ID A0A7J2IDN7_UNCAA Unreviewed; 308 AA. AC A0A7J2IDN7; DT 07-APR-2021, integrated into UniProtKB/TrEMBL. DT 07-APR-2021, sequence version 1. DT 27-MAR-2024, entry version 8. DE RecName: Full=Aspartate carbamoyltransferase {ECO:0000256|HAMAP-Rule:MF_00001}; DE EC=2.1.3.2 {ECO:0000256|HAMAP-Rule:MF_00001}; DE AltName: Full=Aspartate transcarbamylase {ECO:0000256|HAMAP-Rule:MF_00001}; DE Short=ATCase {ECO:0000256|HAMAP-Rule:MF_00001}; GN Name=pyrB {ECO:0000256|HAMAP-Rule:MF_00001, GN ECO:0000313|EMBL:HDH41316.1}; GN ORFNames=ENG12_02780 {ECO:0000313|EMBL:HDH41316.1}; OS Altiarchaeales archaeon. OC Archaea; Candidatus Altarchaeota; Candidatus Altarchaeales. OX NCBI_TaxID=2250256 {ECO:0000313|EMBL:HDH41316.1}; RN [1] {ECO:0000313|EMBL:HDH41316.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HyVt-188 {ECO:0000313|EMBL:HDH41316.1}; RX PubMed=31911466; RA Zhou Z., Liu Y., Xu W., Pan J., Luo Z.H., Li M.; RT "Genome- and Community-Level Interaction Insights into Carbon Utilization RT and Element Cycling Functions of Hydrothermarchaeota in Hydrothermal RT Sediment."; RL mSystems 5:e00795-e00719(2020). 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:0000256|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; CC Evidence={ECO:0000256|ARBA:ARBA00001363, ECO:0000256|HAMAP- CC Rule:MF_00001}; CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; CC (S)-dihydroorotate from bicarbonate: step 2/3. CC {ECO:0000256|ARBA:ARBA00004852, ECO:0000256|HAMAP-Rule:MF_00001}. CC -!- SUBUNIT: Heterooligomer of catalytic and regulatory chains. CC {ECO:0000256|HAMAP-Rule:MF_00001}. CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase CC superfamily. ATCase family. {ECO:0000256|HAMAP-Rule:MF_00001}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:HDH41316.1}. 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; DQZU01000100; HDH41316.1; -; Genomic_DNA. DR AlphaFoldDB; A0A7J2IDN7; -. DR UniPathway; UPA00070; UER00116. DR Proteomes; UP000886325; Unassembled WGS sequence. 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 {ECO:0000256|ARBA:ARBA00022975, ECO:0000256|HAMAP- KW Rule:MF_00001}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00001}. FT DOMAIN 6..147 FT /note="Aspartate/ornithine carbamoyltransferase carbamoyl-P FT binding" FT /evidence="ECO:0000259|Pfam:PF02729" FT DOMAIN 154..301 FT /note="Aspartate/ornithine carbamoyltransferase Asp/Orn- FT binding" FT /evidence="ECO:0000259|Pfam:PF00185" FT BINDING 57 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00001" FT BINDING 58 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00001" FT BINDING 86 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00001" FT BINDING 107 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00001" FT BINDING 135 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00001" FT BINDING 138 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00001" FT BINDING 168 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00001" FT BINDING 227 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00001" FT BINDING 266 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00001" FT BINDING 267 FT /ligand="carbamoyl phosphate" FT /ligand_id="ChEBI:CHEBI:58228" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00001" SQ SEQUENCE 308 AA; 34465 MW; 65289EFA33ACD65A CRC64; MRWTKKHIIS INDFSRDEID FVLEKSGILE KKLGSSSTSS LMNGKILANL FFEPSTRTRM SFEAAMKRLG GITIGFDHPG ISSEVKGETI ADTVRIVSGY ADLIVIRHPI EGSARLASEY SDVPVINGGD GSNQHPTQTL LDLYTIKKEF KSIDGLDICI VGDLKYGRTV HSLASALGNY DVKIRFISPQ ELRAPRQIVK SLSDRGIEVK ETTKLNLKNS DVIYVTRIQK ERFPDPQEYE RVKGAFVLNL NSLEGIRENA IIMHPLPRVS EISPDIDATK HARYFEQAKN GIPVRMALLC LVCGIKFW //