Q7UMW2 · CYSNC_RHOBA

Function

function

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.
APS kinase catalyzes the synthesis of activated sulfate.

Caution

It is not obvious if the APS kinase domain is functional; there is an Ala-555 replacing the conserved active site Ser. Furthermore R.baltica seems to harbor a bona fide single domain APS kinase (CysC).

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 site481-488ATP (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 Processsulfate assimilation
Biological Processsulfur compound metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Bifunctional enzyme CysN/CysC

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

Gene names

    • Name
      cysNC
    • Synonyms
      cysC, cysN
    • Ordered locus names
      RB7941

Organism names

Accessions

  • Primary accession
    Q7UMW2

Proteomes

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00002390801-647Bifunctional enzyme CysN/CysC

Interaction

Subunit

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

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-472Sulfate adenylyltransferase
Domain22-239tr-type G
Region31-38G1
Region89-93G2
Region110-113G3
Region165-168G4
Region204-206G5
Region473-614Adenylyl-sulfate kinase

Sequence similarities

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    647
  • Mass (Da)
    71,170
  • Last updated
    2003-10-01 v1
  • Checksum
    59113B3A36831A31
MSHQSDLIATDIDAYLKQHEQKQLLRFITCGSVDDGKSTLIGRLLYDSKLVYEDELAKVQSDSVRQGSVAGGFDPSLFMDGLKEEREQGITIDVAYRYFSTAKRKFIIADTPGHEQYTRNMATGASSADLAIILIDARHGVLTQTRRHSFIVSLLGIRHVVVAVNKMDIDGVDYSEDRFNEICDDYRSFATRLDLPDLHFIPISALNGDNLVDRSENMPWYTGSTLMNFLETVYIGSDRNLQDFRLPVQLVNRPNLNFRGFCGTIASGIIRKGEEITVLPSRQKSKVKEIVTYDGNLDEAYAPLAVTLTLEDEIDASRGDMIVRSGNLPRSESDVEAMLVWMNEEAMVPGKTYLVKHSTQTVPGNVETLAYKVDVNDLHRMPAPTLELNEIGRVRLSLSAPIHHDPYRRNRTTGAIILVDRITNATVAAGMILDRGTTGSHKSVWDDEVSTDDSSDALSTVTTEERAARFGQKPATVLLTGLTGSGKTSIARAVERKLFDAGRSVAVVDGEFVRRGLSRDLGFSADDRSENLRRSGHLAHTLNDAGLICLASLVAPSDDVRQKVGKLIGEDQFLVVHVATPLDVCRERDTKGQYAKADAGELSNFPGVTAKYDVPTNPDLAVDASTTSIAECADAVVELLKLKGFIK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BX294146
EMBL· GenBank· DDBJ
CAD75662.1
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.
FeedbackHelp