A0A061AE05 · PAPSH_CAEEL

  • Protein
    Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase pps-1
  • Gene
    pps-1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Bifunctional enzyme with both ATP sulfurylase and APS kinase activity, which mediates two steps in the sulfate activation pathway (PubMed:16497669).
The first step is the transfer of a sulfate group to ATP to yield adenosine 5'-phosphosulfate (APS), and the second step is the transfer of a phosphate group from ATP to APS yielding 3'-phosphoadenylylsulfate (PAPS: activated sulfate donor used by sulfotransferase) (PubMed:16497669).
Required for normal growth and development (PubMed:16497669).
Involved in several aspects of both embryonic and postembryonic development, including molting, changes in cell shape, and patterning of epithelial and muscle cells (PubMed:16497669).

Catalytic activity

Pathway

Sulfur metabolism; sulfate assimilation.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site66-71ATP 1 (UniProtKB | ChEBI)
Binding site93-96adenosine 5'-phosphosulfate (UniProtKB | ChEBI)
Binding site105adenosine 5'-phosphosulfate (UniProtKB | ChEBI)
Binding site110-113adenosine 5'-phosphosulfate (UniProtKB | ChEBI)
Binding site136-137adenosine 5'-phosphosulfate (UniProtKB | ChEBI)
Binding site175adenosine 5'-phosphosulfate (UniProtKB | ChEBI)
Binding site190-191adenosine 5'-phosphosulfate (UniProtKB | ChEBI)
Binding site218ATP 1 (UniProtKB | ChEBI)
Binding site449-452ATP 2 (UniProtKB | ChEBI)
Binding site550-554ATP 2 (UniProtKB | ChEBI)
Binding site592ATP 2 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentnucleus
Molecular Functionadenylylsulfate kinase activity
Molecular FunctionATP binding
Molecular Functionsulfate adenylyltransferase (ATP) activity
Biological Process3'-phosphoadenosine 5'-phosphosulfate biosynthetic process
Biological Processphosphorylation
Biological Processsulfate assimilation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase pps-1

Including 2 domains:

  • Recommended name
    Sulfate adenylyltransferase
  • EC number
  • Recommended name
    Adenylyl-sulfate kinase
  • EC number

Gene names

    • Name
      pps-1
    • ORF names
      T14G10.1

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • Bristol N2
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Rhabditina > Rhabditomorpha > Rhabditoidea > Rhabditidae > Peloderinae > Caenorhabditis

Accessions

  • Primary accession
    A0A061AE05
  • Secondary accessions
    • Q22501

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Phenotypes & Variants

Disruption phenotype

Lethal phenotype (PubMed:16497669).
Embryos hatch, initiate growth and development, but arrest at the L2 or L3 larval stages (PubMed:16497669).
Abnormal cuticle (PubMed:16497669).
RNAi-mediated knockdown causes a 42% decrease in 3'-phosphoadenosine 5'-phosphosulfate (PAPS) synthesis activity (PubMed:16497669).
Reduced sulfation of disaccharides of heparan sulfate (HS) proteoglycans (PubMed:16497669).
Defects in cell shape of epidermis and patterning of body wall muscle cells (PubMed:16497669).
Some phenotypes only observed when grown at 25 degrees Celsius; such as shortened malformed tail, exacerbated molting defects, blistering, and sterility (PubMed:16497669).

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004571771-654Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase pps-1

Proteomic databases

Expression

Developmental stage

Widely expressed in epidermal cells, gland cells and in amphid sheath cells throughout development, but not in muscle cells and neurons.

Gene expression databases

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region1-26Disordered
Region1-231Adenylyl-sulfate kinase
Region242-653Sulfate adenylyltransferase

Sequence similarities

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

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

A0A061AE05-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    654
  • Mass (Da)
    73,172
  • Last updated
    2014-09-03 v1
  • Checksum
    F5034E4C96E83556
MLTPRDENNEGDAMPMLKKPRYSSLSGQSTNITYQEHTISREERAAAVGRHEGFRGCTIWFTGLSGAGKTTISFALERTLNKLGIPCYGLDGDNIRHGLCKNLGFSKEDRQENIRRVAEVAKLFADSGMICLAAFISPFQEDRLDARKIHESENVKFIEVHVSTTLEVCEQRDPKPSELYKKARAGQILGFTGIDSAYEPPENAEIILDAGKDGVQQCVQKVLDHLESKGLLPEQIPDVPAVRELFVSDDLTVAELLKESQNLPTVELTKVDLQWLQVLAEGWATPLSGFMRERQYLQSMHFGQLLDLKHKVAFVGEKSDDKEDSWPMMDDINQSIPIVLPISDDVKKGLEGVTRIALKYNGQVYAILSDPEIFEHRKDERVCRQFGTNDPRHPAVAQVLESGNWLLGGDVAVVQKIQFNDGLDKYRKTPNELRAIFAEKNADAVFAFQLRNPIHNGHALLMRDTREKLLAEHKNPILLLHPLGGWTKDDDVPLDIRIKQHEAVIAERVLDPEWTVLSIFPSPMMYAGPTEVQWHARSRIAAGIQHYIVGRDPAGIQKPGSPDALYETTHGAKVLSMAPGLSALHILPFRVAAYDKTAKKMSFFDTSRKEDFENISGTKMRGLARNGDTPPEGFMAPTAWEVLAGYYKSLQNSN

A0A061AE05-2

  • Name
    a
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Features

Showing features for alternative sequence.

TypeIDPosition(s)Description
Alternative sequenceVSP_061753176-178in isoform a

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BX284604
EMBL· GenBank· DDBJ
CAA93098.1
EMBL· GenBank· DDBJ
Genomic DNA
BX284604
EMBL· GenBank· DDBJ
CDR32729.1
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