ID   PYRB_BRUSU              Reviewed;         322 AA.
AC   P65612; Q8YC62;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-NOV-2008, entry version 29.
DE   RecName: Full=Aspartate carbamoyltransferase;
DE            EC=2.1.3.2;
DE   AltName: Full=Aspartate transcarbamylase;
DE            Short=ATCase;
GN   Name=pyrB; OrderedLocusNames=BRA0599;
OS   Brucella suis.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Brucellaceae; Brucella.
OX   NCBI_TaxID=29461;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330 / Biovar 1;
RX   MEDLINE=22247741; PubMed=12271122; DOI=10.1073/pnas.192319099;
RA   Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA   Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA   Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A.,
RA   Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O.,
RA   Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M.,
RA   Fraser C.M.;
RT   "The Brucella suis genome reveals fundamental similarities between
RT   animal and plant pathogens and symbionts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
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; AE014292; AAN33788.1; -; Genomic_DNA.
DR   RefSeq; NP_699783.1; -.
DR   HSSP; P00479; 3CSU.
DR   GeneID; 1165039; -.
DR   GenomeReviews; AE014292_GR; BRA0599.
DR   KEGG; bms:BRA0599; -.
DR   TIGR; BRA0599; -.
DR   HOGENOM; P65612; -.
DR   BioCyc; BSUI204722:BR_A0599-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; IPR006130; Asp/Orn_carbamoyltranf.
DR   InterPro; IPR006132; Asp/Orn_carbamoyltranf_P_bd.
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    322       Aspartate carbamoyltransferase.
FT                                /FTId=PRO_0000113109.
SQ   SEQUENCE   322 AA;  34802 MW;  81B6208851B9521B CRC64;
     MTNQTVSPLF PHRHLLGIKG LSPLDILCLL DLADQEIAVS RQPEKKKSVL RGRTQINLFF
     EASTRTQSSF ELAGKRLGAD VMNMSVGNSS VKKGETLIDT AMTLNAMQPD ILVIRHASAG
     AAALLAQKVG CSVVNAGDGA HEHPTQALLD ALTIRRAKGQ IENLIVAICG DVLHSRVARS
     NILLLNALGA RVRVVAPSTL LPAGMADMSV EVFNSMEEGL KDADVVMMLR LQRERMAGSF
     VPSVREYFHF YGLDREKLKF AKPDALVMHP GPMNRGVEIA SDVADGPQSV IQQQVEMGVA
     VRMAVMEALL DPRRNPGNGE PA
//