ID OTC_STAAS Reviewed; 333 AA. AC Q6GA45; DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 1. DT 04-NOV-2026, entry version 115. DE RecName: Full=Ornithine carbamoyltransferase {ECO:0000255|HAMAP-Rule:MF_01109}; DE Short=OTCase {ECO:0000255|HAMAP-Rule:MF_01109}; DE EC=2.1.3.3 {ECO:0000255|HAMAP-Rule:MF_01109}; GN Name=argF {ECO:0000255|HAMAP-Rule:MF_01109}; GN OrderedLocusNames=SAS1102; OS Staphylococcus aureus (strain MSSA476). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=282459; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MSSA476; RX PubMed=15213324; DOI=10.1073/pnas.0402521101; RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J., RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A., RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C., RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z., RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N., RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A., RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M., RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.; RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence RT for the rapid evolution of virulence and drug resistance."; RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004). 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:0000250}. 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:0000255|HAMAP-Rule:MF_01109}; CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine CC from L-ornithine and carbamoyl phosphate: step 1/3. {ECO:0000255|HAMAP- CC Rule:MF_01109}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01109}. CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase CC superfamily. OTCase family. {ECO:0000255|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; BX571857; CAG42878.1; -; Genomic_DNA. DR RefSeq; WP_000793612.1; NC_002953.3. DR AlphaFoldDB; Q6GA45; -. DR SMR; Q6GA45; -. DR KEGG; sas:SAS1102; -. DR HOGENOM; CLU_043846_3_1_9; -. DR OMA; AAEEDWH; -. DR UniPathway; UPA00068; UER00112. 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-UniRule. DR GO; GO:0019240; P:L-citrulline biosynthetic process; IEA:TreeGrafter. DR FunFam; 3.40.50.1370:FF:000004; 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 NCBIfam; NF003286; PRK04284.1; 1. DR PANTHER; PTHR45753:SF2; ORNITHINE CARBAMOYLTRANSFERASE; 1. DR PANTHER; PTHR45753; ORNITHINE CARBAMOYLTRANSFERASE, 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 Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm; Transferase. FT CHAIN 1..333 FT /note="Ornithine carbamoyltransferase" FT /id="PRO_0000113017" FT BINDING 56..59 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109" FT BINDING 83 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109" FT BINDING 107 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109" FT BINDING 134..137 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109" FT BINDING 167 FT /ligand="L-ornithine" FT /ligand_id="ChEBI:CHEBI:46911" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109" FT BINDING 231 FT /ligand="L-ornithine" FT /ligand_id="ChEBI:CHEBI:46911" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109" FT BINDING 235..236 FT /ligand="L-ornithine" FT /ligand_id="ChEBI:CHEBI:46911" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109" FT BINDING 273..274 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109" FT BINDING 318 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109" SQ SEQUENCE 333 AA; 37534 MW; 4AEBB45E867C04A1 CRC64; MKNLRNRSFL TLLDFSRQEV EFLLTLSEDL KRAKYIGTEK PMLKNKNIAL LFEKDSTRTR CAFEVAAHDQ GANVTYLGPT GSQMGKKETT KDTARVLGGM YDGIEYRGFS QRTVETLAEY SGVPVWNGLT DEDHPTQVLA DFLTAKEVLK KDYADINFTY VGDGRNNVAN ALMQGAAIMG MNFHLVCPKE LNPTDELLNR CKNIAAENGG NILITDNIDQ GVKGSDVIYT DVWVSMGEPD EVWKERLELL KPYQVNKEMM DKTGNPNVIF EHCLPSFHNA DTKIGQQIFE KYGIREMEVT DEVFESKASV VFQEAENRMH TIKAVMVATL GEF //