ID   PYRB_BACAH              Reviewed;         306 AA.
AC   A0RHR1;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   16-JUN-2009, entry version 22.
DE   RecName: Full=Aspartate carbamoyltransferase;
DE            EC=2.1.3.2;
DE   AltName: Full=Aspartate transcarbamylase;
DE            Short=ATCase;
GN   Name=pyrB; OrderedLocusNames=BALH_3519;
OS   Bacillus thuringiensis (strain Al Hakam).
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=412694;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17337577; DOI=10.1128/JB.00241-07;
RA   Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N.,
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., Green L.D., Han C.S., Hill K.K., Hitchcock P.,
RA   Jackson P.J., Keim P., Kewalramani A.R., Longmire J., Lucas S.,
RA   Malfatti S., Martinez D., McMurry K., Meincke L.J., Misra M.,
RA   Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B.,
RA   Reilly L.P., Richardson P., Robinson D.L., Saunders E., Tapia R.,
RA   Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O.,
RA   Wills P.L., Gilna P., Brettin T.S.;
RT   "The complete genome sequence of Bacillus thuringiensis Al Hakam.";
RL   J. Bacteriol. 189:3680-3681(2007).
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; CP000485; ABK86754.1; -; Genomic_DNA.
DR   RefSeq; YP_896261.1; -.
DR   GeneID; 4544127; -.
DR   GenomeReviews; CP000485_GR; BALH_3519.
DR   KEGG; btl:BALH_3519; -.
DR   NMPDR; fig|412694.5.peg.3379; -.
DR   OMA; A0RHR1; RTVVNLF.
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    306       Aspartate carbamoyltransferase.
FT                                /FTId=PRO_0000321073.
SQ   SEQUENCE   306 AA;  34921 MW;  2B20448D32C2D60C CRC64;
     MTMSHLLTMS ELSEVEISEI LKDAEDFANG KESKTTEQTF VANLFFENST RTRFSFEVAE
     KRLGLDVLNF SADASSVQKG ETLYDTIRTL ESIGTKAVVI RHEQDRYFDE LKDQVNIPIL
     NAGDGCGNHP TQCLLDLLTI KQEFGRFEGL QIAIVGDVRH SRVARSNAEA LTKLGATIYF
     ASPEEWKDED NTFGTYKPLD ELVPEVDVMM LLRVQHERHD HYETDIMKEY HEKHGLTVER
     EKRMKEGSII MHPAPVNRDV EIASELVECE RSRIFKQMEN GVYVRMAVLK RALPNVLGGM
     KHELLV
//