ID D9SN23_CLOC7 Unreviewed; 310 AA. AC D9SN23; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAR-2024, entry version 80. DE RecName: Full=ornithine carbamoyltransferase {ECO:0000256|ARBA:ARBA00013007}; DE EC=2.1.3.3 {ECO:0000256|ARBA:ARBA00013007}; GN OrderedLocusNames=Clocel_2146 {ECO:0000313|EMBL:ADL51889.1}; OS Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=573061 {ECO:0000313|EMBL:ADL51889.1, ECO:0000313|Proteomes:UP000002730}; RN [1] {ECO:0000313|EMBL:ADL51889.1, ECO:0000313|Proteomes:UP000002730} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35296 / DSM 3052 / OCM 3 / 743B RC {ECO:0000313|Proteomes:UP000002730}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L., RA Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N., RA Hemme C.L., Woyke T.; RT "Complete sequence of Clostridium cellulovorans 743B."; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. 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; CC Evidence={ECO:0000256|ARBA:ARBA00001065, ECO:0000256|HAMAP- CC Rule:MF_01109}; CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine CC from L-ornithine and carbamoyl phosphate: step 1/3. CC {ECO:0000256|ARBA:ARBA00004975}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01109}. CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase CC superfamily. OTCase family. {ECO:0000256|ARBA:ARBA00007805, CC ECO:0000256|HAMAP-Rule:MF_01109}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP002160; ADL51889.1; -; Genomic_DNA. DR RefSeq; WP_010076892.1; NC_014393.1. DR AlphaFoldDB; D9SN23; -. DR STRING; 573061.Clocel_2146; -. DR KEGG; ccb:Clocel_2146; -. DR eggNOG; COG0078; Bacteria. DR HOGENOM; CLU_043846_3_2_9; -. DR OrthoDB; 9802587at2; -. DR Proteomes; UP000002730; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0004585; F:ornithine carbamoyltransferase activity; IEA:UniProtKB-UniRule. DR Gene3D; 3.40.50.1370; Aspartate/ornithine carbamoyltransferase; 2. DR HAMAP; MF_01109; OTCase; 1. DR InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd. DR InterPro; IPR006130; Asp/Orn_carbamoylTrfase. DR InterPro; IPR036901; Asp/Orn_carbamoylTrfase_sf. DR InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd. DR InterPro; IPR002292; Orn/put_carbamltrans. DR InterPro; IPR024904; OTCase_ArgI. DR NCBIfam; TIGR00658; orni_carb_tr; 1. DR PANTHER; PTHR45753; ORNITHINE CARBAMOYLTRANSFERASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR45753:SF3; ORNITHINE TRANSCARBAMYLASE, MITOCHONDRIAL; 1. DR Pfam; PF00185; OTCace; 1. DR Pfam; PF02729; OTCace_N; 1. DR PRINTS; PR00100; AOTCASE. DR PRINTS; PR00102; OTCASE. DR SUPFAM; SSF53671; Aspartate/ornithine carbamoyltransferase; 1. DR PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01109}; KW Reference proteome {ECO:0000313|Proteomes:UP000002730}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01109}. FT DOMAIN 4..144 FT /note="Aspartate/ornithine carbamoyltransferase carbamoyl-P FT binding" FT /evidence="ECO:0000259|Pfam:PF02729" FT DOMAIN 150..303 FT /note="Aspartate/ornithine carbamoyltransferase Asp/Orn- FT binding" FT /evidence="ECO:0000259|Pfam:PF00185" FT BINDING 53..56 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109" FT BINDING 80 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109" FT BINDING 104 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109" FT BINDING 131..134 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109" FT BINDING 162 FT /ligand="L-ornithine" FT /ligand_id="ChEBI:CHEBI:46911" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109" FT BINDING 226 FT /ligand="L-ornithine" FT /ligand_id="ChEBI:CHEBI:46911" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109" FT BINDING 230..231 FT /ligand="L-ornithine" FT /ligand_id="ChEBI:CHEBI:46911" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109" FT BINDING 266..267 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109" FT BINDING 294 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109" SQ SEQUENCE 310 AA; 35263 MW; 6ABA3A4D0129860C CRC64; MKAKDLLTLK DLSKEEILEI IDLSEQLKYE TKHGIEHHYL KGKTLGMIFR KHSTRTRVSF EVGMYQLGGF ALFLNSSDIQ MSRGEAIEDT GRVLARYLDG IMIRTFDQRE VEELAAASRI PIINGLTDEE HPCQVLADLL TIKENKRKFK GLKVAFVGDG HNMANTLMIG CLKVDMDFSI ATPKGYETKE KIIEAARLVE KDSLGTLTIT NSPEEAVKDA DVVITDVWTS MGQETEKNLR KEIFKSYQVN KQLMSFAKID AMVLHCLPAH KDEEITTEIF EEHQEEIFEE SENRLHVQKA VLVKLMGKNN //