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G0LF10 · G0LF10_HALWC

Function

function

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.
Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site145ATP 1 (UniProtKB | ChEBI)
Binding site200ATP 1 (UniProtKB | ChEBI)
Binding site206ATP 1 (UniProtKB | ChEBI)
Binding site207ATP 1 (UniProtKB | ChEBI)
Binding site239ATP 1 (UniProtKB | ChEBI)
Binding site241ATP 1 (UniProtKB | ChEBI)
Binding site246ATP 1 (UniProtKB | ChEBI)
Binding site272ATP 1 (UniProtKB | ChEBI)
Binding site273ATP 1 (UniProtKB | ChEBI)
Binding site274ATP 1 (UniProtKB | ChEBI)
Binding site315ATP 1 (UniProtKB | ChEBI)
Binding site315Mg2+ 1 (UniProtKB | ChEBI)
Binding site315Mn2+ 1 (UniProtKB | ChEBI)
Binding site332ATP 1 (UniProtKB | ChEBI)
Binding site332Mg2+ 2 (UniProtKB | ChEBI)
Binding site332Mg2+ 1 (UniProtKB | ChEBI)
Binding site332Mn2+ 1 (UniProtKB | ChEBI)
Binding site332Mn2+ 2 (UniProtKB | ChEBI)
Binding site334Mg2+ 2 (UniProtKB | ChEBI)
Binding site334Mn2+ 2 (UniProtKB | ChEBI)
Binding site750ATP 2 (UniProtKB | ChEBI)
Binding site789ATP 2 (UniProtKB | ChEBI)
Binding site791ATP 2 (UniProtKB | ChEBI)
Binding site796ATP 2 (UniProtKB | ChEBI)
Binding site821ATP 2 (UniProtKB | ChEBI)
Binding site822ATP 2 (UniProtKB | ChEBI)
Binding site823ATP 2 (UniProtKB | ChEBI)
Binding site824ATP 2 (UniProtKB | ChEBI)
Binding site864ATP 2 (UniProtKB | ChEBI)
Binding site864Mg2+ 3 (UniProtKB | ChEBI)
Binding site864Mn2+ 3 (UniProtKB | ChEBI)
Binding site876ATP 2 (UniProtKB | ChEBI)
Binding site876Mg2+ 4 (UniProtKB | ChEBI)
Binding site876Mg2+ 3 (UniProtKB | ChEBI)
Binding site876Mn2+ 4 (UniProtKB | ChEBI)
Binding site876Mn2+ 3 (UniProtKB | ChEBI)
Binding site878Mg2+ 4 (UniProtKB | ChEBI)
Binding site878Mn2+ 4 (UniProtKB | ChEBI)

GO annotations

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

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Carbamoyl phosphate synthase large chain
  • EC number
  • Alternative names
    • Carbamoyl phosphate synthetase ammonia chain

Gene names

    • Name
      carB
    • Ordered locus names
      Hqrw_3840

Organism names

Accessions

  • Primary accession
    G0LF10

Proteomes

Subcellular Location

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.

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-435Carboxyphosphate synthetic domain
Domain149-361ATP-grasp
Domain714-905ATP-grasp
Region973-1088Allosteric 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.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,088
  • Mass (Da)
    117,528
  • Last updated
    2011-10-19 v1
  • MD5 Checksum
    3EABD6F13D84012082473FB66B137973
MTDEDANDNMRVDTNSADSTSADRTILLIGSGPIQIGQAAEFDYSGAQACRALQEEGARVVLVNSNPATIMTDPEMADRVYIEPITTEAIAEIIRSEQPDGVIAGLGGQTGLNVTAELAEEGVLETHNVEIMGTPLETIYATEDRDLFRQRMERIGQPVPQSTTISLTEDEAVQSLTEADLKDRVHEAVETVGGLPVIARTTYTLGGSGSGVVAEMNELIERVRKGLRLSRNSEVLITESIAGWVELEYEVMRDADDSTIIICNMENLDPMGIHTGESIVVTPSQVIPDEGHQAMRDAALDVIRELGIQGGCNIQFAWHDDGTPGGEYRVVEVNPRVSRSSALASKATGYPIARVTAKVALGKRLHEINNEITGETTAAFEPAIDYIVTKVPRWPKDKFDNVDFELSTAMKSTGEAMAIGRTFEESLLKALRSSEYDPAANLETLSDETLKSEYLSRPTPDRAYAIFEAFDREYTVDTVAELTGIKQWYLKRFQRVPTALKTAEEGELTAAATTGVTNTEIAETTEKTIDVVEKTVPGRTYKQVDTCAGEFAAQTPYYYSSRKPEFTSGSGPYEGAAAAGELRVDRDIESVVVVGGGPIRIGQGVEFDYCSVHAVRALRELGIDAHVINNNPETVSTDYDTSDGLFFEPITAEEVADVAEATNADGVMVQFGGQTSVNIGHPLEAELDRRGLDCDILGTSVDAMDLAEDRDRFNRLMSSLDIKQPVGGSATSESEALTLANDLGYPVLVRPSYVLGGRAMDVVHSDVELQEYIEEAVRVSPDKPILIDQFLADAIELDVDAVADGERTIIGGVMEHVESAGVHSGDSACMIPPRSLSAETMARVRTVTEDIATALDTVGLLNVQLAIKDDEVYVLEANPRSSRTVPFVSKATGVPIAKLAAKVMAGESLTTLDVTEQIPAETSVKEVVLPFDRLPGSDPRLGPEMKSTGEVMGTAATFGKAYDKAQHSVGKPIPSSGTAWVDLSDEEFPAPDSNDGAALRDGYDACFELVTFSEDDDVDTLINALRQGEIDIVISRDRDPLEVCVEEEITYFSTTASAFAALEAIDSKNDPIDIDPVSDRPTLKNNWG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
FR746099
EMBL· GenBank· DDBJ
CCC41573.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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