Essential maintenance is planned to begin on Fri Jan 24 2025. The website may be temporarily unavailable. Please use our fallback: https://wwwdev.ebi.ac.uk/uniprot/front-end/fallback/ in case of any outage.

A0A0E3MJ78 · A0A0E3MJ78_SACSO

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.

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 site127ATP 1 (UniProtKB | ChEBI)
Binding site167ATP 1 (UniProtKB | ChEBI)
Binding site173ATP 1 (UniProtKB | ChEBI)
Binding site174ATP 1 (UniProtKB | ChEBI)
Binding site206ATP 1 (UniProtKB | ChEBI)
Binding site208ATP 1 (UniProtKB | ChEBI)
Binding site213ATP 1 (UniProtKB | ChEBI)
Binding site239ATP 1 (UniProtKB | ChEBI)
Binding site240ATP 1 (UniProtKB | ChEBI)
Binding site241ATP 1 (UniProtKB | ChEBI)
Binding site282ATP 1 (UniProtKB | ChEBI)
Binding site282Mg2+ 1 (UniProtKB | ChEBI)
Binding site282Mn2+ 1 (UniProtKB | ChEBI)
Binding site296ATP 1 (UniProtKB | ChEBI)
Binding site296Mg2+ 1 (UniProtKB | ChEBI)
Binding site296Mg2+ 2 (UniProtKB | ChEBI)
Binding site296Mn2+ 2 (UniProtKB | ChEBI)
Binding site296Mn2+ 1 (UniProtKB | ChEBI)
Binding site298Mg2+ 2 (UniProtKB | ChEBI)
Binding site298Mn2+ 2 (UniProtKB | ChEBI)
Binding site709ATP 2 (UniProtKB | ChEBI)
Binding site748ATP 2 (UniProtKB | ChEBI)
Binding site750ATP 2 (UniProtKB | ChEBI)
Binding site755ATP 2 (UniProtKB | ChEBI)
Binding site779ATP 2 (UniProtKB | ChEBI)
Binding site780ATP 2 (UniProtKB | ChEBI)
Binding site781ATP 2 (UniProtKB | ChEBI)
Binding site782ATP 2 (UniProtKB | ChEBI)
Binding site822ATP 2 (UniProtKB | ChEBI)
Binding site822Mg2+ 3 (UniProtKB | ChEBI)
Binding site822Mn2+ 3 (UniProtKB | ChEBI)
Binding site834ATP 2 (UniProtKB | ChEBI)
Binding site834Mg2+ 3 (UniProtKB | ChEBI)
Binding site834Mg2+ 4 (UniProtKB | ChEBI)
Binding site834Mn2+ 4 (UniProtKB | ChEBI)
Binding site834Mn2+ 3 (UniProtKB | ChEBI)
Binding site836Mg2+ 4 (UniProtKB | ChEBI)
Binding site836Mn2+ 4 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctionATP binding
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
    • ORF names
      HFC64_14825
      , SSOP1_0634
      , SULA_1731
      , SULB_1732
      , SULC_1730
      , SULG_08680
      , SULH_08680
      , SULI_08680
      , SULM_08670
      , SULN_08670
      , SULO_08680
      , SULZ_08605

Organism names

Accessions

  • Primary accession
    A0A0E3MJ78

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
Region1-399Carboxyphosphate synthetic domain
Domain131-325ATP-grasp
Region400-548Oligomerization domain
Region549-930Carbamoyl phosphate synthetic domain
Domain673-863ATP-grasp
Domain930-1051MGS-like
Region931-1051Allosteric 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
    1,051
  • Mass (Da)
    118,204
  • Last updated
    2015-06-24 v1
  • MD5 Checksum
    16AD7372B9885D73494BD4E0EBEBCB70
MRETPKKVLVIGSGPIKIAEAAEFDYSGSQALKALKEEGIETVLVNSNVATVQTSKKFADKLYMLPVVWWAVEKVIEKERPDGIMIGFGGQTALNVGVDLHKKGVLQKYNVKVLGTQIDGIEKALSREKFRETMIENNLPVPPSLSARSEEEAIKNAKIVGYPVMVRVSFNLGGRGSMVAWTEEDLKKNIRRALSQSYIGEVLLEKYLYHWIELEYEVMRDKKGNSAVIACIENLDPMGVHTGESTVVAPCQTLDNLEYQNMRTYTIEVARSINLIGECNVQFALNPRGYEYYIIETNPRMSRSSALASKATGYPLAYVSAKLALGYELHEVINKVSGRTCACFEPSLDYIVTKIPRWDLSKFENVDQSLATEMMSVGEVMSIGRSFEESLQKAIRMLDIGEPGVVGGKVYESNMSKEEALKYLKERRPYWFLYAAKAFKEGATINEVYEVTGINEFFLNKIKGLVDFYETLRKLKEIDKETLKLAKKLGFSDEQISKALNKSTEYVRKIRYETNTIPVVKLIDTLAGEWPAVTNYMYLTYNGTEDDIEFSQGNKLLIIGAGGFRIGVSVEFDWSVVSLMEAGSKYFDEVAVLNYNPETVSTDWDIARKLYFDEISVERVLDLIKKEKFRYVATFSGGQIGNSIAKELEENGVRLLGTSGSSVDIAENREKFSKLLDKLGISQPDWISATSLGEIKKFANEVGFPVLVRPSYVLSGSSMKIAYSEEELYEYVRRATEISPKYPVVISKYIENAIEAEIDGVSDGNKVLGITLEHIEEAGVHSGDATMSIPFRKLSENNVNRMRENVLNIARELNIKGPFNVQFVVKENTPYIIELNLRASRSMPFSSKAKGINLINESMKAIFDGLDFSEDYYEPPSKYWAVKSAQFSWSQLRGAYPFLGPEMKSTGEAASFGVTFYDALLKSWLSSMPNRIPNKNGIALVYGNKNLDYLKDTADNLTRFGLTVYSISELPLQDIETIDKMKAEELVRAKKVEIIVTDGYLKKFDYNIRRTAVDYNIPIILNGRLGYEVSKAFLNYDSLTFFEISEYGGGI

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP011055
EMBL· GenBank· DDBJ
AKA73978.1
EMBL· GenBank· DDBJ
Genomic DNA
CP011056
EMBL· GenBank· DDBJ
AKA76675.1
EMBL· GenBank· DDBJ
Genomic DNA
CP011057
EMBL· GenBank· DDBJ
AKA79369.1
EMBL· GenBank· DDBJ
Genomic DNA
CP033235
EMBL· GenBank· DDBJ
AZF68455.1
EMBL· GenBank· DDBJ
Genomic DNA
CP033236
EMBL· GenBank· DDBJ
AZF71075.1
EMBL· GenBank· DDBJ
Genomic DNA
CP033237
EMBL· GenBank· DDBJ
AZF73695.1
EMBL· GenBank· DDBJ
Genomic DNA
CP033238
EMBL· GenBank· DDBJ
AZF76318.1
EMBL· GenBank· DDBJ
Genomic DNA
CP033239
EMBL· GenBank· DDBJ
AZF78926.1
EMBL· GenBank· DDBJ
Genomic DNA
CP033240
EMBL· GenBank· DDBJ
AZF81531.1
EMBL· GenBank· DDBJ
Genomic DNA
CP033241
EMBL· GenBank· DDBJ
AZF84108.1
EMBL· GenBank· DDBJ
Genomic DNA
CP050869
EMBL· GenBank· DDBJ
QPG50918.1
EMBL· GenBank· DDBJ
Genomic DNA
LT549890
EMBL· GenBank· DDBJ
SAI84189.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help