ID   PYRB_ECO57              Reviewed;         311 AA.
AC   P0A788; P00479; Q47555; Q47557;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Aspartate carbamoyltransferase catalytic subunit;
DE            EC=2.1.3.2;
DE   AltName: Full=Aspartate transcarbamylase;
DE            Short=ATCase;
GN   Name=pyrB; OrderedLocusNames=Z5856, ECs5222;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       (S)-dihydroorotate from bicarbonate: step 2/3.
CC   -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC       superfamily. ATCase family. {ECO:0000305}.
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DR   EMBL; AE005174; AAG59443.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB38645.1; -; Genomic_DNA.
DR   PIR; F91281; F91281.
DR   RefSeq; NP_313249.1; NC_002695.1.
DR   RefSeq; WP_000013046.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; P0A788; -.
DR   SMR; P0A788; -.
DR   STRING; 155864.EDL933_5595; -.
DR   EnsemblBacteria; AAG59443; AAG59443; Z5856.
DR   EnsemblBacteria; BAB38645; BAB38645; ECs_5222.
DR   GeneID; 66671836; -.
DR   GeneID; 913842; -.
DR   KEGG; ece:Z5856; -.
DR   KEGG; ecs:ECs_5222; -.
DR   PATRIC; fig|386585.9.peg.5461; -.
DR   eggNOG; COG0540; Bacteria.
DR   HOGENOM; CLU_043846_1_2_6; -.
DR   OMA; FPTEREY; -.
DR   UniPathway; UPA00070; UER00116.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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; Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..311
FT                   /note="Aspartate carbamoyltransferase catalytic subunit"
FT                   /id="PRO_0000113129"
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