A0A517LY00 · A0A517LY00_9BACT

  • Protein
    Multifunctional fusion protein
  • Gene
    cysNC
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    5/5

Function

function

APS kinase catalyzes the synthesis of activated sulfate.
Catalyzes the synthesis of activated sulfate.
With CysD forms the ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric-sulfuric acid anhydride bond driven by GTP hydrolysis by CysN coupled to ATP hydrolysis by CysD.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Catalytic activity

Pathway

Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 1/3.
Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site31-38GTP (UniProtKB | ChEBI)
Binding site110-114GTP (UniProtKB | ChEBI)
Binding site165-168GTP (UniProtKB | ChEBI)
Binding site483-490ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Functionadenylylsulfate kinase activity
Molecular FunctionATP binding
Molecular FunctionGTP binding
Molecular FunctionGTPase activity
Molecular Functionsulfate adenylyltransferase (ATP) activity
Biological Processhydrogen sulfide biosynthetic process
Biological Processphosphorylation
Biological Processsulfate assimilation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Multifunctional fusion protein

Including 2 domains:

  • Recommended name
    Sulfate adenylyltransferase subunit 1
  • EC number
  • Alternative names
    • ATP-sulfurylase large subunit
    • Sulfate adenylate transferase
      (SAT
      )
  • Recommended name
    Adenylyl-sulfate kinase
  • EC number
  • Alternative names
    • APS kinase
    • ATP adenosine-5'-phosphosulfate 3'-phosphotransferase
    • Adenosine-5'-phosphosulfate kinase

Gene names

    • Name
      cysNC
    • Synonyms
      cysC
      , cysN
    • ORF names
      EC9_16760

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • EC9
  • Taxonomic lineage
    Bacteria > Planctomycetota > Planctomycetia > Pirellulales > Pirellulaceae > Rosistilla

Accessions

  • Primary accession
    A0A517LY00

Proteomes

PTM/Processing

Keywords

Interaction

Subunit

Heterodimer composed of CysD, the smaller subunit, and CysN.

Family & Domains

Features

Showing features for domain, region, compositional bias.

Type
IDPosition(s)Description
Domain22-237Tr-type G
Region447-471Disordered
Compositional bias453-467Polar residues

Sequence similarities

Belongs to the APS kinase family.
In the C-terminal section; belongs to the APS kinase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    649
  • Mass (Da)
    71,480
  • Last updated
    2019-10-16 v1
  • Checksum
    9F8CBC69ED2D50FB
MSHQSDLISTDINAYLKQHEQKQLLRFITCGSVDDGKSTLIGRLLFDSKMLYEDELAKMEADSKTQGAAGGEFDPALATDGLKEEREQGITIDVAYRYFSTARRKFIIADTPGHEQYTRNMATGASSADLAVILIDARHGVMTQTKRHSFIVSLLGIRHVVVAINKMDLVDFSEEKYNEICADYKSFAVRLDLPDLHFIPLSALNGDNVVEPSPNTPWYRGSTLMNFLESVYIGSDRNLQDFRFPVQWVNRPNLDFRGFCGTIASGIIRQGDEVMIMPSRKTTKVKEIVTHDGNLEEAFASQSVTLTLADEVDCSRGDMIVRPGNVPQTADAIEAILVWMSASPMVPGKTYVVKHATQTVTGAIETLRYQIDVNTVHRTLSPQLNLNEIGRCRLSLNESICFDAYRNNRATGALILIDRLTNETVAAGMILDRSSSGKSQAIWEEDLAESTGEEDSSGQLSQVSSEEREARYGQKPATVLLTGLTCSGKTTIARAVERRLFDSGRSVSVLDGQQVRRGLSKDLGYSFEDRSENLRRAAYSAHLVNDSGLICIASFVAPNASVRDKVASVIGKERFLTIHVDAPIDVCRSRDTTGQYADADAGKLQDFPGVSAPYEAPEAADLTLNTDTQSIDACVDAVIDLLKQRGFIR

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias453-467Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP036261
EMBL· GenBank· DDBJ
QDS87497.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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