AC   MF_01210;
DC   Protein; auto
c?   <OC:Bacteria>
TR   HAMAP; MF_01210_B; -; 1; level=0
c?   <OC:Archaea>
TR   HAMAP; MF_01210_A; -; 1; level=0
XX
Names: CPSase_L_chain
XX
ID   CARB
DE   RecName: Full=Carbamoyl phosphate synthase large chain;
DE            EC=6.3.4.16;
DE            EC=6.3.5.5;
DE   AltName: Full=Carbamoyl phosphate synthetase ammonia chain;
GN   Name=carB;
XX
CC   -!- FUNCTION: Large subunit of the glutamine-dependent carbamoyl phosphate
CC       synthetase (CPSase). CPSase catalyzes the formation of carbamoyl
CC       phosphate from the ammonia moiety of glutamine, carbonate, and
CC       phosphate donated by ATP, constituting the first step of 2 biosynthetic
CC       pathways, one leading to arginine and/or urea and the other to
CC       pyrimidine nucleotides. The large subunit (synthetase) binds the
CC       substrates ammonia (free or transferred from glutamine from the small
CC       subunit), hydrogencarbonate and ATP and carries out an ATP-coupled
CC       ligase reaction, activating hydrogencarbonate by forming carboxy
CC       phosphate which reacts with ammonia to form carbamoyl phosphate.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP +
CC         carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate;
CC         Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359,
CC         ChEBI:CHEBI:456216; EC=6.3.5.5;
CC   -!- CATALYTIC ACTIVITY: [Carbamoyl phosphate synthase large chain]:
CC       Reaction=2 ATP + hydrogencarbonate + NH4(+) = 2 ADP + carbamoyl
CC         phosphate + 2 H(+) + phosphate; Xref=Rhea:RHEA:18029,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228,
CC         ChEBI:CHEBI:456216; EC=6.3.4.16;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC       Note=Binds 4 Mg(2+) or Mn(2+) ions per subunit.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl
CC       phosphate from bicarbonate: step 1/1.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       (S)-dihydroorotate from bicarbonate: step 1/3.
CC   -!- SUBUNIT: Composed of two chains; the small (or glutamine) chain
CC       promotes the hydrolysis of glutamine to ammonia, which is used by the
CC       large (or ammonia) chain to synthesize carbamoyl phosphate. Tetramer of
CC       heterodimers (alpha,beta)4.
CC   -!- DOMAIN: The large subunit is composed of 2 ATP-grasp domains that are
CC       involved in binding the 2 ATP molecules needed for carbamoyl phosphate
CC       synthesis. The N-terminal ATP-grasp domain (referred to as the
CC       carboxyphosphate synthetic component) catalyzes the ATP-dependent
CC       phosphorylation of hydrogencarbonate to carboxyphosphate and the
CC       subsequent nucleophilic attack by ammonia to form a carbamate
CC       intermediate. The C-terminal ATP-grasp domain (referred to as the
CC       carbamoyl phosphate synthetic component) then catalyzes the
CC       phosphorylation of carbamate with the second ATP to form the end
CC       product carbamoyl phosphate. The reactive and unstable enzyme
CC       intermediates are sequentially channeled from one active site to the
CC       next through the interior of the protein over a distance of at least 96
CC       A.
CC   -!- SIMILARITY: Belongs to the CarB family.
XX
DR   Pfam; PF00289; CPSase_L_chain; 1; trigger=no
DR   Pfam; PF02142; MGS; 1; trigger=no
DR   Pfam; PF02786; CPSase_L_D2; 1; trigger=no
DR   Pfam; PF02787; CPSase_L_D3; 1; trigger=no
DR   PRINTS; PR00098; CPSASE; 1; trigger=no
DR   PROSITE; PS00866; CPSASE_1; 1; trigger=no
DR   PROSITE; PS00867; CPSASE_2; 1; trigger=no
DR   PROSITE; PS50975; ATP_GRASP; 1-2; trigger=yes
DR   PROSITE; PS51855; MGS; 1; trigger=yes
DR   NCBIfam; TIGR01369; CPSaseII_lrg; 1; trigger=no
XX
KW   Amino-acid biosynthesis
KW   Arginine biosynthesis
KW   Pyrimidine biosynthesis
KW   Ligase
KW   Repeat
KW   ATP-binding
KW   Nucleotide-binding
XX
GO   GO:0005524; F:ATP binding
GO   GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity
GO   GO:0006526; P:arginine biosynthetic process
GO   GO:0006221; P:pyrimidine nucleotide biosynthetic process
XX
FT   From: CARB_ECOLI (P00968)
case <OC:Bacteria>
FT   REGION          Nter..403
FT                   /note="Carboxyphosphate synthetic domain"
FT   REGION          404..553
FT                   /note="Oligomerization domain"
FT   REGION          554..936
FT                   /note="Carbamoyl phosphate synthetic domain"
FT   REGION          937..Cter
FT                   /note="Allosteric domain"
FT   BINDING         129
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT   Condition: R
FT   BINDING         169
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT   Condition: R
FT   BINDING         175
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT   Condition: G
FT   BINDING         176
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT   Condition: G
FT   BINDING         208
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT   Condition: [EKQR]
FT   BINDING         210
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT   Condition: [LIV]
FT   BINDING         215
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT   Condition: E
FT   BINDING         241
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT   Condition: G
FT   BINDING         242
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT   Condition: [IV]
FT   BINDING         243
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT   Condition: H
FT   BINDING         285
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT   Condition: Q
FT   BINDING         285
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT   Condition: Q
FT   BINDING         285
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT   Condition: Q
FT   BINDING         299
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT   Condition: E
FT   BINDING         299
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT   Condition: E
FT   BINDING         299
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT   Condition: E
FT   BINDING         299
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT   Condition: E
FT   BINDING         299
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT   Condition: E
FT   BINDING         301
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT   Condition: N
FT   BINDING         301
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT   Condition: N
FT   BINDING         715
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT   Condition: R
FT   BINDING         754
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT   BINDING         756
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT   Condition: [LIV]
FT   BINDING         761
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT   Condition: E
FT   BINDING         786
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT   Condition: G
FT   BINDING         787
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT   Condition: [IV]
FT   BINDING         788
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT   Condition: H
FT   BINDING         789
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT   Condition: S
FT   BINDING         829
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT   Condition: Q
FT   BINDING         829
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT   Condition: Q
FT   BINDING         829
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="3"
FT   Condition: Q
FT   BINDING         841
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT   Condition: E
FT   BINDING         841
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT   Condition: E
FT   BINDING         841
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="4"
FT   Condition: E
FT   BINDING         841
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="3"
FT   Condition: E
FT   BINDING         841
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="4"
FT   Condition: E
FT   BINDING         843
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="4"
FT   Condition: N
FT   BINDING         843
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="4"
FT   Condition: N
end case
FT   From: CARB_SULTO (Q970U7)
case <OC:Archaea>
FT   REGION          Nter..399
FT                   /note="Carboxyphosphate synthetic domain"
FT   REGION          400..548
FT                   /note="Oligomerization domain"
FT   REGION          549..930
FT                   /note="Carbamoyl phosphate synthetic domain"
FT   REGION          931..Cter
FT                   /note="Allosteric domain"
FT   BINDING         127
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT   Condition: R
FT   BINDING         167
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT   Condition: R
FT   BINDING         173
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT   Condition: G
FT   BINDING         174
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT   Condition: G
FT   BINDING         206
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT   Condition: [EKQR]
FT   BINDING         208
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT   Condition: [LIV]
FT   BINDING         213
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT   Condition: E
FT   BINDING         239
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT   Condition: G
FT   BINDING         240
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT   Condition: [IV]
FT   BINDING         241
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT   Condition: H
FT   BINDING         282
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT   Condition: Q
FT   BINDING         282
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT   Condition: Q
FT   BINDING         282
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT   Condition: Q
FT   BINDING         296
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT   Condition: E
FT   BINDING         296
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT   Condition: E
FT   BINDING         296
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT   Condition: E
FT   BINDING         296
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT   Condition: E
FT   BINDING         296
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT   Condition: E
FT   BINDING         298
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT   Condition: N
FT   BINDING         298
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT   Condition: N
FT   BINDING         710
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT   Condition: R
FT   BINDING         749
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT   BINDING         751
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT   Condition: [LIV]
FT   BINDING         756
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT   Condition: E
FT   BINDING         780
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT   Condition: G
FT   BINDING         781
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT   Condition: [IV]
FT   BINDING         782
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT   Condition: H
FT   BINDING         783
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT   Condition: S
FT   BINDING         823
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT   Condition: Q
FT   BINDING         823
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT   Condition: Q
FT   BINDING         823
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="3"
FT   Condition: Q
FT   BINDING         835
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT   Condition: E
FT   BINDING         835
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT   Condition: E
FT   BINDING         835
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="4"
FT   Condition: E
FT   BINDING         835
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="3"
FT   Condition: E
FT   BINDING         835
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="4"
FT   Condition: E
FT   BINDING         837
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="4"
FT   Condition: N
FT   BINDING         837
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="4"
FT   Condition: N
end case
XX
case <OC:Bacteria>
Size: 1020-1167;
end case
case <OC:Archaea>
Size: 1024-1076;
end case
Related: None;
Template: P00968; O50302; Q9ZB63; O32771; P77886; Q9RLS9;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: in HALH5, GEOSE, BACSU, LACPL
Plasmid: None
Comments: Bacillaceae, Geobacillus and lactobacillaceae seem to posess two members of
 this family: one specific for arginine biosynthesis (called CARY_ in ID, and
 CARB in GN) and the other specific for pyrimidine synthesis (called CARB_ in
 ID, and PYRAB in GN).
 Sequence of carB is split into two genes in AQUAE, METJA and METKA.
 Weird insertion in NOSS1, THEMA and ZYMMO (sequences not shown in alignment).
XX
# Revision 1.51 2023/09/19
//