ID   PYRB_ENTFA              Reviewed;         308 AA.
AC   Q9L4T8;
DT   01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Aspartate carbamoyltransferase;
DE            EC=2.1.3.2;
DE   AltName: Full=Aspartate transcarbamylase;
DE            Short=ATCase;
GN   Name=pyrB; OrderedLocusNames=EF_1719;
OS   Enterococcus faecalis (strain ATCC 700802 / V583).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=226185;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 19433 / DSM 20478 / JCM 8726 / NBRC 100481 / NCIMB 775;
RA   Cooke P.A., Shanley M.S., O'Donovan G.A.;
RT   "Enterococcus faecalis pyrimidine biosynthetic gene (pyrB) encoding
RT   aspartate transcarbamoylase.";
RL   Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700802 / V583;
RX   PubMed=12663927; DOI=10.1126/science.1080613;
RA   Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA   Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA   Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA   DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA   Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA   Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT   "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT   faecalis.";
RL   Science 299:2071-2074(2003).
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; AF264709; AAF72727.1; -; Genomic_DNA.
DR   EMBL; AE016830; AAO81495.1; -; Genomic_DNA.
DR   RefSeq; NP_815425.1; NC_004668.1.
DR   RefSeq; WP_002357411.1; NZ_KE136528.1.
DR   AlphaFoldDB; Q9L4T8; -.
DR   SMR; Q9L4T8; -.
DR   STRING; 226185.EF_1719; -.
DR   EnsemblBacteria; AAO81495; AAO81495; EF_1719.
DR   GeneID; 60894015; -.
DR   KEGG; efa:EF1719; -.
DR   PATRIC; fig|226185.45.peg.1793; -.
DR   eggNOG; COG0540; Bacteria.
DR   HOGENOM; CLU_043846_2_1_9; -.
DR   OMA; FPTEREY; -.
DR   SABIO-RK; Q9L4T8; -.
DR   UniPathway; UPA00070; UER00116.
DR   Proteomes; UP000001415; 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   CHAIN           1..308
FT                   /note="Aspartate carbamoyltransferase"
FT                   /id="PRO_0000113133"
SQ   SEQUENCE   308 AA;  34980 MW;  3472C9C8780C3624 CRC64;
     MIITSERISL KHLLTAEALT DREVMGLIRR AGEFKQGAKW HPEERQYFAT NLFFENSTRT
     HKSFEVAEKK LGLEVIEFEA SRSSVQKGET LYDTVLTMSA IGVDVAVIRH GKENYYDELI
     QSKTIQCSII NGGDGSGQHP TQCLLDLMTI YEEFGGFEGL KVAIVGDITH SRVAKSNMQL
     LNRLGAEIYF SGPEEWYDHQ FDVYGQYVPL DEIVEKVDVM MLLRVQHERH DGKESFSKEG
     YHLEYGLTNE RATRLQKHAI IMHPAPVNRD VELADELVES LQSRIVAQMS NGVFMRMAIL
     EAILHGKA