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Database: UniProt
Entry: A5FWH1
LinkDB: A5FWH1
Original site: A5FWH1 
ID   PYRB_ACICJ              Reviewed;         311 AA.
AC   A5FWH1;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   29-OCT-2014, entry version 50.
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=Acry_0733;
OS   Acidiphilium cryptum (strain JF-5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acidiphilium.
OX   NCBI_TaxID=349163;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JF-5;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Sims D., Brettin T., Bruce D., Han C., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Magnuson T.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Acidiphilium cryptum JF-5.";
RL   Submitted (MAY-2007) 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; CP000697; ABQ29953.1; -; Genomic_DNA.
DR   RefSeq; WP_011941735.1; NC_009484.1.
DR   RefSeq; YP_001233872.1; NC_009484.1.
DR   ProteinModelPortal; A5FWH1; -.
DR   STRING; 349163.Acry_0733; -.
DR   EnsemblBacteria; ABQ29953; ABQ29953; Acry_0733.
DR   GeneID; 5162211; -.
DR   KEGG; acr:Acry_0733; -.
DR   PATRIC; 20646444; VBIAciCry6074_1221.
DR   eggNOG; COG0540; -.
DR   HOGENOM; HOG000022685; -.
DR   KO; K00609; -.
DR   OMA; MTLNAMR; -.
DR   OrthoDB; EOG61KBJZ; -.
DR   BioCyc; ACRY349163:GHET-743-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    311       Aspartate carbamoyltransferase.
FT                                /FTId=PRO_0000321059.
SQ   SEQUENCE   311 AA;  33475 MW;  16FFB92DF2154AE2 CRC64;
     MRLPTRHLLG IEGLHPRDIS ALLDLAESYV LLNRSGKTRR DVLRGRTLIN LFFEDSTRTR
     TSFELAGKRL GADVINMSVS TSSVSKGETL LDTAATLNAM NCDLLVVRHK ASGAPALLAQ
     KVDAAVINAG DGMHEHPTQA LLDALTIRRN KGTLAGLTVA ICGDIAHSRV ARSNLLLLTA
     MGSRVRVVGP PTLIPSGIDQ FGATVFHDMR EGLRDADIVM ALRLQTERMS AGLIPSAREF
     FTFYGLDAAK LAMAKPDALV MHPGPMNRGV EIDSQVADDA TRSVIREQVE MGVAIRMAVL
     DVLARTALAH A
//
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