A0A2Z5UBX1 · A0A2Z5UBX1_9SPHN

  • Protein
    Multifunctional fusion protein
  • Gene
    cysN
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

Function

function

APS kinase catalyzes the synthesis of activated sulfate.
Catalyzes the synthesis of activated sulfate.
Proposed to provide activated sulfate for transfer to Nod factor. ATP sulfurylase may be the GTPase, regulating ATP sulfurylase activity.
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.

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 site35-42GTP (UniProtKB | ChEBI)
Binding site114-118GTP (UniProtKB | ChEBI)
Binding site169-172GTP (UniProtKB | ChEBI)
Binding site472-479ATP (UniProtKB | ChEBI)
Active site546Phosphoserine intermediate

GO annotations

AspectTerm
Molecular Functionadenylylsulfate kinase activity
Molecular FunctionATP binding
Molecular FunctionGTP binding
Molecular FunctionGTPase activity
Molecular Functionguanosine tetraphosphate binding
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
      cysN
    • Synonyms
      cysC
    • ORF names
      SPYCW_1601

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • EG6
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Sphingomonadales > Sphingomonadaceae > Sphingopyxis

Accessions

  • Primary accession
    A0A2Z5UBX1

Proteomes

PTM/Processing

Keywords

Interaction

Subunit

Heterodimer composed of CysD, the smaller subunit, and CysN.
Sulfate-activating enzymes, NodP and NodQ, may be physically associated.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain26-240Tr-type G

Sequence similarities

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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    633
  • Mass (Da)
    69,676
  • Last updated
    2018-10-10 v1
  • Checksum
    B387D45037FF7654
MTDPIYVTDALIAEDIDAYLAGHEKKSLLRFITCGSVDDGKSTLIGRLLYDSKMIFEDQLAALEADSKRVGTQGQEIDFALLVDGLAAEREQGITIDVAYRFFTTEKRKFIVADTPGHEQYTRNMVTGASTADLAVILIDARKGVLTQTRRHSFLAHLIGIKHIVLAVNKMDLVGYDKTVFERILLSYRAFASEIGITNFTAIPISGFKGDNITALSDNMPWFKGPALIEHLENVEIGAAADEAKPFRLPVQWVNRPNLDFRGFSGQLASGTVRPGDAVRILPSGKTTTVDRIVTLDGDLEEAVAGQSVTLTLADEVDCSRGDVIAASDAPPEAADQFEATLVWMADEAMIAGRAYWLKLATQTVSATIQQPKYEINVNTLDHLAAKTLDLNGIGVVEISTDKPIVFEAYGDNRTLGGFILIDKLTNATVAAGMLHFSLRRAQNVHWQASDVDRDMRANLKNQRPALLWFTGLSGSGKSTIANLVEKKLHRMNRHSFLLDGDNVRHGLNRDLGFTEADRIENIRRVGEVAKLMTDAGLIVITAFISPFRAEREMVRAMLPEGEFIEVFIDTPLAEAERRDVKGLYKKARAGQLKNFTGIDSPYEAPENPEIRIDTTAMTPEEAADLIIDRLLG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP017603
EMBL· GenBank· DDBJ
BBB08585.1
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