(data stored in ACNUC7421 zone)

SWISSPROT: PYRB_PSEAB

ID   PYRB_PSEAB              Reviewed;         334 AA.
AC   Q02U10;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   07-JUN-2017, entry version 64.
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=PA14_05260;
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14;
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
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}.
DR   EMBL; CP000438; ABJ15369.1; -; Genomic_DNA.
DR   RefSeq; WP_003084569.1; NC_008463.1.
DR   ProteinModelPortal; Q02U10; -.
DR   SMR; Q02U10; -.
DR   EnsemblBacteria; ABJ15369; ABJ15369; PA14_05260.
DR   KEGG; pau:PA14_05260; -.
DR   HOGENOM; HOG000022685; -.
DR   KO; K00609; -.
DR   OMA; WCDVANM; -.
DR   UniPathway; UPA00070; UER00116.
DR   Proteomes; UP000000653; Chromosome.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR   GO; GO:0004070; F:aspartate carbamoyltransferase activity; IEA:UniProtKB-EC.
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   PANTHER; PTHR11405:SF53; PTHR11405:SF53; 1.
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;
DR   PRODOM; Q02U10.
DR   SWISS-2DPAGE; Q02U10.
KW   Complete proteome; Pyrimidine biosynthesis; Transferase.
FT   CHAIN         1    334       Aspartate carbamoyltransferase.
FT                                /FTId=PRO_0000301607.
SQ   SEQUENCE   334 AA;  36629 MW;  2DC90450FA2E42E9 CRC64;
     MPTDAKRPLQ LNDQGQLRHF ISLDGLPREL LTEILDTADS FLEVGARAVK KVPLLRGKTV
     CNVFFENSTR TRTTFELAAQ RLSADVISLN VSTSSTSKGE TLTDTLRNLE AMAADMFVVR
     HSDSGAAHFI AEHVSPNVAV INGGDGRHAH PTQGMLDMLT IRRHKGNFEQ LSVAIVGDIL
     HSRVARSNML ALKTLGCPDI RVIAPRTLLP IGLEEQYGVR VFTNADEGLK DVDVVIMLRL
     QRERMQGGLL PSEGEFFKLY GLTEKRLKLA KPDAIVMHPG PINRGVEIES AVADGAQSVI
     LNQVTYGIAI RMAVLSMAMS GQNTQRQLEQ EDAE
//

If you have problems or comments...

PBIL Back to PBIL home page