A0A971T701 · A0A971T701_9FIRM

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.

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 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 site705ATP 2 (UniProtKB | ChEBI)
Binding site744ATP 2 (UniProtKB | ChEBI)
Binding site746ATP 2 (UniProtKB | ChEBI)
Binding site750ATP 2 (UniProtKB | ChEBI)
Binding site775ATP 2 (UniProtKB | ChEBI)
Binding site776ATP 2 (UniProtKB | ChEBI)
Binding site777ATP 2 (UniProtKB | ChEBI)
Binding site778ATP 2 (UniProtKB | ChEBI)
Binding site818ATP 2 (UniProtKB | ChEBI)
Binding site818Mg2+ 3 (UniProtKB | ChEBI)
Binding site818Mn2+ 3 (UniProtKB | ChEBI)
Binding site830ATP 2 (UniProtKB | ChEBI)
Binding site830Mg2+ 3 (UniProtKB | ChEBI)
Binding site830Mg2+ 4 (UniProtKB | ChEBI)
Binding site830Mn2+ 4 (UniProtKB | ChEBI)
Binding site830Mn2+ 3 (UniProtKB | ChEBI)
Binding site832Mg2+ 4 (UniProtKB | ChEBI)
Binding site832Mn2+ 4 (UniProtKB | ChEBI)
Binding site1081substrate
Binding site1132substrate
Binding site1142-1143substrate
Binding site1230substrate
Site1232Could be important to modulate the pK values of the two catalytic cysteine residues
Binding site1263substrate
Site1281Could be important to modulate the pK values of the two catalytic cysteine residues
Binding site1281-1282substrate
Binding site1291-1292substrate

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctionATP binding
Molecular Functioncarbamoyl-phosphate synthase (glutamine-hydrolyzing) activity
Molecular Functiondiaminopimelate epimerase activity
Molecular Functionmetal ion binding
Biological Processarginine biosynthetic process
Biological Processglutamine metabolic process
Biological Processlysine biosynthetic process via diaminopimelate
Biological Processpyrimidine nucleotide biosynthetic process

Keywords

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
      GXY34_11545

Organism names

Accessions

  • Primary accession
    A0A971T701

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
Region1-401Carboxyphosphate synthetic domain
Domain133-327ATP-grasp
Domain669-859ATP-grasp
Domain928-1071MGS-like
Region928-1347Allosteric 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
    1,347
  • Mass (Da)
    147,999
  • Last updated
    2023-02-22 v1
  • Checksum
    6CF8DB5A32316A1F
MPLDQDIKKVLVIGSGPIVIGQAAEFDYAGTQACRALKEEGLEVVLVNSNPATIMTDYAMADQIYIEPMTLETIKRIIIKESPDSILSTLGGQTGLTLSMQLAKEGFLKRQGIKLLGANPATIDKAEDRQMFKDTMQSIGEPVIPSLVVTDVIAARAFAREIGYPVIVRPAFTLGGTGGGIAANEKELQEIAANGLRLSPINQVLIEQCVSGWKEIEFEVMRDRAGNVITVCSMENFDPVGVHTGDSIVIAPAVTLSDKEYQMLRSAALNIITALEVEGGCNCQFALHPDSFEYAVIEVNPRVSRSSALASKATGYPIAKVAAKIAVGYTLDEIRNAVTGKTYACFEPALDYVVVKVPKWPFDKFVYAQRALGTQMKATGEVMAIGTSFEQCIMKAVRGAEISLDSLNLPKLKELSDRQIEQLLCECNDERLFVVYEALQRGISCEVIHEVTKIDSWFLNKLANLTILEKELAAGHLTQELYQSAKRLGYPDKVIERLAGGKIEQPLRASYKMVDTCAAEFEAETPYFYSTYDKVNEAEQFIKARSTGKQTIIVFGSGPIRIGQGIEFDYASVHCVWALKKAGYEVVIVNNNPETVSTDFDTADRLYFEPLTDEDVMNVIYTEHPYGVVVAFGGQTAIKLTKFLESQGVRILGTPADSIDAAEDRERFDALLEKLSIKRPQGHTVMKVQEALQVANQLEYPVLMRPSYVLGGQNMIIAFSDDDIREYMDIILTYNIENPVLIDKYLLGIEIEVDAICDGEDILIPGIMEHIERAGIHSGDSIAVYPAWNLSGEVIEQVIDYSKKLALALNTQGLINIQYVIHAGEIYVIEVNPRSSRTIPYISKVTGVPMVDLATRAMLGEKLIDMGYGTGLYKTPPYVAVKVPVFSFEKLVDVDVALGPEMKSTGEVLGIGKTLAEALYKGLVAAGYQMVRQGGVLITVRDSDKPEIVDIAKQYAELGFTLYATSGTAKYLEQAGLRAISVKKIHEAEQDNIQTLLESGKISYIISTSSKGRLPGRDSVKMRRQAVQTAIPCLTSLDTADALAKSLKSRYAQSNTELVDINHMRSERRQLAFTKMQSCGNDYIYFDCFEQQIISPESLSVYLSDRHYGIGSDGIVLICPSDQADAKMQMFNLDGSESKMSGNALTCMGKYIYENQIAVKDEITIETPSGVKKLRLYIQNGKVHSVCVDMGPAELKPEKIPVQLAGREIVNHPVTIAGRDYHITCVSMGNPHCVVFEDNLDSVNLDEIGPAFEYSPLFPERVNVEFVTVIDQNTIKMRVWERGNGETLAAGTSACAGVVAAVRNGCCHQDQYILVKQKGGNLVVKCTDETVFMTGKPEAIFKGTVEI

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAAYCK010000120
EMBL· GenBank· DDBJ
NLW92216.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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