A0A076JFY8 · A0A076JFY8_BIFAD

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 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 site717ATP 2 (UniProtKB | ChEBI)
Binding site765ATP 2 (UniProtKB | ChEBI)
Binding site767ATP 2 (UniProtKB | ChEBI)
Binding site772ATP 2 (UniProtKB | ChEBI)
Binding site797ATP 2 (UniProtKB | ChEBI)
Binding site798ATP 2 (UniProtKB | ChEBI)
Binding site799ATP 2 (UniProtKB | ChEBI)
Binding site800ATP 2 (UniProtKB | ChEBI)
Binding site840ATP 2 (UniProtKB | ChEBI)
Binding site840Mg2+ 3 (UniProtKB | ChEBI)
Binding site840Mn2+ 3 (UniProtKB | ChEBI)
Binding site852ATP 2 (UniProtKB | ChEBI)
Binding site852Mg2+ 3 (UniProtKB | ChEBI)
Binding site852Mg2+ 4 (UniProtKB | ChEBI)
Binding site852Mn2+ 4 (UniProtKB | ChEBI)
Binding site852Mn2+ 3 (UniProtKB | ChEBI)
Binding site854Mg2+ 4 (UniProtKB | ChEBI)
Binding site854Mn2+ 4 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctionATP binding
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
      AD0028_0571
      , AL0467_0592
      , B0070_0596
      , DWX79_02325
      , ERS852382_01198
      , F3K97_02905
      , GA629_01610
      , GA752_01690
      , NE692_00280
      , QEP23_03325

Organism names

  • Taxonomic identifier
  • Strains
    • 2789STDY5608824
    • 70B
    • AD2-8
    • AL46-7
    • AF21-27
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Bifidobacteriales > Bifidobacteriaceae > Bifidobacterium

Accessions

  • Primary accession
    A0A076JFY8

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
Region1-402Carboxyphosphate synthetic domain
Domain133-328ATP-grasp
Domain681-881ATP-grasp
Region963-1126Allosteric domain
Domain964-1126MGS-like

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,126
  • Mass (Da)
    123,155
  • Last updated
    2014-10-29 v1
  • Checksum
    F5B3E169FF0FE42A
MPKRTDIKSVMVIGSGPIVIGQAAEFDYSGTQACRVLREEGIRVILVNSNPATIMTDPEMADATYIEPISTPILEQIIAKERPDALLPTLGGQTALNAAMALGEAGVLKKYNVELIGASLDAIDRGEDRELFKKVVEEAGAESARSDIAHSLEEVDKIAEKFGYPLVVRPSFTMGGLGSGIAHDEDELHRIAGAGIHYSPTDEVLIEEGIEGWKEYELELMRDKKDNVVVVCPIENVDPVGVHTGDSITVAPVFTLTDREYQKLRDIGIAIIRGVGVDTGGCNIQFAVNPDTGRIIVIEMNPRVSRSSALASKATGFPIAKIATKLALGYTLDEIQNDITQSTPASFEPTIDYVVTKVPRFAFEKFPGADPTLTTSMKSVGEAMALAGNFQESLGKAMRSIDKRHMGFNWDGDKPSEDEVSQLLDAIKVPTEHRYLQIQRALWGGATEEQIFAATKIDPWFIRQFALINETALEVKNAEKLTRKLLKKAKLAGLSDLQIAHLRRLGDEGENTIRELRWSYDLRPVFKTVDTCAAEFDAATPYYYSCYADETELRPRDREAVIILGSGPNRIGQGIEFDYTCVHAVQELGKNYDTIMVNCNPETVSTDYDMSDRLYFEPLTFEDVLEIYEAEKKMGPIKGVIVQLGGQTPLSLAARLKAAGVPILGTTPESIDLAENRELFGEVLKKADMNAPRYGTALSLDEAREAAHAIGYPVLVRPSYVLGGRGMEIVYDDAQLRKYVDRALKEAQADTVVSGRLPSPLLIDKFLQDAVEIDVDALFDGEELYIGGIMEHVEEAGVHSGDAACTLPPSTLSDDQIRRLREGTYAIAKGCGVQGLINVQYAFMANTLYVIEANPRASRTVPFASKATGVALAKAAARIMVGETIQQQRDNGLLLPHGDGGDIHRGQQVAVKESVLPFKRFRTPLGKTVDVLLGPEMRSTGEVMGFDRDFPHAFAKSQLAAYEGGLPTSGNVFISVNDTDKRQLPLFAARLVELGFNIWATEGTASVLRRYGIDSKIVDKISVRMDSDPDDPITTYHAEGSVGKNVVQLIEEGAIDLILNTPNSRGSRSDGYAIRSAAIAADLPQFTTMTEFSAVLMAIEAVRNNDYQIMSIQDHSTQLFELESRD

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CYYI01000004
EMBL· GenBank· DDBJ
CUN73552.1
EMBL· GenBank· DDBJ
Genomic DNA
WDLT01000001
EMBL· GenBank· DDBJ
KAB5748218.1
EMBL· GenBank· DDBJ
Genomic DNA
WDIP01000001
EMBL· GenBank· DDBJ
KAB5887292.1
EMBL· GenBank· DDBJ
Genomic DNA
JANFYM010000001
EMBL· GenBank· DDBJ
MCQ4791916.1
EMBL· GenBank· DDBJ
Genomic DNA
LNKC01000003
EMBL· GenBank· DDBJ
OSG88953.1
EMBL· GenBank· DDBJ
Genomic DNA
LNKF01000002
EMBL· GenBank· DDBJ
OSG95329.1
EMBL· GenBank· DDBJ
Genomic DNA
LNKI01000001
EMBL· GenBank· DDBJ
OSH01532.1
EMBL· GenBank· DDBJ
Genomic DNA
CP047129
EMBL· GenBank· DDBJ
QHB62313.1
EMBL· GenBank· DDBJ
Genomic DNA
QRVT01000001
EMBL· GenBank· DDBJ
RGS65939.1
EMBL· GenBank· DDBJ
Genomic DNA
CP123050
EMBL· GenBank· DDBJ
WGJ18115.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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