I4YGQ7 · I4YGQ7_WALMC

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.

TypeIDPosition(s)Description
Binding site200sulfate (UniProtKB | ChEBI)
Binding site200-203ATP (UniProtKB | ChEBI)
Active site201
Active site202
Binding site202sulfate (UniProtKB | ChEBI)
Active site203
Site206Transition state stabilizer
Site209Transition state stabilizer
Binding site294-297ATP (UniProtKB | ChEBI)
Binding site298sulfate (UniProtKB | ChEBI)
Site333Induces change in substrate recognition on ATP binding
Binding site336ATP (UniProtKB | ChEBI)
Binding site437-4403'-phosphoadenylyl sulfate (UniProtKB | ChEBI); allosteric inhibitor
Binding site5213'-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
      WALSEDRAFT_59459

Organism names

Accessions

  • Primary accession
    I4YGQ7

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
Region1-172N-terminal
Domain5-167ATP-sulfurylase PUA-like
Domain178-390Sulphate adenylyltransferase catalytic
Region398-576Allosteric 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
    576
  • Mass (Da)
    64,322
  • Last updated
    2012-09-05 v1
  • Checksum
    A980947E9DA9ED7C
MSNPCHGNVLKDLHVRDADKHDALVAESETLPSVSLTERQLCDLELIMNGGFSPLEGFMNKKDYEGVVENMRLTDGLVFTIPVTLDLSSEKIKELGLSESSRVTLRDPRDENPLAIITIEDIWQPNKENEAAKVFGAGENDLAHPAIAYLHNNVKDSYVGGKVQAVNPPLHYDYVAQRFTPAELRSHFKKLAWRKVVAFQTRNPMHRAHRELTVRAARQRQANVLIHPVVGLTKPGDVDHFTRVRVYQSIMPKYPNGMAQLALLPLAMRMAGPREAVWHAIIRKNFGTTHFIVGRDHAGPGKNSHGKDFYGPYDAQELVTSFKDELKIEMVPFQMMTYLPETDEYQPVDEVPQGTPTANISGTELRRRLKTGAHIPDWFSYDSVVKTLRESYPPRLQQGFTIMLTGLWNSGKDQIAKALQVKLNEQGGRSVSLLLGETVRQELSTELGFSREDRHKNLQRIAFVSAELSRAGAAVIASPIAPIEESRKQARKTVETTGGAGNFFLIHVATPLDICEKTDRRGVYAKARKGEIKNFTGVSDDYEEPKDADLTVDVAQQPISEIVHSIVLLLEGEGLV

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JH668225
EMBL· GenBank· DDBJ
EIM23149.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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