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Database: UniProt/SWISS-PROT
Entry: PYRB_RHOOB
LinkDB: PYRB_RHOOB
Original site: PYRB_RHOOB 
ID   PYRB_RHOOB              Reviewed;         314 AA.
AC   C1B4I7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   26-NOV-2014, entry version 38.
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=ROP_69290;
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=632772;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4;
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; AP011115; BAH55176.1; -; Genomic_DNA.
DR   RefSeq; YP_002784121.1; NC_012522.1.
DR   ProteinModelPortal; C1B4I7; -.
DR   STRING; 632772.ROP_69290; -.
DR   EnsemblBacteria; BAH55176; BAH55176; ROP_69290.
DR   GeneID; 7744500; -.
DR   KEGG; rop:ROP_69290; -.
DR   PATRIC; 23231311; VBIRhoOpa21106_7014.
DR   eggNOG; COG0540; -.
DR   HOGENOM; HOG000022685; -.
DR   KO; K00609; -.
DR   OMA; MTVFYEN; -.
DR   OrthoDB; EOG61KBJZ; -.
DR   BioCyc; ROPA632772:GH0Q-6985-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; Transferase.
FT   CHAIN         1    314       Aspartate carbamoyltransferase.
FT                                /FTId=PRO_1000116154.
SQ   SEQUENCE   314 AA;  33669 MW;  8C2E9EB7D6F857C6 CRC64;
     MKHLLSIADL TRESAVELLD EAERFEQALL GREVRKLPTL RGRTVMTVFF ENSTRTRVSF
     EVAGKWMSAD VINVSASSSS VSKGESLRDT AMTLRAAGAD ALIVRHPASG AAHQIASWTG
     RQDDGGPAVI NAGDGTHEHP TQALLDALTL RQRLGDIEGK RIAIVGDILH SRVARSNALL
     LSMLGAEVVL VAPPTLLPVG VSSWPVSVAH SLDAELPGLD AVLMLRVQAE RMNGGFFPSQ
     REYSINYGLS EKRLALLPEH AVVLHPGPML RGMEIASAVA DSTRTAVLQQ VTNGVHMRMA
     VLFRLLVGAE DVAG
//
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