ID   PYRB_BACHK              Reviewed;         304 AA.
AC   Q6HES5;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   16-JUN-2009, entry version 40.
DE   RecName: Full=Aspartate carbamoyltransferase;
DE            EC=2.1.3.2;
DE   AltName: Full=Aspartate transcarbamylase;
DE            Short=ATCase;
GN   Name=pyrB; OrderedLocusNames=BT9727_3631;
OS   Bacillus thuringiensis subsp. konkukian.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=180856;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=97-27;
RX   PubMed=16621833; DOI=10.1128/JB.188.9.3382-3390.2006;
RA   Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S.,
RA   Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O.,
RA   Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T.,
RA   Goodwin L.A., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA   Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K.,
RA   Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C.,
RA   Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P.,
RA   Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G.,
RA   Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L.,
RA   Brettin T.S., Gilna P.;
RT   "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT   thuringiensis isolates closely related to Bacillus anthracis.";
RL   J. Bacteriol. 188:3382-3390(2006).
CC   -!- CATALYTIC ACTIVITY: Carbamoyl phosphate + L-aspartate = phosphate
CC       + N-carbamoyl-L-aspartate.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; UMP from HCO(3)(-): step 2/6.
CC   -!- SIMILARITY: Belongs to the ATCase/OTCase family.
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DR   EMBL; AE017355; AAT60636.1; -; Genomic_DNA.
DR   RefSeq; YP_037951.1; -.
DR   GeneID; 2855677; -.
DR   GenomeReviews; AE017355_GR; BT9727_3631.
DR   KEGG; btk:BT9727_3631; -.
DR   HOGENOM; Q6HES5; -.
DR   OMA; Q6HES5; RTVVNLF.
DR   BioCyc; BTHU281309:BT9727_3631-MON; -.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR   GO; GO:0004070; F:aspartate carbamoyltransferase activity; IEA:HAMAP.
DR   GO; GO:0006207; P:'de novo' pyrimidine base biosynthetic process; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00001; -; 1.
DR   InterPro; IPR006132; Asp/Orn_carbamoyltranf_P_bd.
DR   InterPro; IPR006130; Asp/Orn_carbamoylTrfase.
DR   InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn_bd.
DR   InterPro; IPR002082; Aspartate_carbamoyltransf_euk.
DR   Pfam; PF00185; OTCace; 1.
DR   Pfam; PF02729; OTCace_N; 1.
DR   PRINTS; PR00100; AOTCASE.
DR   PRINTS; PR00101; ATCASE.
DR   TIGRFAMs; TIGR00670; asp_carb_tr; 1.
DR   PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Pyrimidine biosynthesis; Transferase.
FT   CHAIN         1    304       Aspartate carbamoyltransferase.
FT                                /FTId=PRO_0000113096.
SQ   SEQUENCE   304 AA;  34722 MW;  7E4FE09447EE773E CRC64;
     MSHLLTMSEL SEVEISEILK DAEDFANGKE SKTTEQTFVA NLFFENSTRT RFSFEVAEKR
     LGLDVLNFSA DASSVQKGET LYDTIRTLES IGTKAVVIRH EQDRYFDELK DQVNIPILNA
     GDGCGNHPTQ CLLDLLTIKQ EFGRFEGLKI AIVGDVRHSR VARSNAEALT KLGATIYFAS
     PEEWKDEDNT FGTYKPLDEL VPEVDVMMLL RVQHERHDHY ETDIMKEYHE KHGLTVEREK
     RMKEGSIIMH PAPVNRDVEI ASELVECERS RIFKQMENGV YVRMAVLKRA LPNVLGGMKH
     ELFV
//