ID PYRB_BACCL Reviewed; 308 AA. AC P41008; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 2. DT 02-SEP-2026, entry version 100. 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}; OS Bacillus caldolyticus. OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Anoxybacillaceae; OC Geobacillus; Geobacillus thermoleovorans group. OX NCBI_TaxID=1394; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=DSM 405 / NBRC 15313 / YP-T; RX PubMed=7516791; DOI=10.1099/00221287-140-3-479; RA Ghim S.Y., Nielsen P., Neuhard J.; RT "Molecular characterization of pyrimidine biosynthesis genes from the RT thermophile Bacillus caldolyticus."; RL Microbiology 140:479-491(1994). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-61. RC STRAIN=DSM 405 / NBRC 15313 / YP-T; RX PubMed=8206848; DOI=10.1128/jb.176.12.3698-3707.1994; RA Ghim S.Y., Neuhard J.; RT "The pyrimidine biosynthesis operon of the thermophile Bacillus RT caldolyticus includes genes for uracil phosphoribosyltransferase and uracil RT permease."; RL J. Bacteriol. 176:3698-3707(1994). 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 ECO:0000305}. 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; X73308; CAA51736.1; -; Genomic_DNA. DR EMBL; X76083; CAA53698.1; -; Genomic_DNA. DR PIR; I40166; I40166. DR AlphaFoldDB; P41008; -. DR SMR; P41008; -. DR UniPathway; UPA00070; UER00116. 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:000011; 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; Transferase. FT CHAIN 1..308 FT /note="Aspartate carbamoyltransferase catalytic subunit" FT /id="PRO_0000113091" FT BINDING 49 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001" FT BINDING 50 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001" FT BINDING 77 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001" FT BINDING 99 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001" FT BINDING 127 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001" FT BINDING 130 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001" FT BINDING 160 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001" FT BINDING 211 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001" FT BINDING 252 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001" FT BINDING 253 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001" SQ SEQUENCE 308 AA; 34871 MW; FAAA34EA1620291A CRC64; MTHLFALSEL PLDEIHRLLD EAERFRSGRI WRPAAPMYVA NLFFEPSTRT KCSFEMAERK LGLHVIPFDP ERSSVQKGET LYDTVRTLEA IGVDAVVIRH HEDAYFEALR HAVGIPIINA GDGCGHHPTQ SLLDLLTIRQ EFGAFTGLTV AIIGDIRHSR VARSNAEVLT RLGANVLFSG PEEWKDETNP YGTYVEVDEA IARADVVMLL RIQHERHAET MGLTKEEYHA RYGLTLERAR RMKSGAIILH PAPVNRGVEI ASELVEAKAS RIFKQMENGV YVRMAVLKRA MEGRMEHGRM AEKWHVVQ //