ID PYRB_ALIB4 Reviewed; 295 AA. AC A8ERG2; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 13-NOV-2007, sequence version 1. DT 04-NOV-2026, entry version 88. 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=Abu_0261; OS Aliarcobacter butzleri (strain RM4018) (Arcobacter butzleri). OC Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria; OC Campylobacterales; Arcobacteraceae; Aliarcobacter. OX NCBI_TaxID=367737; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RM4018; RX PubMed=18159241; DOI=10.1371/journal.pone.0001358; RA Miller W.G., Parker C.T., Rubenfield M., Mendz G.L., Woesten M.M.S.M., RA Ussery D.W., Stolz J.F., Binnewies T.T., Hallin P.F., Wang G., Malek J.A., RA Rogosin A., Stanker L.H., Mandrell R.E.; RT "The complete genome sequence and analysis of the Epsilonproteobacterium RT Arcobacter butzleri."; RL PLoS ONE 2:E1358-E1358(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; CP000361; ABV66536.1; -; Genomic_DNA. DR RefSeq; WP_012012120.1; NC_009850.1. DR AlphaFoldDB; A8ERG2; -. DR SMR; A8ERG2; -. DR STRING; 367737.Abu_0261; -. DR GeneID; 24304465; -. DR KEGG; abu:Abu_0261; -. DR eggNOG; COG0540; Bacteria. DR HOGENOM; CLU_043846_2_0_7; -. DR OMA; AALRWVM; -. DR UniPathway; UPA00070; UER00116. DR Proteomes; UP000001136; 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 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..295 FT /note="Aspartate carbamoyltransferase catalytic subunit" FT /id="PRO_1000057008" 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 161 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001" FT BINDING 212 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001" FT BINDING 251 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" 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" SQ SEQUENCE 295 AA; 33236 MW; 0C623460192C91EB CRC64; MQHLIRTSDF TKEEILDIFE DARGFLDFKP CEILKGKIIV TLFFENSTRT RSSFEIAAKR LGAEIVNLDV GTSSTKKGET MYDTVANINA MGPDAIVIRH SECGLPESLI GYVDCPIINA GDGRHSHPTQ ALLDLFTIYE HFNGQTEGKK IAIVGDVRNS RVAGSNRRLL PRFGIDVNLV APDCFKYEGN EFKQFNTIAE VIDDMDVVMS LRSQLERHNI TYFESLQEYA KDFCITPELM EGRDFLLLHP GPVNRNIDIS DEVLKDPRCK VLEQVRNGVA VRAAILKKLI LNNKN //