A0A3C0BLF1 · A0A3C0BLF1_9SPIR

  • Protein
    Multifunctional fusion protein
  • Gene
    carB
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Organism
  • 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, site, active site.

TypeIDPosition(s)Description
Binding site129ATP 1 (UniProtKB | ChEBI)
Binding site170ATP 1 (UniProtKB | ChEBI)
Binding site176ATP 1 (UniProtKB | ChEBI)
Binding site177ATP 1 (UniProtKB | ChEBI)
Binding site209ATP 1 (UniProtKB | ChEBI)
Binding site211ATP 1 (UniProtKB | ChEBI)
Binding site216ATP 1 (UniProtKB | ChEBI)
Binding site242ATP 1 (UniProtKB | ChEBI)
Binding site243ATP 1 (UniProtKB | ChEBI)
Binding site244ATP 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 site736ATP 2 (UniProtKB | ChEBI)
Binding site775ATP 2 (UniProtKB | ChEBI)
Binding site781ATP 2 (UniProtKB | ChEBI)
Binding site806ATP 2 (UniProtKB | ChEBI)
Binding site807ATP 2 (UniProtKB | ChEBI)
Binding site808ATP 2 (UniProtKB | ChEBI)
Binding site809ATP 2 (UniProtKB | ChEBI)
Binding site849ATP 2 (UniProtKB | ChEBI)
Binding site849Mg2+ 3 (UniProtKB | ChEBI)
Binding site849Mn2+ 3 (UniProtKB | ChEBI)
Binding site861ATP 2 (UniProtKB | ChEBI)
Binding site861Mg2+ 3 (UniProtKB | ChEBI)
Binding site861Mg2+ 4 (UniProtKB | ChEBI)
Binding site861Mn2+ 3 (UniProtKB | ChEBI)
Binding site861Mn2+ 4 (UniProtKB | ChEBI)
Binding site863Mg2+ 4 (UniProtKB | ChEBI)
Binding site863Mn2+ 4 (UniProtKB | ChEBI)
Binding site1112substrate
Binding site1163substrate
Binding site1173-1174substrate
Site1284Could be important to modulate the pK values of the two catalytic cysteine residues
Binding site1315substrate
Site1333Could be important to modulate the pK values of the two catalytic cysteine residues
Binding site1333-1334substrate
Active site1342Proton acceptor
Binding site1343-1344substrate

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 Functionlyase 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
      DCL73_11990

Organism names

  • Taxonomic identifier
  • Organism
    Treponema sp
  • Strain
    • UBA12315
  • Taxonomic lineage
    Bacteria > Spirochaetota > Spirochaetia > Spirochaetales > Treponemataceae > Treponema

Accessions

  • Primary accession
    A0A3C0BLF1

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.

TypeIDPosition(s)Description
Region1-402Carboxyphosphate synthetic domain
Domain133-328ATP-grasp
Region576-958Carbamoyl phosphate synthetic domain
Domain700-890ATP-grasp
Domain959-1099MGS-like
Region959-1399Allosteric 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
    1,399
  • Mass (Da)
    152,553
  • Last updated
    2019-01-16 v1
  • Checksum
    3BDC61FE1AD0A9C5
MPLNSSIHKVMVIGSGPIVIGQAAEFDYAGTQACKALKEQGLSVVLVNSNPATLMTDHSMADAIYIEPLIPETIQRIIEKEKPDSLLSTLGGQTGLTLSMELAKSGFLESHHVQLLGARPDTIDKAEDRQMFKDTMLSIGEPCIPSKVVTDLKAALDFADSEIGYPAIVRPAFTLGGTGGGIANDHAELAEIAQNGLHRSPIHQILVEKCISGWKEIEFEVMRDHSGNVLTVCSMENFDPVGVHTGDSIVIAPTVTLADKEYQMLRSAALNIISSLKMEGGCNVQLALKPDSFEYAVIEVNPRVSRSSALASKATGYPIAKVATLIAIGYNLDEIPNFVTKKTAACFEPVLDYVVVKMPKFPFDKFVYAKRTLGTQMKATGEVMSIGRTFEEALMKAARGAEVGVNSLRLKAFTEESDERIKQRVGECTDQRLFAIFEALKRGLMTIDEIHAVTMIDVWFLAKIRHIVDREAQLESVNAGKAVLTPELYLQAKKDGFPDKVITGLSGVKIPGSMGNTKEAKQAASLAAKGKLAHIPATYKMVDTCAGEFNAETPYFYGGYDKQNEAAVFLEERKNKKSKKGTIIVLGSGPIRIGQGIEFDYASVQCVWSLKKLGYDVVTINNNPETVSTDFDTSDRLYFEPLTPEDVMSVINTEKPLGVVVAFGGQTAIKLTKFLDSQGIRILGTSADSIDIAEDRERFEALCDKLGINKPKGETVLTTEEALASANRLTYPVLLRPSYVLGGQNMIIAFNDDDVKEYMEIILAQGIENPVLVDKYMMGTELEVDAICDGKDILIPGIMEHIERTGIHSGDSIAVYPSWNLNDILRQKILKQSRELALALGTKGLVNIQYLIYNNDLYIIEVNPRSSRTVPYISKVTGVPMVELATRAMLGEKVKDFGYGTGLYRIPPYFAVKVPVFSFEKLMDVDTHLGPEMKSTGEVLGLASTMEEAIFKGLIGAGYRMKKTGGVLFTVRKTDQFEIPDLARKFYDMGFKLYATEGTAEVISDFGMEVTVVNKIHENPDDNLLTLLDTGKIDYVVSTSAKGRDPRADSVRMRRHAVERDIPCLTAIDTANALANCLMSHYTAENVELVNINELRETKEKLHFYKMQSTGNDFIIIDAEHQVVTNPGGLAVSLCKRHAGIGADSLVLIKNSDKADAYMQFFNLDGSEGRMAGNAIRAVAKYLYDNNINGVKDKSDESAPTAKLTIDTASGIKKLTLYKLNGKVSSVTVDMGCPQFTAESLPTTLKPVDMKGGASMPAKAIVNVPLTVAGTGYDVTCLSVGTPHCVVFCGFVDKVDLETVGPQFENNEAFPNRTNTEFVRVVGRNELKMRTWERGNGETPACGTGACAAAIAAVLNGYCPMNENITVKVRGGTLVVKYTGDTVYLTGQSDLTYEGDIEI

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DMFX01000087
EMBL· GenBank· DDBJ
HAH62806.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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