ID   PYRB_STREM              Reviewed;         311 AA.
AC   B4U3B0;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 72.
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=Sez_1125;
OS   Streptococcus equi subsp. zooepidemicus (strain MGCS10565).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=552526;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGCS10565;
RX   PubMed=18716664; DOI=10.1371/journal.pone.0003026;
RA   Beres S.B., Sesso R., Pinto S.W.L., Hoe N.P., Porcella S.F., Deleo F.R.,
RA   Musser J.M.;
RT   "Genome sequence of a lancefield group C Streptococcus zooepidemicus strain
RT   causing epidemic nephritis: new information about an old disease.";
RL   PLoS ONE 3:E3026-E3026(2008).
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; CP001129; ACG62477.1; -; Genomic_DNA.
DR   RefSeq; WP_012515742.1; NC_011134.1.
DR   AlphaFoldDB; B4U3B0; -.
DR   SMR; B4U3B0; -.
DR   EnsemblBacteria; ACG62477; ACG62477; Sez_1125.
DR   KEGG; sez:Sez_1125; -.
DR   HOGENOM; CLU_043846_2_1_9; -.
DR   OMA; FPTEREY; -.
DR   UniPathway; UPA00070; UER00116.
DR   Proteomes; UP000001873; 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_1000088803"
SQ   SEQUENCE   311 AA;  35103 MW;  9753B9C9EFF5BC23 CRC64;
     MSVVNNRVAL KHLVSMEHLT NEEVMGLISR GSEYKAGKVA IKDNSRHFAA NLFFENSTRT
     HKSFEVAENK LGLRVLDFNA DTSAVNKGET LYDTVLTMSA LGTEICVIRH PEDDYYQQLI
     DSPTITASIV NGGDGSGQHP SQCLLDLLTI YEEFGHFDGL KIAIAGDLTH SRVAKSNMQI
     LKRLGAELYF YGPEQWYSSE FDSYGRYMAI DHIIDQLDVL MLLRVQHERH DGSQSFSKED
     YHRQFGLTEE RYRRLKDSAI IMHPAPVNRD VEIADHLVEA PKARIVAQMA NGVFVRMAII
     EAILNGRNEN V