ID   PYRB_STRMU              Reviewed;         308 AA.
AC   Q8DUP5;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 111.
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=SMU_858;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA   Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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; AE014133; AAN58574.1; -; Genomic_DNA.
DR   RefSeq; NP_721268.1; NC_004350.2.
DR   RefSeq; WP_002262007.1; NC_004350.2.
DR   AlphaFoldDB; Q8DUP5; -.
DR   SMR; Q8DUP5; -.
DR   STRING; 210007.SMU_858; -.
DR   PRIDE; Q8DUP5; -.
DR   EnsemblBacteria; AAN58574; AAN58574; SMU_858.
DR   KEGG; smu:SMU_858; -.
DR   PATRIC; fig|210007.7.peg.765; -.
DR   eggNOG; COG0540; Bacteria.
DR   HOGENOM; CLU_043846_2_1_9; -.
DR   OMA; FPTEREY; -.
DR   PhylomeDB; Q8DUP5; -.
DR   UniPathway; UPA00070; UER00116.
DR   Proteomes; UP000002512; 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_0000113205"
SQ   SEQUENCE   308 AA;  34724 MW;  4E0BE19A460B2ED2 CRC64;
     MVVTDGVVSL KHLVSMEILS NEEVLGLIKR GLAFKEKKVT FSLDRQYFAA NLFFEASTRT
     HKSFEVAEKK LGLDVIEFDA KTSSVNKGET LYDTILTMSA LGVDICVVRH SQDDYYKELI
     DSRTIQTSIV NGGDGSGQHP SQCLLDLMTI YDEFASFENL KIAIAGDITH SRVAKSNMQI
     LKRLGAQIYF AGPKEWYSSE FDVYGKYVAI DDIINQIDVM MLLRVQHERH DGKESFSKKA
     YHQHYGLTEE RYKQLKSSAI IMHPAPVNRD VEIADSLVEA PKSRIVAQMK NGVFVRMAIL
     EAILRGKT