A0A517ZVC8 · A0A517ZVC8_9PLAN

  • 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.

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 site148ATP 1 (UniProtKB | ChEBI)
Binding site188ATP 1 (UniProtKB | ChEBI)
Binding site194ATP 1 (UniProtKB | ChEBI)
Binding site195ATP 1 (UniProtKB | ChEBI)
Binding site227ATP 1 (UniProtKB | ChEBI)
Binding site229ATP 1 (UniProtKB | ChEBI)
Binding site234ATP 1 (UniProtKB | ChEBI)
Binding site260ATP 1 (UniProtKB | ChEBI)
Binding site261ATP 1 (UniProtKB | ChEBI)
Binding site262ATP 1 (UniProtKB | ChEBI)
Binding site304ATP 1 (UniProtKB | ChEBI)
Binding site304Mg2+ 1 (UniProtKB | ChEBI)
Binding site304Mn2+ 1 (UniProtKB | ChEBI)
Binding site318ATP 1 (UniProtKB | ChEBI)
Binding site318Mg2+ 2 (UniProtKB | ChEBI)
Binding site318Mg2+ 1 (UniProtKB | ChEBI)
Binding site318Mn2+ 1 (UniProtKB | ChEBI)
Binding site318Mn2+ 2 (UniProtKB | ChEBI)
Binding site320Mg2+ 2 (UniProtKB | ChEBI)
Binding site320Mn2+ 2 (UniProtKB | ChEBI)
Binding site739ATP 2 (UniProtKB | ChEBI)
Binding site778ATP 2 (UniProtKB | ChEBI)
Binding site780ATP 2 (UniProtKB | ChEBI)
Binding site785ATP 2 (UniProtKB | ChEBI)
Binding site810ATP 2 (UniProtKB | ChEBI)
Binding site811ATP 2 (UniProtKB | ChEBI)
Binding site812ATP 2 (UniProtKB | ChEBI)
Binding site813ATP 2 (UniProtKB | ChEBI)
Binding site853ATP 2 (UniProtKB | ChEBI)
Binding site853Mg2+ 3 (UniProtKB | ChEBI)
Binding site853Mn2+ 3 (UniProtKB | ChEBI)
Binding site869ATP 2 (UniProtKB | ChEBI)
Binding site869Mg2+ 4 (UniProtKB | ChEBI)
Binding site869Mg2+ 3 (UniProtKB | ChEBI)
Binding site869Mn2+ 4 (UniProtKB | ChEBI)
Binding site869Mn2+ 3 (UniProtKB | ChEBI)
Binding site871Mg2+ 4 (UniProtKB | ChEBI)
Binding site871Mn2+ 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
      Mal52_49310

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • Mal52
  • Taxonomic lineage
    Bacteria > Planctomycetota > Planctomycetia > Planctomycetales > Planctomycetaceae > Symmachiella

Accessions

  • Primary accession
    A0A517ZVC8

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, compositional bias.

TypeIDPosition(s)Description
Region1-421Carboxyphosphate synthetic domain
Domain152-347ATP-grasp
Domain703-898ATP-grasp
Domain965-1107MGS-like
Region965-1113Allosteric domain
Region1090-1113Disordered
Compositional bias1098-1113Polar residues

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
    1,113
  • Mass (Da)
    121,830
  • Last updated
    2019-10-16 v1
  • Checksum
    9077715739B0CF55
MVMVVDSDCNPARLEGTTDVPRRDDIHKILIIGSGPIVIGQACEFDYSGTQACKALREEGYEVVLVNSNPATIMTDPDTAHRTYVEPITWEYVQKIIEVERPDALLPTLGGQTGLNTAMDLARRGILEQLGCQLIGAKEDVIAKAEGRQTFKDAMVEIGLDVPISETVHNMEEARAALKVVGLPTVIRPSYTLGGVGGGIAYNRDEFDAMVQKGIDLSPVGEVLLEESIIGWKEYEMEVMRDKNDNVVIICAIENFDAMGVHTGDSITVAPAQTLTDKEYQRMRDATISIMREIGVETGGSNVQFAINPENGRMIVIEMNPRVSRSSALASKATGFPIAKIAAKLAVGYTLDEIPNDITRETLACFEPTIDYVVTKIPRWTFEKFPEADAVLTTQMKSVGETMAIGRTFKESLQKAVRGLETGHFGLGGGKNDLWGTSEQPADDEIQRKLATPNDERLYYIRYAFKAGMSLEHVHELTRIDPWFLDNILELTEIEAELRQVTRLEDVDDSLLLKAKRHGFSDRQLSFWWAASEMDIRQHRKERGVVATFKQVDTCAAEFEAYTPYYYSTYESEDETPAKQSDKKRVMILGGGPNRIGQGIEFDYCCCQASFALRELGIESIMVNSNPETVSTDYDTSDILFFEPLTTEDVLNICDRMQPDGVIVQFGGQTPLNLARGLEAAGVTIIGTSPVMIDAAEDREKFQGILEQLGLRQPPNGIATNVEGARQAAERIGYPILVRPSYVLGGRAMEICYDEPSLVKYMTEAVDASPDHPVLIDQFLEDATEVDVDAISDGKLTLVGGVMEHIEEAGVHSGDSACALPPFSLSDEVITEIKEATYALAGALKVRGLMNIQFAVKEVNGDHLVYILEVNPRASRTSPFVSKATGISLPRMAAKIMVGVSLEEQGITTEPWPEYYSVKESVFPFQRFAGVDIILGPEMRSTGEVMGIDERFSLAFAKSQLAAGSQLPREPCKVFVSVAAPHKQAIIGPARVLYRRGFKLVGTAGTAAVLREAGIEVETVRKIQEGRPNLLDFLANGDIHLILNTPNGKGARTDEGKIRAAAVAHGVPCITTLSGCQAVARAMEAMAEDPKPRVRALQDWASTTSPSSTSTNS

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1098-1113Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP036276
EMBL· GenBank· DDBJ
QDU46411.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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