ID PYRB_FRAAA Reviewed; 318 AA. AC Q0RF77; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 1. DT 18-JUN-2025, entry version 97. DE RecName: Full=Aspartate carbamoyltransferase catalytic subunit {ECO:0000255|HAMAP-Rule:MF_00001}; DE EC=2.1.3.2 {ECO:0000255|HAMAP-Rule:MF_00001}; DE AltName: Full=Aspartate transcarbamylase {ECO:0000255|HAMAP-Rule:MF_00001}; DE Short=ATCase {ECO:0000255|HAMAP-Rule:MF_00001}; GN Name=pyrB {ECO:0000255|HAMAP-Rule:MF_00001}; GN OrderedLocusNames=FRAAL5238; OS Frankia alni (strain DSM 45986 / CECT 9034 / ACN14a). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Frankiales; OC Frankiaceae; Frankia. OX NCBI_TaxID=326424; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 45986 / CECT 9034 / ACN14a; RX PubMed=17151343; DOI=10.1101/gr.5798407; RA Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N., RA Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A., RA Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P., RA Goltsman E., Huang Y., Kopp O.R., Labarre L., Lapidus A., Lavire C., RA Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J., RA Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F., RA Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C., RA Benson D.R.; RT "Genome characteristics of facultatively symbiotic Frankia sp. strains RT reflect host range and host plant biogeography."; RL Genome Res. 17:7-15(2007). 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:0000255|HAMAP-Rule:MF_00001}. CC -!- CATALYTIC ACTIVITY: CC Reaction=carbamoyl phosphate + L-aspartate = N-carbamoyl-L-aspartate + CC phosphate + H(+); 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; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00001}; CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; CC (S)-dihydroorotate from bicarbonate: step 2/3. {ECO:0000255|HAMAP- CC 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:0000255|HAMAP-Rule:MF_00001}. CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase CC superfamily. ATCase family. {ECO:0000255|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; CT573213; CAJ63871.1; -; Genomic_DNA. DR AlphaFoldDB; Q0RF77; -. DR SMR; Q0RF77; -. DR STRING; 326424.FRAAL5238; -. DR KEGG; fal:FRAAL5238; -. DR eggNOG; COG0540; Bacteria. DR HOGENOM; CLU_043846_2_0_11; -. DR UniPathway; UPA00070; UER00116. DR Proteomes; UP000000657; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. 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-UniRule. DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro. DR FunFam; 3.40.50.1370:FF:000007; Aspartate carbamoyltransferase; 1. DR FunFam; 3.40.50.1370:FF:000012; Aspartate carbamoyltransferase; 1. 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 NCBIfam; NF002032; PRK00856.1; 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; Reference proteome; Transferase. FT CHAIN 1..318 FT /note="Aspartate carbamoyltransferase catalytic subunit" FT /id="PRO_0000321102" FT BINDING 66 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001" FT BINDING 67 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001" FT BINDING 94 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001" FT BINDING 116 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001" FT BINDING 144 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001" FT BINDING 147 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001" FT BINDING 177 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001" FT BINDING 231 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001" FT BINDING 272 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001" FT BINDING 273 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001" SQ SEQUENCE 318 AA; 34245 MW; 26A57F4ED0CFE646 CRC64; MVGVGGERRS GMKGHLLSTE DLSRDDALLV LDTAERMARV AEASVRKLPT LRGRTVVNLF FEDSTRTRTS FEVAAKRLSA DVINFSARGS SVSKGESLKD TAQTLEAMGA DAVVCRHSAS GAPHRLATWV RGSVVNAGDG THEHPTQALL DAFTMRQRLG RVDGLAVTIV GDVLHSRVAR SNVWLLATLG ASVTVVAPPT LLPIGVSSWP VEVSYDLDAV LPKTDVVMML RVQRERMSAA FFPTEREYSR RYGLDVDRAA TLPEHALVMH PGPMVRGMEI ASRVADSDRS TVVEQVANGV SVRMAVLYLL LGGSGEVS //