GenomeNet

Database: UniProt
Entry: B9DPM9
LinkDB: B9DPM9
Original site: B9DPM9 
ID   PYRB_STACT              Reviewed;         302 AA.
AC   B9DPM9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   26-NOV-2014, entry version 41.
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};
GN   OrderedLocusNames=Sca_0814;
OS   Staphylococcus carnosus (strain TM300).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus.
OX   NCBI_TaxID=396513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TM300;
RX   PubMed=19060169; DOI=10.1128/AEM.01982-08;
RA   Rosenstein R., Nerz C., Biswas L., Resch A., Raddatz G.,
RA   Schuster S.C., Goetz F.;
RT   "Genome analysis of the meat starter culture bacterium Staphylococcus
RT   carnosus TM300.";
RL   Appl. Environ. Microbiol. 75:811-822(2009).
CC   -!- CATALYTIC ACTIVITY: Carbamoyl phosphate + L-aspartate = phosphate
CC       + N-carbamoyl-L-aspartate. {ECO:0000255|HAMAP-Rule:MF_00001}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; (S)-dihydroorotate from bicarbonate: step 2/3.
CC       {ECO:0000255|HAMAP-Rule:MF_00001}.
CC   -!- SIMILARITY: Belongs to the ATCase/OTCase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00001}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AM295250; CAL27724.1; -; Genomic_DNA.
DR   RefSeq; YP_002633909.1; NC_012121.1.
DR   ProteinModelPortal; B9DPM9; -.
DR   STRING; 396513.Sca_0814; -.
DR   GeneID; 7551999; -.
DR   KEGG; sca:Sca_0814; -.
DR   PATRIC; 19602402; VBIStaCar105558_0815.
DR   eggNOG; COG0540; -.
DR   HOGENOM; HOG000022685; -.
DR   KO; K00609; -.
DR   OMA; NIDIERS; -.
DR   OrthoDB; EOG61KBJZ; -.
DR   BioCyc; SCAR396513:GJ9G-829-MONOMER; -.
DR   UniPathway; UPA00070; UER00116.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR   GO; GO:0004070; F:aspartate carbamoyltransferase activity; IEA:UniProtKB-HAMAP.
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; IPR002082; Asp_carbamoyltransf.
DR   InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd.
DR   Pfam; PF00185; OTCace; 1.
DR   Pfam; PF02729; OTCace_N; 1.
DR   PRINTS; PR00100; AOTCASE.
DR   PRINTS; PR00101; ATCASE.
DR   SUPFAM; SSF53671; SSF53671; 1.
DR   TIGRFAMs; TIGR00670; asp_carb_tr; 1.
DR   PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Pyrimidine biosynthesis; Reference proteome;
KW   Transferase.
FT   CHAIN         1    302       Aspartate carbamoyltransferase.
FT                                /FTId=PRO_1000116157.
SQ   SEQUENCE   302 AA;  34388 MW;  746D4C12CB999999 CRC64;
     MKQLVSMEDL TNEEIYSLIE TAIEYKKGNK PNKFTDKYVS NLFFENSTRT KCSFEMAERQ
     LGLQEIPFET STSSVKKGES LYDTCKTLES IGVDALVIRH PQNDYYKELE GLNIPVINGG
     DGSGQHPTQS LLDIMTIYEE YKDFKDLNVL ICGDIKNSRV ARSNYQALTA LGANVKFAAP
     GEWVDESLDA PYVKIDDVIE ETDIVMLLRV QHERHDGELS FDPHEYHEKY GLTKDRYNRM
     KSEAIVMHPA PVNRGVEIDS DLVEAPKARI FKQMKNGMFL RMSVITHILA EKEEGVIFDV
     AN
//
DBGET integrated database retrieval system