ID PYRB_PROM1 Reviewed; 339 AA. AC A2C066; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 20-FEB-2007, sequence version 1. DT 27-MAR-2024, entry version 82. 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=NATL1_03121; OS Prochlorococcus marinus (strain NATL1A). OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; OC Prochlorococcaceae; Prochlorococcus. OX NCBI_TaxID=167555; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NATL1A; RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231; RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., RA Richardson P., Chisholm S.W.; RT "Patterns and implications of gene gain and loss in the evolution of RT Prochlorococcus."; RL PLoS Genet. 3:2515-2528(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 = 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; CP000553; ABM74876.1; -; Genomic_DNA. DR RefSeq; WP_011823086.1; NC_008819.1. DR AlphaFoldDB; A2C066; -. DR SMR; A2C066; -. DR KEGG; pme:NATL1_03121; -. DR eggNOG; COG0540; Bacteria. DR HOGENOM; CLU_043846_2_0_3; -. DR UniPathway; UPA00070; UER00116. DR Proteomes; UP000002592; 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; Transferase. FT CHAIN 1..339 FT /note="Aspartate carbamoyltransferase catalytic subunit" FT /id="PRO_0000301605" FT BINDING 59 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001" FT BINDING 60 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001" FT BINDING 87 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001" FT BINDING 109 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001" FT BINDING 142 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001" FT BINDING 145 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001" FT BINDING 182 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001" FT BINDING 253 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001" FT BINDING 294 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001" FT BINDING 295 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001" SQ SEQUENCE 339 AA; 37947 MW; CC29BB14BDF7FA99 CRC64; MNNWKHNHVL DLSTFSLEDY KTVLELTTRF KDVHKSSSKK LPALHGRLIA NLFFEPSTRT RTSFELAAKR LSADVQNFSV SSSSLSKGET PLDTILTYIS MGADILVIRH ESTNVPAELA NYVDINNINT SILNAGDGFH SHPSQGLLDL FTLATFFNPN EPSTNSLLNK KITIVGDILH SRVARSNLWA LTACGAEVTL CGPPSLLPEE FIDFVQNPRL GQNFDPINKR GSVFIKRSLK DALKNSDAVM TLRLQKERMK QNMLKDLDSY YAQYGITHES LKWCEKKVPV LHPGPVNRGV EISNRLVEDN SINLISKQVE NGIPTRMALL YLLGLNKKD //