ID   PYRB_ECOL5              Reviewed;         311 AA.
AC   Q0T9E3;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Aspartate carbamoyltransferase {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}; OrderedLocusNames=ECP_4495;
OS   Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=362663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=536 / UPEC;
RX   PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA   Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA   Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT   "Role of pathogenicity island-associated integrases in the genome
RT   plasticity of uropathogenic Escherichia coli strain 536.";
RL   Mol. Microbiol. 61:584-595(2006).
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   -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC       superfamily. ATCase family. {ECO:0000255|HAMAP-Rule:MF_00001}.
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DR   EMBL; CP000247; ABG72436.1; -; Genomic_DNA.
DR   RefSeq; WP_000013046.1; NC_008253.1.
DR   AlphaFoldDB; Q0T9E3; -.
DR   SMR; Q0T9E3; -.
DR   STRING; 362663.ECP_4495; -.
DR   EnsemblBacteria; ABG72436; ABG72436; ECP_4495.
DR   GeneID; 66671836; -.
DR   KEGG; ecp:ECP_4495; -.
DR   HOGENOM; CLU_043846_1_2_6; -.
DR   OMA; FPTEREY; -.
DR   UniPathway; UPA00070; UER00116.
DR   Proteomes; UP000009182; 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:cellular amino acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.1370; -; 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   PANTHER; PTHR11405:SF16; PTHR11405:SF16; 1.
DR   Pfam; PF00185; OTCace; 1.
DR   Pfam; PF02729; OTCace_N; 1.
DR   PRINTS; PR00100; AOTCASE.
DR   SUPFAM; SSF53671; SSF53671; 1.
DR   TIGRFAMs; TIGR00670; asp_carb_tr; 1.
DR   PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
PE   3: Inferred from homology;
KW   Pyrimidine biosynthesis; Transferase.
FT   CHAIN           1..311
FT                   /note="Aspartate carbamoyltransferase"
FT                   /id="PRO_0000301574"
SQ   SEQUENCE   311 AA;  34427 MW;  CC2F5ACBD73E0E3E CRC64;
     MANPLYQKHI ISINDLSRDD LNLVLATAAK LKANPQPELL KHKVIASCFF EASTRTRLSF
     ETSMHRLGAS VVGFSDSANT SLGKKGETLA DTISVISTYV DAIVMRHPQE GAARLATEFS
     GNVPVLNAGD GSNQHPTQTL LDLFTIQETQ GRLDNLHVAM VGDLKYGRTV HSLTQALAKF
     DGNRFYFIAP DALAMPQYIL DMLDEKGIAW SLHSSIEEVM AEVDILYMTR VQKERLDPSE
     YANVKAQFVL RASDLHNAKA NMKVLHPLPR VDEIATDVDK TPHAWYFQQA GNGIFARQAL
     LALVLNRDLV L