ID B2JDU5_PARP8 Unreviewed; 309 AA. AC B2JDU5; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 02-SEP-2026, entry version 105. DE RecName: Full=Ornithine carbamoyltransferase {ECO:0000256|ARBA:ARBA00016634, ECO:0000256|NCBIfam:TIGR00658}; DE EC=2.1.3.3 {ECO:0000256|ARBA:ARBA00013007, ECO:0000256|NCBIfam:TIGR00658}; GN OrderedLocusNames=Bphy_0529 {ECO:0000313|EMBL:ACC69721.1}; OS Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 / OS STM815) (Burkholderia phymatum). OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria; OC Burkholderiales; Burkholderiaceae; Paraburkholderia. OX NCBI_TaxID=391038 {ECO:0000313|EMBL:ACC69721.1, ECO:0000313|Proteomes:UP000001192}; RN [1] {ECO:0000313|Proteomes:UP000001192} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815 RC {ECO:0000313|Proteomes:UP000001192}; RX PubMed=25197461; DOI=10.4056/sigs.4861021; RA Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A., Melkonian R., RA James E.K., Young J.P., Bena G., Hauser L., Land M., Kyrpides N., Bruce D., RA Chain P., Copeland A., Pitluck S., Woyke T., Lizotte-Waniewski M., RA Bristow J., Riley M.; RT "Complete genome sequence of Burkholderia phymatum STM815(T), a broad host RT range and efficient nitrogen-fixing symbiont of Mimosa species."; RL Stand. Genomic Sci. 9:763-774(2014). CC -!- FUNCTION: Reversibly catalyzes the transfer of the carbamoyl group from CC carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to CC produce L-citrulline. {ECO:0000256|ARBA:ARBA00003822}. CC -!- CATALYTIC ACTIVITY: CC Reaction=carbamoyl phosphate + L-ornithine = L-citrulline + phosphate + CC H(+); Xref=Rhea:RHEA:19513, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:46911, ChEBI:CHEBI:57743, ChEBI:CHEBI:58228; EC=2.1.3.3; CC Evidence={ECO:0000256|ARBA:ARBA00048772, 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|ARBA:ARBA00004496, CC 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; CP001043; ACC69721.1; -; Genomic_DNA. DR RefSeq; WP_012399946.1; NC_010622.1. DR AlphaFoldDB; B2JDU5; -. DR STRING; 391038.Bphy_0529; -. DR KEGG; bph:Bphy_0529; -. DR eggNOG; COG0078; Bacteria. DR HOGENOM; CLU_043846_3_2_4; -. DR OrthoDB; 9802587at2; -. DR UniPathway; UPA00068; UER00112. DR Proteomes; UP000001192; Chromosome 1. 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 GO; GO:0006526; P:L-arginine biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0019240; P:L-citrulline biosynthetic process; IEA:TreeGrafter. DR FunFam; 3.40.50.1370:FF:000008; Ornithine carbamoyltransferase; 1. 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 NCBIfam; NF001986; PRK00779.1; 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:UP000001192}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01109}. FT DOMAIN 7..147 FT /note="Aspartate/ornithine carbamoyltransferase carbamoyl-P FT binding" FT /evidence="ECO:0000259|Pfam:PF02729" FT DOMAIN 154..301 FT /note="Aspartate/ornithine carbamoyltransferase Asp/Orn- FT binding" FT /evidence="ECO:0000259|Pfam:PF00185" FT BINDING 56..59 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109" FT BINDING 83 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109" FT BINDING 107 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109" FT BINDING 134..137 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109" FT BINDING 165 FT /ligand="L-ornithine" FT /ligand_id="ChEBI:CHEBI:46911" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109" FT BINDING 223 FT /ligand="L-ornithine" FT /ligand_id="ChEBI:CHEBI:46911" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109" FT BINDING 227..228 FT /ligand="L-ornithine" FT /ligand_id="ChEBI:CHEBI:46911" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109" FT BINDING 263..264 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109" FT BINDING 291 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01109" SQ SEQUENCE 309 AA; 35398 MW; 903AAF89DFA24CC4 CRC64; MTAKTIRHYL QFNDFSLEDY EYVLERARIL KRKFKNYETY HPLHDRTLAM IFEKNSTRTR LSFEAGIFQL GGHAVFMSTR DTQLGRGEPI EDAAQVISRM VDIIMIRTFG QDIIQRFAEN SRVPVINGLT NEYHPCQVLA DIFTYYEHRG PIRGKTVAWV GDANNMLYTW IEAAQILGFT LRLSTPPGYK LDRALVAPES APFYEEFDDP NEACKGADLV TTDVWTSMGF EAENEARKKA FADWCVDADM MSRASKDALF MHCLPAHRGE EVSAEVIDGP QSVVWDEAEN RLHVQKALME FLLLGKLNH //