Essential maintenance is planned to begin on Fri Jan 24 2025. The website may be temporarily unavailable. Please use our fallback: https://wwwdev.ebi.ac.uk/uniprot/front-end/fallback/ in case of any outage.

A1D858 · MET3_NEOFI

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.

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 site4513'-phosphoadenylyl sulfate (UniProtKB | ChEBI); allosteric inhibitor
Binding site477-4783'-phosphoadenylyl sulfate (UniProtKB | ChEBI); allosteric inhibitor
Binding site5163'-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
      NFIA_070730

Organism names

Accessions

  • Primary accession
    A1D858

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00002836891-574Sulfate adenylyltransferase

Interaction

Subunit

Homohexamer. Dimer of trimers.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region1-169N-terminal
Region170-394Catalytic
Region395-574Allosteric 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 N-terminal section; belongs to the sulfate adenylyltransferase family.
In the C-terminal section; belongs to the APS kinase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    574
  • Mass (Da)
    64,275
  • Last updated
    2007-01-23 v1
  • MD5 Checksum
    1050C90A88ACC4214B320AD240D3B95B
MANPPHGGVLKDLLARDAPRHDELEIEAEQLPAIVLTERQLCDLELIMNGGFSPLEGFMNQKDYDSVCENVRLADGNLFSMPITLDVSQAVIDDGKLKPGSRVTLRDFRDDRNLAILTIDDIYRPDKAKEAKLVFGGDEEHPAIKYLYNKVQEFYVGGKIEAINKLNHYDYVALRYTPAELRVHFDKLGWNRVVAFQTRNPMHRAHRELTVRAARARQANVLIHPVVGLTKPGDIDHFTRVRAYQALLPRYPNGMAVLGLLGLAMRMGGPREAIWHAIIRKNHGATHFIVGRDHAGPGKNSKGQEFYGPYDAQHAVEKYREELGIEVVEFQQVTYLPDTDEYKPKDEVPAGVKTLDISGTELRNRLRTGAPIPEWFSYPEVVKILRESSPPRHTQGFTIFLTGYMNSGKDAIARALQVTLNQQGGRSVSLLLGDTVRHELSSELGFSREDRHTNIQRIAFVAGELTRAGAAVIASPIAPYEESRNAARDAVTQAGGNFFLVHVATPLEYCEKTDKRGIYAKARRGEIKGFTGVDDPYETPSKADLTVDVSKQTVRSIVHEIILMLETEGFFDRS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DS027690
EMBL· GenBank· DDBJ
EAW21902.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help