A0A2H9SGB5 · A0A2H9SGB5_9GAMM

  • Protein
    Carbamoyl phosphate synthase large chain
  • Gene
    carB
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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 site169ATP 1 (UniProtKB | ChEBI)
Binding site175ATP 1 (UniProtKB | ChEBI)
Binding site176ATP 1 (UniProtKB | ChEBI)
Binding site208ATP 1 (UniProtKB | ChEBI)
Binding site210ATP 1 (UniProtKB | ChEBI)
Binding site215ATP 1 (UniProtKB | ChEBI)
Binding site241ATP 1 (UniProtKB | ChEBI)
Binding site242ATP 1 (UniProtKB | ChEBI)
Binding site243ATP 1 (UniProtKB | ChEBI)
Binding site285ATP 1 (UniProtKB | ChEBI)
Binding site285Mg2+ 1 (UniProtKB | ChEBI)
Binding site285Mn2+ 1 (UniProtKB | ChEBI)
Binding site299ATP 1 (UniProtKB | ChEBI)
Binding site299Mg2+ 2 (UniProtKB | ChEBI)
Binding site299Mg2+ 1 (UniProtKB | ChEBI)
Binding site299Mn2+ 2 (UniProtKB | ChEBI)
Binding site299Mn2+ 1 (UniProtKB | ChEBI)
Binding site301Mg2+ 2 (UniProtKB | ChEBI)
Binding site301Mn2+ 2 (UniProtKB | ChEBI)
Binding site712ATP 2 (UniProtKB | ChEBI)
Binding site751ATP 2 (UniProtKB | ChEBI)
Binding site753ATP 2 (UniProtKB | ChEBI)
Binding site758ATP 2 (UniProtKB | ChEBI)
Binding site783ATP 2 (UniProtKB | ChEBI)
Binding site784ATP 2 (UniProtKB | ChEBI)
Binding site785ATP 2 (UniProtKB | ChEBI)
Binding site786ATP 2 (UniProtKB | ChEBI)
Binding site826ATP 2 (UniProtKB | ChEBI)
Binding site826Mg2+ 3 (UniProtKB | ChEBI)
Binding site826Mn2+ 3 (UniProtKB | ChEBI)
Binding site838ATP 2 (UniProtKB | ChEBI)
Binding site838Mg2+ 3 (UniProtKB | ChEBI)
Binding site838Mg2+ 4 (UniProtKB | ChEBI)
Binding site838Mn2+ 3 (UniProtKB | ChEBI)
Binding site838Mn2+ 4 (UniProtKB | ChEBI)
Binding site840Mg2+ 4 (UniProtKB | ChEBI)
Binding site840Mn2+ 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
      CK424_04040

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • BC.3.72
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Legionellales > Legionellaceae > Legionella

Accessions

  • Primary accession
    A0A2H9SGB5

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
Region1-403Carboxyphosphate synthetic domain
Domain133-328ATP-grasp
Domain676-867ATP-grasp
Domain935-1079MGS-like
Region935-1079Allosteric domain

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
    1,079
  • Mass (Da)
    118,946
  • Last updated
    2018-02-28 v1
  • Checksum
    13A306C3BD61B2E6
MPKRTDIQSILILGAGPIVIGQACEFDYSGTQAVRALKREGYRVILINSNPATIMTDPELADATYIEPVLWPEVAAVIKKERPDALLPTMGGQTALNCALDLVREGVLEAYGVELIGASEDAIDKAENRDKFRTLMQEIGLDMPRSMIAHSLDEAMVALGVLGFPAIIRPSFTMGGTGGGIAYNLEEFESICLRGLDLSPTRELLIDESVLGWKEYEMEVVRDRHDNCIIVCSIENLDPMGVHTGDSITVAPAQTLTDKEYQRMRDAAIKVLRAVGVDTGGSNVQFAVNPEDGRLLVVEMNPRVSRSSALASKATGFPIAKIAALLAVGYTLDELKNDITDGKTPASFEPTLDYVVTKMPRFNFDKFPQTSKTLTTQMKSVGEVMAIGANFQESLQKAIRGLEIDRYGLHPLFADQEMSVLRGYLQEPTPDRLWYIADAFRLGMSLEEIHKESRVDPWFLAQIQELVAFEELVLGKTLEHLDEKTLRLLKQRGFSDVYLARLLGCHEREVRQHRLSLGIKPVYQRIDSCAAEFSSDTAYLYSCYQSVCESRPDFSRPKIMILGGGPNRIGQGIEFDYCCVHAAFALRDAGYETIMVNCNPETVSTDVETTDRLYFDPVTLEDVLAVYDLEKPIGVIVDYGGQTPLKLAQELANHGVPILGTSPDAIDEAEDRERFQQLVTRLGLHQPANGTVRSESEAIALAQRIGYPLVVRPSYVLGGRAMEIVYHETDLRRYLEHAVRVSNDSPVLLDKFLEDAIEVDIDAVCDGEDVLIGAIMEHIEQAGIHSGDSACTLPPFSLSVVVQQDLKEQLQLMAKALHVVGLVNAQFAIQGDDIYVLEVNPRASRTVPFVSKATGLPLAKIAARCKVGLSLKQQGLLHIQQVPGFYSVKLPVFPFIKFSGVDSILGPEMKSTGEVMGIAKRFGQAYAKAQRGAGCDIVNRRRAFLSVRDTDKSRIGEIAKRLIALGFDIVATRGTTAVIQAAGIACERVFKVAEGRPHVVDHIKNHEIDFIVNTTEGKQAIADSFDIRRSALQYKVSYTTTLSGAEAACLAMKYEERDTVTRLQDLHERFSYAKTSNDG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
PEQK01000012
EMBL· GenBank· DDBJ
PJD92759.1
EMBL· GenBank· DDBJ
Genomic DNA

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