AC MF_01109; DC Protein; auto TR HAMAP; MF_01109; -; 1; level=0 XX Names: OTCase XX case defined and not ID OTCC DE RecName: Full=Ornithine carbamoyltransferase, catabolic; DE Short=OTCase; DE EC=2.1.3.3; else ID OTC DE RecName: Full=Ornithine carbamoyltransferase; DE Short=OTCase; DE EC=2.1.3.3; end case case and GN Name=argI; end case case and not GN Name=argF; end case case not GN Name=arcB; end case XX CC -!- CATALYTIC ACTIVITY: CC Reaction=carbamoyl phosphate + L-ornithine = H(+) + L-citrulline + CC phosphate; Xref=Rhea:RHEA:19513, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:46911, ChEBI:CHEBI:57743, CC ChEBI:CHEBI:58228; EC=2.1.3.3; case CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine CC from L-ornithine and carbamoyl phosphate: step 1/3. end case case not CC -!- PATHWAY: Amino-acid degradation; L-arginine degradation via ADI CC pathway; carbamoyl phosphate from L-arginine: step 2/2. end case CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase CC superfamily. OTCase family. XX DR Pfam; PF00185; OTCace; 1; trigger=no DR Pfam; PF02729; OTCace_N; 1; trigger=no DR PRINTS; PR00100; AOTCASE; 1; trigger=no DR NCBIfam; TIGR00658; Orni_carb_tr; 1; trigger=no DR PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1; trigger=no XX case KW Amino-acid biosynthesis KW Arginine biosynthesis end case case not KW Arginine metabolism end case KW Cytoplasm KW Transferase XX GO GO:0004585; F:ornithine carbamoyltransferase activity case GO GO:0006526; P:arginine biosynthetic process end case case not GO GO:0019546; P:arginine deiminase pathway end case GO GO:0005737; C:cytoplasm XX FT From: OTC1_ECOLI (P04391) FT BINDING 56..59 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT Condition: S-[TS]-R-T FT BINDING 134..137 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT Condition: H-x(2)-Q FT BINDING 236..237 FT /ligand="L-ornithine" FT /ligand_id="ChEBI:CHEBI:46911" FT Condition: S-[MIL] FT BINDING 274..275 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT Condition: C-L FT BINDING 83 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT Condition: [QN] FT BINDING 107 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT Condition: R FT BINDING 168 FT /ligand="L-ornithine" FT /ligand_id="ChEBI:CHEBI:46911" FT Condition: N FT BINDING 232 FT /ligand="L-ornithine" FT /ligand_id="ChEBI:CHEBI:46911" FT Condition: D FT BINDING 320 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT Condition: [RK] XX Size: 295-354; Related: MF_02102!; Template: P04391; P9WIT9; Q8DCF5; Scope: Bacteria Archaea Fusion: Nter: None Cter: None Duplicate: in ECOL6, LACLA, PSEAE, PSEPK, RHIME, SALTI, SALTY, STAAM, STAAN, STAAW, STAES, STRA3, STRA5 Plasmid: in HALSA, RHIME Comments: OTCases can be involved in the biosynthesis of arginine and in its catabolism, by the arginine deiminase pathway. Some bacteria possess two distinct OTCases; some do not degrade arginine using this pathway and others do not synthesize arginine. As it is impossible to distinguish between anabolic and catabolic OTCases based on sequence similarity alone, if paralogs are found in a given genome, then one is probably the anabolic enzyme and the other the catabolic one, named arcB, which is usually located in the arcABC operon. E.coli K-12 carries two genes for anabolic OTCase, argF and argI; their products interact to form a family of four trimeric isoenzymes. Only argI can be found in E.coli B, E.coli W or in other enterobacteria. XX # Revision 1.40 2023/06/01 //