AC MF_02234; DC Protein; auto TR HAMAP; MF_02234; -; 1; level=0 XX Names: AOTCase XX ID AOTC DE RecName: Full=N-acetylornithine carbamoyltransferase; DE EC=2.1.3.9; DE AltName: Full=N-acetyl-L-ornithine transcarbamylase; DE Short=AOTCase; DE Short=Acetylornithine transcarbamylase; GN Name=argF'; XX CC -!- FUNCTION: Catalyzes the transfer of the carbamoyl group from carbamoyl CC phosphate to the delta-amino group of N(2)-acetyl-L-ornithine to CC produce N(2)-acetyl-L-citrulline. This is a step in an alternative CC arginine biosynthesis pathway. CC -!- CATALYTIC ACTIVITY: CC Reaction=carbamoyl phosphate + N(2)-acetyl-L-ornithine = H(+) + N(2)- CC acetyl-L-citrulline + phosphate; Xref=Rhea:RHEA:18609, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57805, CC ChEBI:CHEBI:58228, ChEBI:CHEBI:58765; EC=2.1.3.9; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18610; CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis. CC -!- SUBUNIT: Homotrimer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase CC superfamily. AOTCase family. XX DR Pfam; PF00185; OTCace; 1; trigger=no DR Pfam; PF02729; OTCace_N; 1; trigger=no DR PRINTS; PR00100; AOTCASE; 1; trigger=no XX KW Amino-acid biosynthesis KW Arginine biosynthesis KW Cytoplasm KW Transferase XX GO GO:0043857; F:N-acetylornithine carbamoyltransferase activity GO GO:0006526; P:arginine biosynthetic process GO GO:0005737; C:cytoplasm XX FT From: AOTC_XANCP (Q8P8J2) FT BINDING 49..52 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /ligand_note="ligand shared between two neighboring FT subunits" FT /note="in other chain" FT Condition: S-x-R-T FT BINDING 148..151 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /ligand_note="ligand shared between two neighboring FT subunits" FT /note="in other chain" FT Condition: H-P-C-Q FT BINDING 294..295 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /ligand_note="ligand shared between two neighboring FT subunits" FT /note="in other chain" FT Condition: C-L FT BINDING 77 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /ligand_note="ligand shared between two neighboring FT subunits" FT Condition: W FT BINDING 112 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /ligand_note="ligand shared between two neighboring FT subunits" FT /note="in other chain" FT Condition: R FT BINDING 144 FT /ligand="N(2)-acetyl-L-ornithine" FT /ligand_id="ChEBI:CHEBI:57805" FT Condition: E FT BINDING 252 FT /ligand="N(2)-acetyl-L-ornithine" FT /ligand_id="ChEBI:CHEBI:57805" FT Condition: K FT BINDING 295 FT /ligand="N(2)-acetyl-L-ornithine" FT /ligand_id="ChEBI:CHEBI:57805" FT Condition: L FT BINDING 322 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /ligand_note="ligand shared between two neighboring FT subunits" FT /note="in other chain" FT Condition: R FT SITE 92 FT /note="Key residue in conferring substrate specificity for FT N-acetyl-L-ornithine versus N-succinyl-L-ornithine" FT Condition: E FT MOD_RES 302 FT /note="N6-carboxylysine" FT Condition: K XX Size: 310-370; Related: None; Template: Q8P8J2; Scope: Bacteria Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: None XX # Revision 1.7 2022/11/19 //