AC   MF_00001;
DC   Protein; auto
TR   HAMAP; MF_00001; -; 1; level=0
XX
Names: Asp_carb_tr
XX
ID   PYRB
DE   RecName: Full=Aspartate carbamoyltransferase;
DE            EC=2.1.3.2;
DE   AltName: Full=Aspartate transcarbamylase;
DE            Short=ATCase;
GN   Name=pyrB;
XX
CC   -!- FUNCTION: Catalyzes the condensation of carbamoyl phosphate and
CC       aspartate to form carbamoyl aspartate and inorganic phosphate, the
CC       committed step in the de novo pyrimidine nucleotide biosynthesis
CC       pathway.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-
CC         aspartate + phosphate; Xref=Rhea:RHEA:20013, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29991, ChEBI:CHEBI:32814, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58228; EC=2.1.3.2;
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       (S)-dihydroorotate from bicarbonate: step 2/3.
case <OC:Bacteria>
CC   -!- SUBUNIT: Heterododecamer (2C3:3R2) of six catalytic PyrB chains
CC       organized as two trimers (C3), and six regulatory PyrI chains organized
CC       as three dimers (R2).
else case <OC:Archaea>
CC   -!- SUBUNIT: Heterooligomer of catalytic and regulatory chains.
end case
CC   -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC       superfamily. ATCase family.
XX
DR   Pfam; PF00185; OTCace; 1; trigger=no
DR   NCBIfam; TIGR00670; asp_carb_tr; 1; trigger=no
DR   PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1; trigger=no
XX
KW   Pyrimidine biosynthesis
KW   Transferase
XX
GO   GO:0004070; F:aspartate carbamoyltransferase activity
GO   GO:0006221; P:pyrimidine nucleotide biosynthetic process
XX
FT   From: PYRB_ECOLI (P0A786)
FT   BINDING         55
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT   Condition: R
FT   BINDING         56
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT   Condition: T
FT   BINDING         85
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT   Condition: K
FT   BINDING         106
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT   Condition: R
FT   BINDING         135
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT   Condition: H
FT   BINDING         138
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT   Condition: Q
FT   BINDING         168
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT   Condition: R
FT   BINDING         230
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT   Condition: R
FT   BINDING         268
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT   Condition: [GASL]
FT   BINDING         269
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT   Condition: P
XX
Size: 291-475;
Related: None;
Template: P0A786; P05654; Q58976; Q55338;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: MF_00002 (pyrI)
Duplicate: in SHEHH
Plasmid: None
Comments: None
XX
# Revision 1.37 2023/09/19
//