A0A0M6Y2H9 · A0A0M6Y2H9_9HYPH

  • 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 site129ATP 1 (UniProtKB | ChEBI)
Binding site187ATP 1 (UniProtKB | ChEBI)
Binding site193ATP 1 (UniProtKB | ChEBI)
Binding site194ATP 1 (UniProtKB | ChEBI)
Binding site226ATP 1 (UniProtKB | ChEBI)
Binding site228ATP 1 (UniProtKB | ChEBI)
Binding site233ATP 1 (UniProtKB | ChEBI)
Binding site259ATP 1 (UniProtKB | ChEBI)
Binding site260ATP 1 (UniProtKB | ChEBI)
Binding site261ATP 1 (UniProtKB | ChEBI)
Binding site303ATP 1 (UniProtKB | ChEBI)
Binding site303Mg2+ 1 (UniProtKB | ChEBI)
Binding site303Mn2+ 1 (UniProtKB | ChEBI)
Binding site317ATP 1 (UniProtKB | ChEBI)
Binding site317Mg2+ 1 (UniProtKB | ChEBI)
Binding site317Mg2+ 2 (UniProtKB | ChEBI)
Binding site317Mn2+ 2 (UniProtKB | ChEBI)
Binding site317Mn2+ 1 (UniProtKB | ChEBI)
Binding site319Mg2+ 2 (UniProtKB | ChEBI)
Binding site319Mn2+ 2 (UniProtKB | ChEBI)
Binding site743ATP 2 (UniProtKB | ChEBI)
Binding site803ATP 2 (UniProtKB | ChEBI)
Binding site805ATP 2 (UniProtKB | ChEBI)
Binding site810ATP 2 (UniProtKB | ChEBI)
Binding site835ATP 2 (UniProtKB | ChEBI)
Binding site836ATP 2 (UniProtKB | ChEBI)
Binding site837ATP 2 (UniProtKB | ChEBI)
Binding site838ATP 2 (UniProtKB | ChEBI)
Binding site878ATP 2 (UniProtKB | ChEBI)
Binding site878Mg2+ 3 (UniProtKB | ChEBI)
Binding site878Mn2+ 3 (UniProtKB | ChEBI)
Binding site890ATP 2 (UniProtKB | ChEBI)
Binding site890Mg2+ 3 (UniProtKB | ChEBI)
Binding site890Mg2+ 4 (UniProtKB | ChEBI)
Binding site890Mn2+ 4 (UniProtKB | ChEBI)
Binding site890Mn2+ 3 (UniProtKB | ChEBI)
Binding site892Mg2+ 4 (UniProtKB | ChEBI)
Binding site892Mn2+ 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
      LAL4801_01979

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • CECT 4801
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Stappiaceae > Roseibium

Accessions

  • Primary accession
    A0A0M6Y2H9

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.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-421Carboxyphosphate synthetic domain
Domain133-346ATP-grasp
Domain707-919ATP-grasp
Domain985-1120MGS-like
Region985-1120Allosteric 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
    1,120
  • Mass (Da)
    120,604
  • Last updated
    2015-12-09 v1
  • Checksum
    0F7F2E4DA61541DD
MPKRTDISSILIIGAGPIVIGQACEFDYSGTQACKALREEGYRIILVNSNPATIMTDPDLADATYIEPITPELVAKIIEKERPDALLPTMGGQTALNCALDLEQMGVLEKYGVEMIGARADVIEKAEDREKFRAAMDVIGLENPRAAIASSPAIHDENGRIVGYDRNAGYLEAMRAIDEIGLPAIIRPAFTLGGTGGGVAYNREEFETIVRSGIDASPVGQVLIDESLLGWKEYEMEVVRDTADNCIIICSIENVDPMGVHTGDSITVAPALTLTDKEYQIMRDASIAVLREIGVETGGSNVQFAVNPDNGRLVVIEMNPRVSRSSALASKATGFPIAKIAAKLAVGYTLDELENDITGGATPASFEPTIDYVVTKIPRFAFEKFPGSEATLTTAMKSVGEVMAIGRTFNESLQKALRGLETGLNGFDETEIPGLDQGDDRNALRAAVSTPTPTRLLNVAQAMRLGMTVEEIYEASGINPWFLEQIEAILEMEAKVRKLGLPKDAANLRKLKSMGFSDARLASLADLDASDVAKLRKQLDVHPVYKRIDTCAAEFASPTAYMYSTYEAPFMGQPACEANPSDRKKVVILGGGPNRIGQGIEFDYCCCHAAFALEDAGYETIMVNCNPETVSTDYDTSDRLYFEPLTAEDVLEIMRKEQENGTLHGVIVQFGGQTPLKLAQALVKADVPILGTSPDMIDLAEDRDRFQKLLIKLDMKQPENGIAYSVEQGRLIAGQLGLPLVVRPSYVLGGRAMQIIRDEEALNSYLLGTLPELVPAEVRAKYPNDKTGQINTVLGTNPLLFDRYLDGAIEVDVDALCDGKDVFVCGIMEHIEEAGIHSGDSACSLPPFSLGEEMLEELKRQTTALALALEVGGLMNVQYAIKNGEIFVLEVNPRASRTVPFVAKTIGAPVAKIASRIMAGESLASFGLSEKKLDHIAVKEAVFPFARFPGVDTILGPEMRSTGEVMGLDTAFGKAFAKSQIGCGTGVPDKGTVFVSMRDEDKAGVLDAVRSLEAGGFTIIATGGTQKFLEDKGIAVKKINKVLEGRPHIVDAIKNGEVQLVFNTTEGAQAISDSRSMRRAALLNKVPYYTTLAGSVAAAKGIAAHKAGSLEVRPLQSYFG

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CXST01000001
EMBL· GenBank· DDBJ
CTQ43539.1
EMBL· GenBank· DDBJ
Genomic DNA

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