A0A1Q4HNU2 · A0A1Q4HNU2_9MYCO

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

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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, active site.

TypeIDPosition(s)Description
Binding site14-21GTP (UniProtKB | ChEBI)
Binding site91-95GTP (UniProtKB | ChEBI)
Binding site146-149GTP (UniProtKB | ChEBI)
Binding site452-459ATP (UniProtKB | ChEBI)
Active site526Phosphoserine intermediate

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 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
      cysN
    • Synonyms
      cysC
    • ORF names
      BRW65_23335

Organism names

  • Taxonomic identifier
  • Strain
    • M11
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycobacterium

Accessions

  • Primary accession
    A0A1Q4HNU2

Proteomes

PTM/Processing

Keywords

Interaction

Subunit

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

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain5-220Tr-type G

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
    616
  • Mass (Da)
    67,711
  • Last updated
    2017-04-12 v1
  • Checksum
    90337E80586D65D4
MATPTTLLRLATAGSVDDGKSTLIGRLLYDSKAVMEDQWAAVEQTSKERGHDYTDLALVTDGLRAEREQGITIDVAYRYFATPKRKFIIADTPGHIQYTRNMVTGASTAQLVIVLVDARHGLLEQSRRHAFLASLLGIQHIVLAVNKMDLIGWDREKFEAIRDEFHAFAARLDVHDVATIPMSALHGDNVVTKSDQTPWYEGPALLSHLEEVYIAGDRNLVDVRFPVQYVIRPHTREHQDHRSYAGTVASGVMRPGDEVVVLPIGKTTRITAIDGPNGPVEEAFPPMAVSISLADEIDISRGDLIARSNNHPRVTQEFDATVCWMADDATLEPGRDYVIKHTTRTTRARVTGLDYRLDVNTLHRDKTATALQLNELGRISLRTQVPLLLDEYTRNASTGSFILIDPHTNGTVAAGMVLRDVSAQTASPNTVRHRSSAPAEARPRGKTVWFTGLSGSGKSSVAMLVEQKLLEKGVAAYVLDGDNLRHGLNADLGFSMADRAENLRRLAHVATLLADSGNVVLVPAISPLHEQREMARNVHAAAGFDFVEVFCDTPIEECEQRDPKGLYAKARAGEIAHFTGIDSPYQPPANPDLRLTPELSVEEQAQSIIDLLESRA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MPNT01000028
EMBL· GenBank· DDBJ
OJZ69288.1
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