A0A1V5KDU6 · A0A1V5KDU6_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, active 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 site688ATP 2 (UniProtKB | ChEBI)
Binding site727ATP 2 (UniProtKB | ChEBI)
Binding site733ATP 2 (UniProtKB | ChEBI)
Binding site758ATP 2 (UniProtKB | ChEBI)
Binding site759ATP 2 (UniProtKB | ChEBI)
Binding site760ATP 2 (UniProtKB | ChEBI)
Binding site761ATP 2 (UniProtKB | ChEBI)
Binding site801ATP 2 (UniProtKB | ChEBI)
Binding site801Mg2+ 3 (UniProtKB | ChEBI)
Binding site801Mn2+ 3 (UniProtKB | ChEBI)
Binding site813ATP 2 (UniProtKB | ChEBI)
Binding site813Mg2+ 3 (UniProtKB | ChEBI)
Binding site813Mg2+ 4 (UniProtKB | ChEBI)
Binding site813Mn2+ 3 (UniProtKB | ChEBI)
Binding site813Mn2+ 4 (UniProtKB | ChEBI)
Binding site815Mg2+ 4 (UniProtKB | ChEBI)
Binding site815Mn2+ 4 (UniProtKB | ChEBI)
Binding site1115substrate
Binding site1213substrate
Site1215Could be important to modulate the pK values of the two catalytic cysteine residues
Binding site1246substrate
Site1264Could be important to modulate the pK values of the two catalytic cysteine residues
Binding site1264-1265substrate
Active site1273Proton acceptor
Binding site1274-1275substrate

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 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
      BWY81_01631

Organism names

Accessions

  • Primary accession
    A0A1V5KDU6

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
Domain652-842ATP-grasp
Domain911-1051MGS-like
Region911-1330Allosteric 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
    1,330
  • Mass (Da)
    143,895
  • Last updated
    2017-06-07 v1
  • Checksum
    A2497D086CCFF1B8
MPMLEGIKKVMMIGSGPIVIGQAAEFDYSGTQACRVLKAAGLEVVLVNSNPATIMTDRANADEIYLEPLTLETIRRIIEKERPDGLLAGFGGQTGLTVSSQLAKEGFLDRMGVHILGTPAEAIDRAEDRELFKETMEAIGQPLIPSATATDVEHALEIAEKIGYPVIVRPAFTLGGAGGGVAYSADELSAVAAIGLEASPIHQALIEKYIYGWKEIEFEVMRDGVGNAIAICSMENVDPVGVHTGDSIVVAPALTLANREYNILRTAAIDIVSALGVVGGCNCQFALNPDSFEYAVIEVNPRVSRSSALASKATGFPIAKVAAKIALGYRLDEIKNDVTGKACACFEPAIDYVVVKLPRWPFDKFAGASRRLGTQMKATGEVMAIAPTFEAALMKAVRGSEIGMDTLNLKQDGDIRKRLAAMDDRRLFTVFEAIAAGVSFDEIFEITRIDRFFLGRLRKLADFEKNPSYAEGKRLGYTDKALKRLGVDAPGAFLFSYKMVDTCAAEFDAETPYFYATTDKACDSRRFPRSGRPTIVVLGSGPIRIGQGIEFDYSSVHCVRALREMGYEVAIVNNNPETVSTDYDTADRLYFEPLTEEDVLSVVAAENPVGVVVAFGGQTAVKLAKALDRHGIRILGTSAEGIDLAEDRDRFDKMLESLGIRRPAGMGVLTEEEAVLAANKLGYPVLVRPSYVIGGQNMTIAYADKEVRAYMRTILLTGIENPVLVDKYMPGIELEVDVISDGEDVLIPGIMEHIERAGVHSGDSIAVYPPYNLTDGMKKELIDCSERLALALGTKGLVNIQYLIYEGRLYVIEVNPRASRTVPYISKVTGVPMVDLASRVMLGAKLKDLGCGTGLVRTPPYFAVKVPVFSFEKLADVNSYLGPEMKSTGEVLGVGKNMNEALFKGLTAAGIRVPSAGKMGVLLSLDDRDHYGLMALAKKFFDLGAAMYATETTARAIRQLGIDVVEIPGIKQSDDAFKLLESGKIRYIVYTGAVFDQTMDDYIALHRRALSLSIACLTSLDTANALADILKSRYNERNTELVDLNHMRASRSRLRFSKMQCAGTDYIVVDNRDGRVSCAESLCVSLCDRHFGIGGDGIALIEQSDVADARMRMFNRDGSAGGMAGACLMLVGKYLYDKGIAAKEVVTVEAGGNVKRVELFLSDGRVSSARVDMGVPEFSPARVPVNLPGAEIVDRPHVFAGKEYRITCLSLGNPHCVTFVERVDALDLAKLGPAFEGADIFPERVNASFARAVSERMLKLRTYERSNGETLACGTGACAATVAAVKNGLCREGEDIAVKLPGGDLIARYERGRVSLTGETNLAFEGEIEY

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MWAC01000318
EMBL· GenBank· DDBJ
OPZ66862.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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