A0A0I9TF89 · A0A0I9TF89_9MYCO

  • 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 site134ATP 1 (UniProtKB | ChEBI)
Binding site174ATP 1 (UniProtKB | ChEBI)
Binding site180ATP 1 (UniProtKB | ChEBI)
Binding site181ATP 1 (UniProtKB | ChEBI)
Binding site213ATP 1 (UniProtKB | ChEBI)
Binding site215ATP 1 (UniProtKB | ChEBI)
Binding site220ATP 1 (UniProtKB | ChEBI)
Binding site246ATP 1 (UniProtKB | ChEBI)
Binding site247ATP 1 (UniProtKB | ChEBI)
Binding site248ATP 1 (UniProtKB | ChEBI)
Binding site290ATP 1 (UniProtKB | ChEBI)
Binding site290Mg2+ 1 (UniProtKB | ChEBI)
Binding site290Mn2+ 1 (UniProtKB | ChEBI)
Binding site304ATP 1 (UniProtKB | ChEBI)
Binding site304Mg2+ 1 (UniProtKB | ChEBI)
Binding site304Mg2+ 2 (UniProtKB | ChEBI)
Binding site304Mn2+ 1 (UniProtKB | ChEBI)
Binding site304Mn2+ 2 (UniProtKB | ChEBI)
Binding site306Mg2+ 2 (UniProtKB | ChEBI)
Binding site306Mn2+ 2 (UniProtKB | ChEBI)
Binding site729ATP 2 (UniProtKB | ChEBI)
Binding site768ATP 2 (UniProtKB | ChEBI)
Binding site770ATP 2 (UniProtKB | ChEBI)
Binding site775ATP 2 (UniProtKB | ChEBI)
Binding site800ATP 2 (UniProtKB | ChEBI)
Binding site801ATP 2 (UniProtKB | ChEBI)
Binding site802ATP 2 (UniProtKB | ChEBI)
Binding site803ATP 2 (UniProtKB | ChEBI)
Binding site843ATP 2 (UniProtKB | ChEBI)
Binding site843Mg2+ 3 (UniProtKB | ChEBI)
Binding site843Mn2+ 3 (UniProtKB | ChEBI)
Binding site855ATP 2 (UniProtKB | ChEBI)
Binding site855Mg2+ 4 (UniProtKB | ChEBI)
Binding site855Mg2+ 3 (UniProtKB | ChEBI)
Binding site855Mn2+ 3 (UniProtKB | ChEBI)
Binding site855Mn2+ 4 (UniProtKB | ChEBI)
Binding site857Mg2+ 4 (UniProtKB | ChEBI)
Binding site857Mn2+ 4 (UniProtKB | ChEBI)

GO annotations

AspectTerm
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

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
      ABH38_17720

Organism names

  • Taxonomic identifier
  • Strain
    • UC1
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycobacterium

Accessions

  • Primary accession
    A0A0I9TF89

Proteomes

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.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-407Carboxyphosphate synthetic domain
Domain138-333ATP-grasp
Domain693-884ATP-grasp
Domain966-1113MGS-like
Region966-1124Allosteric 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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,124
  • Mass (Da)
    120,072
  • Last updated
    2015-10-14 v1
  • Checksum
    5622ACFFED3AF5D6
MPRRTDLNHVLVIGSGPIVIGQACEFDYSGTQACRVLRTEGLQVSLVNSNPATIMTDPEYADFTYVEPITPAFIERVIAQQAECGNKIDALLATLGGQTALNTAVALYESRVLERYGVELIGADFDAIQRGEDRQRFKDIVAKVGGESARSRVCFTMDEVRETVEEVGLPVVVRPSFTMGGLGSGMAYSSEEVERMAGAGLAASPSANVLIEESIYGWKEFELELMRDSHDNVVVVCSIENVDPMGVHTGDSVTVAPAMTLTDREYQRMRDLGIAILREVGVDTGGCNIQFAVDPRNGRLIVIEMNPRVSRSSALASKATGFPIAKIAAKLAIGYTLDEIVNDITKETPACFEPTLDYVVVKAPRFAFEKFPGADPTLTTTMKSVGEAMSLGRNFVEALGKVMRSLETSRAGFWTAPDPDGGVEQVLIRLQTPTEGRLYDVELALRLDASIEKVAQVSGIDPWFVAQIDELVRLRSELVAAPVLDAELLRRAKHNGLSDRQIAALRPELAGEDGVRSLRKRLGIHPVYKTVDTCAAEFEAKTPYHYSSYELDPAAETEVAPQAEKPKVLILGSGPNRIGQGIEFDYSCVHAATTLSQAGFETVMVNCNPETVSTDYDTADRLYFEPLTFEDVLEVFHAEEQSAEGGAGVAGVIVQLGGQTPLGLAQRLADAGVPIVGTPPEAIDLAEDRGAFGDVLSAAGLPAPKYGTATTFAQARRIAAEIGYPVLVRPSYVLGGRGMEIVYDEETLKGYITRATALSPEHPVLVDRFLEDAVEIDVDALCDGTEVYIGGVMEHIEEAGIHSGDSACALPPVTLGRSDLEKVRQATEAIARGIGVVGLLNVQYALKDDVLYVLEANPRASRTVPFVSKATAIPLAKACARIMLGASISQLRSEGMLAASGDGGNAAPHAPIAVKEAVLPFHRFRRADGAAIDSLLGPEMKSTGEVMGIDHDFGSAFAKSQTAAYGSLPTQGTVFVSVANRDKRSLVFPVKRLADLGFHVIATEGTAEMLRRNGIPCDEVRKHFEPPQVGRPALSAVDAIRAGDVDMVINTPYGNSGPRIDGYEIRSAAVSVNIPCVTTVQGASAAVQGIEAGIRGDIGVRSLQELHSAIGAGSAADKADKEAQ

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LDPR01000020
EMBL· GenBank· DDBJ
KLO34886.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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