A0A258TU43 · A0A258TU43_9PROT

  • Protein
    Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme
  • Gene
    glnE
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal transduction protein PII (GlnB) which indicates the nitrogen status of the cell.

Caution

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

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Function[glutamate-ammonia-ligase] adenylyltransferase activity
Molecular Function[glutamine synthetase]-adenylyl-L-tyrosine phosphorylase activity
Molecular FunctionATP binding
Molecular Functionmagnesium ion binding
Biological Processregulation of glutamine family amino acid metabolic process

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme
  • Alternative names
    • ATP:glutamine synthetase adenylyltransferase
    • ATase

Including 2 domains:

  • Recommended name
    Glutamine synthetase adenylyl-L-tyrosine phosphorylase
  • EC number
  • Alternative names
    • Adenylyl removase
      (AR
      ; AT-N
      )
  • Recommended name
    Glutamine synthetase adenylyl transferase
  • EC number
  • Alternative names
    • Adenylyl transferase
      (AT
      ; AT-C
      )

Gene names

    • Name
      glnE
    • ORF names
      B7Y41_05195

Organism names

Accessions

  • Primary accession
    A0A258TU43

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-428Adenylyl removase
Domain16-250Glutamate-ammonia ligase adenylyltransferase repeated
Domain285-424PII-uridylyltransferase/Glutamine-synthetase adenylyltransferase
Region437-922Adenylyl transferase
Domain535-775Glutamate-ammonia ligase adenylyltransferase repeated
Domain793-887PII-uridylyltransferase/Glutamine-synthetase adenylyltransferase

Sequence similarities

Belongs to the GlnE family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    922
  • Mass (Da)
    102,077
  • Last updated
    2017-12-20 v1
  • Checksum
    A4AA35B64685881A
MTPAPDQTAPEPELAIARAAAYSRWLNGRLAARPELADWLATASASPVSRSDMLDFLATGIASEDDLKRQLRRLRERVFARVMTRDLNGLADLSEVTRTLTELAEVSVACALDFHHRDLAAIHGEPLDSTGQPQQLIVVGMGKLGGGELNASSDIDLIFVYPEDGETHGGVGNTRKIDNFEFFTRVGKRLINAIGDNTGDGYVFRVDMRLRPYGDSGPLVSSFAMLEDYFYTQAREWERYAWIKGRAITGFPIAGAPERIAELEKLRTPFVFRKYLDFGAFGSMRELHAQIRREVMRRDKADNIKLGPGGIREIEFIAQVFQLIRGGQQASLQMRPTRTLLHQLAAYNLMPEAQTTELEAAYVFLRNLEHRLQYLDDAQTQMLPTGDADRQRVAEAMGFADWAGLLARLDPMRRKVSGQFEQVFGAPQEDQSGHPLAGLCEAPEDEALARLARVGYGDPAAALNQLLALRQGNRYNSLPASNKAMLDGLLPPLIEVAASFPNAADTLTRILDLLEAIARRGPYLALLKEYPQTLRQVARIASSSPWAAQYLTRQPHLLDELLDSRQLMAPPDWPRARQELGLRLAGMVLPNAHADVERQMDELRHFKQSETFRLLAQDLSGMWTLEKLSDHLSDLADLLVGATLELVWNSLTGKHRAAPTPPAFAVIAYGKLGGKELGYASDLDIVFLYDDPHLDAQEVYAKLGKRLNTWMGTLTSAGILYETDLRLRPDGAAGLLVSSVEAFEDYQLHHAWTWEHQALTRARFCCGDPAVGERFGAIRDNVLRQARDTDKLRAEVKEMRQKMHAGHPNTSGMFDIKHDAGGLVDVEFAMQYLVLAHAAQHPEMCANIGNIALLKRAGELGLLPMEIALAAADAYRELRRRQHAAKLRGGGAAGDQARAEHGGLSQEIQAVKALWGDVFGAA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
NCGJ01000003
EMBL· GenBank· DDBJ
OYY94955.1
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