPDVQTILRSQNPPRSKQGFTVLLTGYWNSGASIIAEALQVVLNQDGQRPTTLLKGETIRSELSKELGFTKKDRDANIKRIAFVAGEVTKCGGAVICSPIAPYESARQEAKKTISEQGGFFLVHVATPLEYCIANDRTGTYAKAQRGEIKGFTGIDDPYEVPTNPNLRVDASIHPVSQIVHEIILLLEKEGYIGER

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MCGO01000006
EMBL· GenBank· DDBJ
ORY51081.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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