A0A255E5D9 · A0A255E5D9_9ACTN

Function

function

Large subunit of the glutamine-dependent carbamoyl phosphate synthetase (CPSase). CPSase catalyzes the formation of carbamoyl phosphate from the ammonia moiety of glutamine, carbonate, and phosphate donated by ATP, constituting the first step of 2 biosynthetic pathways, one leading to arginine and/or urea and the other to pyrimidine nucleotides. The large subunit (synthetase) binds the substrates ammonia (free or transferred from glutamine from the small subunit), hydrogencarbonate and ATP and carries out an ATP-coupled ligase reaction, activating hydrogencarbonate by forming carboxy phosphate which reacts with ammonia to form carbamoyl phosphate.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
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 )

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Note: Binds 4 Mg2+ or Mn2+ ions per subunit.

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.
Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site129ATP 1 (UniProtKB | ChEBI)
Binding site173ATP 1 (UniProtKB | ChEBI)
Binding site179ATP 1 (UniProtKB | ChEBI)
Binding site180ATP 1 (UniProtKB | ChEBI)
Binding site212ATP 1 (UniProtKB | ChEBI)
Binding site214ATP 1 (UniProtKB | ChEBI)
Binding site219ATP 1 (UniProtKB | ChEBI)
Binding site245ATP 1 (UniProtKB | ChEBI)
Binding site246ATP 1 (UniProtKB | ChEBI)
Binding site247ATP 1 (UniProtKB | ChEBI)
Binding site289ATP 1 (UniProtKB | ChEBI)
Binding site289Mg2+ 1 (UniProtKB | ChEBI)
Binding site289Mn2+ 1 (UniProtKB | ChEBI)
Binding site303ATP 1 (UniProtKB | ChEBI)
Binding site303Mg2+ 1 (UniProtKB | ChEBI)
Binding site303Mg2+ 2 (UniProtKB | ChEBI)
Binding site303Mn2+ 1 (UniProtKB | ChEBI)
Binding site303Mn2+ 2 (UniProtKB | ChEBI)
Binding site305Mg2+ 2 (UniProtKB | ChEBI)
Binding site305Mn2+ 2 (UniProtKB | ChEBI)
Binding site716ATP 2 (UniProtKB | ChEBI)
Binding site755ATP 2 (UniProtKB | ChEBI)
Binding site757ATP 2 (UniProtKB | ChEBI)
Binding site762ATP 2 (UniProtKB | ChEBI)
Binding site787ATP 2 (UniProtKB | ChEBI)
Binding site788ATP 2 (UniProtKB | ChEBI)
Binding site789ATP 2 (UniProtKB | ChEBI)
Binding site790ATP 2 (UniProtKB | ChEBI)
Binding site830ATP 2 (UniProtKB | ChEBI)
Binding site830Mg2+ 3 (UniProtKB | ChEBI)
Binding site830Mn2+ 3 (UniProtKB | ChEBI)
Binding site842ATP 2 (UniProtKB | ChEBI)
Binding site842Mg2+ 4 (UniProtKB | ChEBI)
Binding site842Mg2+ 3 (UniProtKB | ChEBI)
Binding site842Mn2+ 4 (UniProtKB | ChEBI)
Binding site842Mn2+ 3 (UniProtKB | ChEBI)
Binding site844Mg2+ 4 (UniProtKB | ChEBI)
Binding site844Mn2+ 4 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctionATP binding
Molecular Functioncarbamoyl-phosphate synthase (ammonia) activity
Molecular Functioncarbamoyl-phosphate synthase (glutamine-hydrolyzing) activity
Molecular Functionmetal ion binding
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 large chain
  • EC number
  • Alternative names
    • Carbamoyl phosphate synthetase ammonia chain

Gene names

    • Name
      carB
    • ORF names
      CGZ92_09215

Organism names

  • Taxonomic identifier
  • Strain
    • NML 160184
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Propionibacteriales > Propionibacteriaceae > Parenemella

Accessions

  • Primary accession
    A0A255E5D9

Proteomes

Subcellular Location

Interaction

Subunit

Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate. Tetramer of heterodimers (alpha,beta)4.

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-406Carboxyphosphate synthetic domain
Domain133-332ATP-grasp
Domain680-871ATP-grasp
Domain953-1113MGS-like
Region953-1115Allosteric domain
Region1086-1115Disordered

Domain

The large subunit is composed of 2 ATP-grasp domains that are involved in binding the 2 ATP molecules needed for carbamoyl phosphate synthesis. The N-terminal ATP-grasp domain (referred to as the carboxyphosphate synthetic component) catalyzes the ATP-dependent phosphorylation of hydrogencarbonate to carboxyphosphate and the subsequent nucleophilic attack by ammonia to form a carbamate intermediate. The C-terminal ATP-grasp domain (referred to as the carbamoyl phosphate synthetic component) then catalyzes the phosphorylation of carbamate with the second ATP to form the end product carbamoyl phosphate. The reactive and unstable enzyme intermediates are sequentially channeled from one active site to the next through the interior of the protein over a distance of at least 96 A.

Sequence similarities

Belongs to the CarB family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,115
  • Mass (Da)
    119,237
  • Last updated
    2017-12-20 v1
  • Checksum
    4C15A71C91F9FF2B
MPRRTDIESILVIGSGPIVIGQACEFDYSGTQACRVLKEQGFRVILVNSNPATIMTDPEFADATYVEPITPEFVEHVIAKERPDALLATLGGQTALNAAVALHDNGVLAKYGVELIGASVPAIQRGENREEFKEIVQKLTVPGAYGVAESRICNTIDEVVAAAEELSYPVVVRPSFTMGGVGSGFAHNEAELRRIAGVGLSASPVTEVLIEESILGWKEYELEVMRDKADNVVIICSIENFDPMGVHTGDSITVAPAMTLTDREFQLMRDVAIGVIREVGVETGGCNIQFAINPDDGRMVVIEMNPRVSRSSALASKATGFPIAKIAAMVAIGYTLDEIPNDITEKTPAAFEPTLDYVVVKVPRFAFEKFPSADTTLTTHMKSVGEAMAIGRNFPEALGKALRSMENTHAAFNFAPGDEDLAALLSEIERPTDGRLQKVMRAIVAGATAEQIHEATSIDPWFIDQLVLIHATARAVADAPQLTADLLVEAKRIGLSDEQIGTLRQLGPNVVREVRAALGVRPVYKTVDTCAAEFEARTPYHYSTYDQETEVTPREKPAVLILGSGPNRIGQGIEFDYSCVHAAMTLSEAGYETVMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEVYHAELAAGPVAGVIVQLGGQTPLKLAQALKDAGVPIVGTSPEAIDLAEERGAFGRVLQEAGLPAPKHGTAVSYPEASAIANEIGFPVLVRPSYVLGGRGMEIVYDDASLADYIANATEISADHPVLVDRFLDDAVEIDVDALYDGNELYLGAVMEHIEEAGIHSGDSACTLPPITLGDADIERIRTSTEAIAAGVGVQGLINIQYALASDVLYVLEANPRASRTVPFVSKATATPLAKAAARIMLGASIAELRGEGVLKATGDGADVGSQAPIAVKEAVMPFNRFRTPEGDSVDTVLGPEMRSTGEVMGISPSFGMAFAKSQAAAGTKLPTEGKVFVSAANRDKRHVVFPVKRLADLGYQILATEGTASVLGRYGVDVEVVRKHSQGEGPDGEPTIVQMIHDDQVALIFNTPHGTSRHGRPRFDGWEIRTAATLREVPLCTTVPGLVAAVQAIEARALQGRAEQTQGEPEEHPVRSLQDWAPLLRGEQA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
NMVI01000018
EMBL· GenBank· DDBJ
OYN86510.1
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