A0A354K4H0 · A0A354K4H0_9FIRM

  • Protein
    Multifunctional fusion protein
  • Gene
    carB
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    5/5

Function

function

Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan.
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.
Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.
Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.

Features

Showing features for binding site, active site, site.

Type
IDPosition(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 site284ATP 1 (UniProtKB | ChEBI)
Binding site284Mg2+ 1 (UniProtKB | ChEBI)
Binding site284Mn2+ 1 (UniProtKB | ChEBI)
Binding site298ATP 1 (UniProtKB | ChEBI)
Binding site298Mg2+ 2 (UniProtKB | ChEBI)
Binding site298Mg2+ 1 (UniProtKB | ChEBI)
Binding site298Mn2+ 2 (UniProtKB | ChEBI)
Binding site298Mn2+ 1 (UniProtKB | ChEBI)
Binding site300Mg2+ 2 (UniProtKB | ChEBI)
Binding site300Mn2+ 2 (UniProtKB | ChEBI)
Binding site709ATP 2 (UniProtKB | ChEBI)
Binding site748ATP 2 (UniProtKB | ChEBI)
Binding site750ATP 2 (UniProtKB | ChEBI)
Binding site754ATP 2 (UniProtKB | ChEBI)
Binding site779ATP 2 (UniProtKB | ChEBI)
Binding site780ATP 2 (UniProtKB | ChEBI)
Binding site781ATP 2 (UniProtKB | ChEBI)
Binding site782ATP 2 (UniProtKB | ChEBI)
Binding site822ATP 2 (UniProtKB | ChEBI)
Binding site822Mg2+ 3 (UniProtKB | ChEBI)
Binding site822Mn2+ 3 (UniProtKB | ChEBI)
Binding site834ATP 2 (UniProtKB | ChEBI)
Binding site834Mg2+ 3 (UniProtKB | ChEBI)
Binding site834Mg2+ 4 (UniProtKB | ChEBI)
Binding site834Mn2+ 3 (UniProtKB | ChEBI)
Binding site834Mn2+ 4 (UniProtKB | ChEBI)
Binding site836Mg2+ 4 (UniProtKB | ChEBI)
Binding site836Mn2+ 4 (UniProtKB | ChEBI)
Binding site1087substrate
Binding site1138substrate
Active site1147
Active site1147Proton donor
Binding site1148-1149substrate
Binding site1236substrate
Site1238Could be important to modulate the pK values of the two catalytic cysteine residues
Binding site1269substrate
Site1287Could be important to modulate the pK values of the two catalytic cysteine residues
Binding site1287-1288substrate
Active site1296Proton acceptor
Binding site1297-1298substrate

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctionATP binding
Molecular Functioncarbamoyl-phosphate synthase (ammonia) activity
Molecular Functioncarbamoyl-phosphate synthase (glutamine-hydrolyzing) activity
Molecular Functiondiaminopimelate epimerase activity
Molecular Functionmetal ion binding
Biological Process'de novo' UMP biosynthetic process
Biological Processarginine biosynthetic process
Biological Processglutamine metabolic process
Biological Processlysine biosynthetic process via diaminopimelate

Keywords

Enzyme and pathway databases

    • UPA00034UER00025
    • UPA00068UER00171
    • UPA00070UER00115

Names & Taxonomy

Protein names

  • Recommended name
    Multifunctional fusion protein

Including 2 domains:

  • Recommended name
    Diaminopimelate epimerase
  • EC number
  • Short names
    DAP epimerase
  • Alternative names
    • PLP-independent amino acid racemase
  • Recommended name
    Carbamoyl phosphate synthase large chain
  • EC number
  • Alternative names
    • Carbamoyl phosphate synthetase ammonia chain

Gene names

    • Name
      carB
    • Synonyms
      dapF
    • ORF names
      DDX71_01265

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • UBA9758
  • Taxonomic lineage
    Bacteria > Bacillota > Clostridia > Eubacteriales > Oscillospiraceae > Ruminococcus

Accessions

  • Primary accession
    A0A354K4H0

Proteomes

Subcellular Location

Keywords

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.
Homodimer.

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-401Carboxyphosphate synthetic domain
Domain133-327ATP-grasp
Domain673-863ATP-grasp
Domain931-1074MGS-like
Region931-1353Allosteric 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.
Belongs to the diaminopimelate epimerase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,353
  • Mass (Da)
    146,554
  • Last updated
    2018-11-07 v1
  • Checksum
    3F6C337DCDA041A9
MPLNRDIHKVLVIGSGPIVIGQAAEFDYSGTQACRALKEEGIEVVLVNSNPATIMTDNQIADQIYMEPLKSDVIKRICLKEKPDSILSGLGGQTGLNLCAELAKSGFLAANGIRLLGANPETIARAEDRKLFKETMDSIGQPCIPSGIAEDMETARHIAAEIGYPVIIRPAYTLGGSGGGIAETPSDLEKIAENGLRLSPIHQILVERCIAGWKEIEFEIVRDADGNKLTVCSMENFDPVGIHTGDSIVIAPAVTLADKEYQMLRTAALKIAEVLKIEGGCNCQFALSPDSFEYAVIEVNPRVSRSSALASKATGYPIAKVAAKIAIGYRLYEIANKVTGKTTAAFEPSLDYVAVKMPKFPFEKFASASHRLGTQMKATGEVMAISDSFESALLKALRGAEVKHSALLVRALRSLPDAELREHLVHADDVRLFAAAEAMRRGFSVDEIAEASRIDRWFLHKICKLVTCETALENTPLTDALYRTAKRFGYPDDTIAAISDKALPEKRYRPHYRMVDTCAGEFAAETPYFYGVCKPDAAQEADEAAAFLAGRPHKTVVVLGSGPIRIGQGIEFDYSAVHCVQVLKNAGYEVVLINNNPETVSTDFDTADRLYFEPLTPEDVLSILALEQPVGVVTAFGGQTAIRLARTIEEAGYRLLGASADSIDLAEDRERFDALLESLQIDRPRGCTVDTLEEAAEAVQTLGLPVLVRPSYVLGGQNMNIAFESGDVAAFMQNILADGIDNPVLIDQYIRGTEIEVDAICDGKDILIPGIMEHIERTGVHSGDSIAICPPVHIDDEMRRKILTDTKKICLGLHAVGLINLQYIVKGHSLYVIEVNPRASRTVPFMSKLTGLPLCDCAMRVCLGEKLAAMDYGTGYYKTPPYTAVKVPVFSFEKIGGESQLGPEMKSTGEVIGIGKTLTEALYKGLRAAGYRLEDSGRNGSGVLLTVCDADKPDIVEIARKFARLGFVLYATSGTAAALTRAGLAVHTLRKLHDGDTETFRLMENGTIRYIVSTDANARMAARDGAKIRKKAVELGIPCLTCTDTAAAVANCLHTGYRDSNVELMNMNHLRTAKRRIPFVKMHGCGNDYIYVNCMEKRVSAPESLAVQLSDRHFGIGGDGLVLIESSEIADARMRMFNLDGSEGNMCGNAIRCVAKYLYDNGICTKKEIVIETKSGLRTVTVTTQNGVVTHAAVNMGKAIFEPARIPVQFAGNEMIAQPLTVAGTEYTVTCVSMGNPHCVVFGENPETLNLAAIGPEFEHHPAFPEQVNTEFVQVINRKTLRMRVWERGSGETMACGTGACGTVAAAVKNGFCDPDTDVTVHLNGGDLVIRYTEDAVFMTGEAVLIFSGEIEV

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DNTQ01000016
EMBL· GenBank· DDBJ
HBI84908.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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