A0A9P5T5L0 · A0A9P5T5L0_9FUNG

  • Protein
    Sulfate adenylyltransferase
  • Gene
    MET3
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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 site198sulfate (UniProtKB | ChEBI)
Binding site198-201ATP (UniProtKB | ChEBI)
Active site199
Active site200
Binding site200sulfate (UniProtKB | ChEBI)
Active site201
Site204Transition state stabilizer
Site207Transition state stabilizer
Binding site292-295ATP (UniProtKB | ChEBI)
Binding site296sulfate (UniProtKB | ChEBI)
Site331Induces change in substrate recognition on ATP binding
Binding site334ATP (UniProtKB | ChEBI)
Binding site435-4383'-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
      BGX34_012239

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • NVP85
  • Taxonomic lineage
    Eukaryota > Fungi > Fungi incertae sedis > Mucoromycota > Mortierellomycotina > Mortierellomycetes > Mortierellales > Mortierellaceae > Mortierella

Accessions

  • Primary accession
    A0A9P5T5L0

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homohexamer. Dimer of trimers.

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-170N-terminal
Domain4-165ATP-sulfurylase PUA-like
Domain174-388Sulphate adenylyltransferase catalytic
Region396-574Allosteric 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 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
    574
  • Mass (Da)
    64,265
  • Last updated
    2023-09-13 v1
  • Checksum
    10673F4E10620D2A
MANTPHGGILKDLVARDLPIRDQLLKEAETVPSIVLTERQLCDLELIISGGFSPLEGFLNQKDYNNVVENLRLANGTLWSIPINLDVAQEDIDTLSLKPAQRVALRDPRNDSPIAILTIEDIYKPDKVKEAKLVFGDDDLAHPSVKYIHQNVKDFYVGGSVQAIQPPTHYDYVAYRNTPAEIRAYFQKLNWTRVVAFQTRNPMHRAHRELTVRAARSRQANVLINPVVGLTKPGDIDHFTRVRVYEAIIRRYPTGMAALSLLPLAMRMAGPREALWHAIIRKNHGCSHFIIGRDHAGPGKNSAGKDFYGPYDAQYLVEKYKDEIDIEVVPFQQVTYLPDSDEYVPSNEVPAGAKTLDISGTELRRRLRTGAHIPEWFSYPEVVALLRQSHPPRSKQGFTVFLTGYHASKKEHIARALQVSLNQQGGRSISLLLGETIRGKLSSELGFSKRERDININRLGFVSAELTKAGAGVIVAPIAPYEDARQQARQEIEKVGGFFLIHVATPLEQCIAWDRDGIYERAKKGEITGFTGIDDPYETPKNADLVVDPSTESVAQIVRRIVLLLDKQGYFGDA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAAAVA010000998
EMBL· GenBank· DDBJ
KAF9352256.1
EMBL· GenBank· DDBJ
Genomic DNA

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.
FeedbackHelp