W0FTH5 · W0FTH5_9BACT

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.

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 site699ATP 2 (UniProtKB | ChEBI)
Binding site738ATP 2 (UniProtKB | ChEBI)
Binding site744ATP 2 (UniProtKB | ChEBI)
Binding site769ATP 2 (UniProtKB | ChEBI)
Binding site770ATP 2 (UniProtKB | ChEBI)
Binding site771ATP 2 (UniProtKB | ChEBI)
Binding site772ATP 2 (UniProtKB | ChEBI)
Binding site812ATP 2 (UniProtKB | ChEBI)
Binding site812Mg2+ 3 (UniProtKB | ChEBI)
Binding site812Mn2+ 3 (UniProtKB | ChEBI)
Binding site824ATP 2 (UniProtKB | ChEBI)
Binding site824Mg2+ 3 (UniProtKB | ChEBI)
Binding site824Mg2+ 4 (UniProtKB | ChEBI)
Binding site824Mn2+ 3 (UniProtKB | ChEBI)
Binding site824Mn2+ 4 (UniProtKB | ChEBI)
Binding site826Mg2+ 4 (UniProtKB | ChEBI)
Binding site826Mn2+ 4 (UniProtKB | ChEBI)
Binding site1077substrate
Binding site1128substrate
Binding site1138-1139substrate
Binding site1226substrate
Site1228Could be important to modulate the pK values of the two catalytic cysteine residues
Binding site1259substrate
Site1277Could be important to modulate the pK values of the two catalytic cysteine residues
Binding site1277-1278substrate
Active site1286Proton acceptor
Binding site1287-1288substrate

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
      dapF
    • Synonyms
      carB

Organism names

Accessions

  • Primary accession
    W0FTH5

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
Domain663-853ATP-grasp
Region922-1343Allosteric domain
Domain926-1073MGS-like

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
    1,343
  • Mass (Da)
    145,733
  • Last updated
    2014-03-19 v1
  • Checksum
    915A8395A94F5581
MPKDKSIQKVLVIGSGPIVIGQAAEFDYAGAQACRVLRQEGIRTVLVNSNPATIMTDKHLADAIYLEPLTAETLRRIIALERPDGLLAGLGGQTGLTLAMQLTKDGTLEKYGVRLLGSDINAIERAEDRELFRETLQNMGQPVVPSDTAEDLDTALDIAERIGYPVIVRPAYTLGGTGGGIAADEDELRVIARTGLDLSPITQILVEKCISGWKEIEFETMRDAAGNVIAVCSMENLDPVGIHTGDSIVVAPALTLADREYQMLRSAALEIVTEIGIVGGCNCQFALDPESFEYAVIEVNPRVSRSSALASKATGYPIAKISTRIALGYTLDEIKNDITGKTCACFEPAVDYVVVKVPKWPFDKFNGAARTLGTQMKATGEVMSIAPGFEMALMKAVRGAEIGLDTLNAPPLSDAPVRERLAAQDDRRIFTVFEAFKAGLSVEEIHEITMIDRWFLSKLRALADFETVMSMNDLDEATYRKAKNLGYTDEALRRLTGAAELPGAEMSYKMVDTCAAEFDAETPYFYSCFDEECESRAFERSGKPVVIVLGSGPIRIGQGIEFDYSSVHGVWTLREMGYDVVIINNNPETVSTDYDTADRLYFEPLCPEDVWNIVRLEKPVGVVVAFGGQTAIKLTKFLDSRGVRILGTSADGIDLAEDRARFDALLETFGIRRPSGRGVRTMEEALAAAEELGYPVLLRPSYVIGGQNMTIARDAATAETYMRGILAGGIENPVLVDKYMPGTELEVDVISDGEDVLIPGIMEHIERAGVHSGDSIAVYPPYNLSDSFLERICEVSEKLALALGTRGLVNIQYLIFENELYVIEVNPRASRTVPYISKVTNVPMVDLASQIMLGAKLRDLGYGSGLYRTPPYYAVKVPVFSFEKLSDANSILGPEMKSTGEVLGLGRTLAEALFKGLTAAGLVPAGHLRAGAGVLLSVETGDYQEILGLARRFHALGLKLYATEGTAKAIAALGIEVAAVPNATESPRLRELMETGALSYIVYTGAVKDATMGDYIALHRRAMQLGIPCLTSLDTAGALADIIESRFNESNTELVDIVRLRPWRQTIRFTKMHSCGNDYIFIENFDGSITCPESLCVSLCRPHFGIGGDGVVLMERSSAADVKMRSFNRDGSEGRMAGNNVRCVAKYMYDKGYLRSEQMTVETASGVKRLRLYLRDGKVSSVTADMGRAEFAPADVPVAFDGERMVNESVTVGGGEYRVTCLSMGNPHCVVFAPAIDALDLEQVGPLFEHDPIFPERVNAEFVRVVSRHELRMRCWERGSGETLACGTGACAAVAAAVENGLCDAGTDVTVSVLGGELIVNYTPERVLLTGGVTLVYDGSFEY

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KC246874
EMBL· GenBank· DDBJ
AHF26272.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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