ID C9Z7J9_STRSW Unreviewed; 326 AA. AC C9Z7J9; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 27-MAR-2024, entry version 78. DE RecName: Full=Aspartate carbamoyltransferase {ECO:0000256|HAMAP-Rule:MF_00001}; DE EC=2.1.3.2 {ECO:0000256|HAMAP-Rule:MF_00001}; DE AltName: Full=Aspartate transcarbamylase {ECO:0000256|HAMAP-Rule:MF_00001}; DE Short=ATCase {ECO:0000256|HAMAP-Rule:MF_00001}; GN Name=pyrB {ECO:0000256|HAMAP-Rule:MF_00001, GN ECO:0000313|EMBL:CBG74499.1}; GN OrderedLocusNames=SCAB_75191 {ECO:0000313|EMBL:CBG74499.1}; OS Streptomyces scabiei (strain 87.22). OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces. OX NCBI_TaxID=680198 {ECO:0000313|EMBL:CBG74499.1, ECO:0000313|Proteomes:UP000001444}; RN [1] {ECO:0000313|EMBL:CBG74499.1, ECO:0000313|Proteomes:UP000001444} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=87.22 {ECO:0000313|EMBL:CBG74499.1, RC ECO:0000313|Proteomes:UP000001444}; RX PubMed=20064060; DOI=10.1094/MPMI-23-2-0161; RA Bignell D.R., Seipke R.F., Huguet-Tapia J.C., Chambers A.H., Parry R.J., RA Loria R.; RT "Streptomyces scabies 87-22 contains a coronafacic acid-like biosynthetic RT cluster that contributes to plant-microbe interactions."; RL Mol. Plant Microbe Interact. 23:161-175(2010). CC -!- FUNCTION: Catalyzes the condensation of carbamoyl phosphate and CC aspartate to form carbamoyl aspartate and inorganic phosphate, the CC committed step in the de novo pyrimidine nucleotide biosynthesis CC pathway. {ECO:0000256|HAMAP-Rule:MF_00001}. CC -!- CATALYTIC ACTIVITY: CC Reaction=carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L- CC aspartate + phosphate; Xref=Rhea:RHEA:20013, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:29991, ChEBI:CHEBI:32814, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:58228; EC=2.1.3.2; CC Evidence={ECO:0000256|ARBA:ARBA00001363, ECO:0000256|HAMAP- CC Rule:MF_00001}; CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; CC (S)-dihydroorotate from bicarbonate: step 2/3. CC {ECO:0000256|ARBA:ARBA00004852, ECO:0000256|HAMAP-Rule:MF_00001}. CC -!- SUBUNIT: Heterododecamer (2C3:3R2) of six catalytic PyrB chains CC organized as two trimers (C3), and six regulatory PyrI chains organized CC as three dimers (R2). {ECO:0000256|HAMAP-Rule:MF_00001}. CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase CC superfamily. ATCase family. {ECO:0000256|HAMAP-Rule:MF_00001}. 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; FN554889; CBG74499.1; -; Genomic_DNA. DR RefSeq; WP_013005033.1; NC_013929.1. DR AlphaFoldDB; C9Z7J9; -. DR STRING; 680198.SCAB_75191; -. DR GeneID; 24313637; -. DR KEGG; scb:SCAB_75191; -. DR eggNOG; COG0540; Bacteria. DR HOGENOM; CLU_043846_2_0_11; -. DR UniPathway; UPA00070; UER00116. DR Proteomes; UP000001444; Chromosome. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0004070; F:aspartate carbamoyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro. DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro. DR Gene3D; 3.40.50.1370; Aspartate/ornithine carbamoyltransferase; 2. DR HAMAP; MF_00001; Asp_carb_tr; 1. DR InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd. DR InterPro; IPR006130; Asp/Orn_carbamoylTrfase. DR InterPro; IPR036901; Asp/Orn_carbamoylTrfase_sf. DR InterPro; IPR002082; Asp_carbamoyltransf. DR InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd. DR NCBIfam; TIGR00670; asp_carb_tr; 1. DR PANTHER; PTHR45753:SF6; ASPARTATE 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; PR00101; ATCASE. DR SUPFAM; SSF53671; Aspartate/ornithine carbamoyltransferase; 1. DR PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1. PE 3: Inferred from homology; KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975, ECO:0000256|HAMAP- KW Rule:MF_00001}; Reference proteome {ECO:0000313|Proteomes:UP000001444}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00001}. FT DOMAIN 3..147 FT /note="Aspartate/ornithine carbamoyltransferase carbamoyl-P FT binding" FT /evidence="ECO:0000259|Pfam:PF02729" FT DOMAIN 163..309 FT /note="Aspartate/ornithine carbamoyltransferase Asp/Orn- FT binding" FT /evidence="ECO:0000259|Pfam:PF00185" FT BINDING 55 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00001" FT BINDING 56 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00001" FT BINDING 83 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00001" FT BINDING 105 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00001" FT BINDING 135 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00001" FT BINDING 138 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00001" FT BINDING 176 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00001" FT BINDING 230 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00001" FT BINDING 271 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00001" FT BINDING 272 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00001" SQ SEQUENCE 326 AA; 35623 MW; 7C9CF3AA3D4FD41A CRC64; MQRHLISAAD LTRDDAVLIL DTAEEMARVA DRPIKKLPTL RGRTIVNLFF EDSTRTRISF EAAEKRLSAD VINFTAKGSS VSKGESLKDT AQTLEAMGVD AVVIRHGASG APYRLATSGW IDAAVINAGD GTHQHPTQAL LDAFTMRRRL VGRDAGLGQD LSGKRITLVG DVLHSRVARS NVDLLHTLGA QVTLVAPPTL VPVGVHTWPC EVSYDLDSTL AKSDAVMMLR VQRERMNAAF FPTEREYSRR YGLDGDRMAR MPEHAIVMHP GPMVRGMEIT AEVADSDRCT VVEQVANGVS IRMAVLYLLL GGNEPAVTHT RTTEEK //