A0A2J5Q276 · A0A2J5Q276_9ENTR

  • Protein
    carbamoyl-phosphate synthase (glutamine-hydrolyzing)
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    2/5

Function

Caution

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

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.

Features

Showing features for active site.

133650100150200250300
TypeIDPosition(s)Description
Active site223Nucleophile
Active site307
Active site309

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcarbamoyl-phosphate synthase complex
Molecular FunctionATP binding
Molecular Functioncarbamoyl-phosphate synthase (glutamine-hydrolyzing) activity
Biological Process'de novo' pyrimidine nucleobase biosynthetic process
Biological Process'de novo' UMP biosynthetic process
Biological Processarginine biosynthetic process
Biological Processglutamine metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    carbamoyl-phosphate synthase (glutamine-hydrolyzing)
  • EC number

Gene names

    • ORF names
      CWN49_07890

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • A10
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Klebsiella/Raoultella group > Klebsiella

Accessions

  • Primary accession
    A0A2J5Q276

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain1-87Carbamoyl-phosphate synthase small subunit N-terminal

Sequence similarities

Belongs to the CarA family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    336
  • Mass (Da)
    36,508
  • Last updated
    2018-03-28 v1
  • Checksum
    26EEF96F5EA10B00
SYSRQIVTLTYPHIGNVGTNAADEESSQVHAQGLVIRDLPLIASNFRNTEDLSSYLKRHNIVAIADIDTRKLTRLLREKGAQNGCIIAGDSPDAQLALEKAKAFPGLNGMDLAKEVTTAETYSWTQGSWTLAGDLPEAKAESELPFHVVAYDFGAKRNILRMLVDRGCRLTVVPAKTSAEEVLKMNPDGIFLSNGPGDPAPCDYAIAAIEKFLETDIPVFGICLGHQLLALASGAKTVKMKFGHHGGNHPVKDIDNNVVMITAQNHGFAVDEASMPAHLRVTHKSLFDGTLQGIHRTDKPAFSFQGHPEASPGPHDAAPLFDHFIELIELYRQSAK

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
PIDR01000163
EMBL· GenBank· DDBJ
PLO72429.1
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