ID PYRB_BRUME Reviewed; 322 AA. AC P65611; Q8YC62; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 27-MAR-2024, entry version 101. 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=BMEII0670; OS Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Brucellaceae; Brucella/Ochrobactrum group; Brucella. OX NCBI_TaxID=224914; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=16M / ATCC 23456 / NCTC 10094; RX PubMed=11756688; DOI=10.1073/pnas.221575398; RA DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T., RA Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G., RA Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E., RA Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J., RA Haselkorn R., Kyrpides N.C., Overbeek R.; RT "The genome sequence of the facultative intracellular pathogen Brucella RT melitensis."; RL Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002). 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 = 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; 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; AE008918; AAL53912.1; -; Genomic_DNA. DR PIR; AE3593; AE3593. DR RefSeq; WP_002966034.1; NZ_GG703779.1. DR AlphaFoldDB; P65611; -. DR SMR; P65611; -. DR GeneID; 45125949; -. DR KEGG; bme:BMEII0670; -. DR KEGG; bmel:DK63_2573; -. DR PATRIC; fig|224914.52.peg.2697; -. DR eggNOG; COG0540; Bacteria. DR PhylomeDB; P65611; -. DR UniPathway; UPA00070; UER00116. DR Proteomes; UP000000419; Chromosome II. 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; Transferase. FT CHAIN 1..322 FT /note="Aspartate carbamoyltransferase catalytic subunit" FT /id="PRO_0000113108" FT BINDING 65 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001" FT BINDING 66 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001" FT BINDING 93 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001" FT BINDING 115 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001" FT BINDING 143 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001" FT BINDING 146 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001" FT BINDING 176 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001" FT BINDING 230 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001" FT BINDING 271 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" 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" SQ SEQUENCE 322 AA; 34802 MW; 81B6208851B9521B CRC64; MTNQTVSPLF PHRHLLGIKG LSPLDILCLL DLADQEIAVS RQPEKKKSVL RGRTQINLFF EASTRTQSSF ELAGKRLGAD VMNMSVGNSS VKKGETLIDT AMTLNAMQPD ILVIRHASAG AAALLAQKVG CSVVNAGDGA HEHPTQALLD ALTIRRAKGQ IENLIVAICG DVLHSRVARS NILLLNALGA RVRVVAPSTL LPAGMADMSV EVFNSMEEGL KDADVVMMLR LQRERMAGSF VPSVREYFHF YGLDREKLKF AKPDALVMHP GPMNRGVEIA SDVADGPQSV IQQQVEMGVA VRMAVMEALL DPRRNPGNGE PA //