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Database: UniProt/TrEMBL
Entry: G2N9D5_9ACTO
LinkDB: G2N9D5_9ACTO
Original site: G2N9D5_9ACTO 
ID   G2N9D5_9ACTO            Unreviewed;       335 AA.
AC   G2N9D5;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   11-JUN-2014, entry version 17.
DE   RecName: Full=Aspartate carbamoyltransferase;
DE            EC=2.1.3.2;
DE   AltName: Full=Aspartate transcarbamylase;
GN   Name=pyrB; ORFNames=SACTE_0891;
OS   Streptomyces sp. SirexAA-E.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Streptomycineae; Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=862751;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SirexAA-E;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Davenport K., Detter J.C., Han C.,
RA   Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I.,
RA   Adams A., Raffa K., Adams S., Book A., Currie C., Woyke T.;
RT   "Complete sequence of Streptomyces sp. SirexAA-E.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SirexAA-E;
RX   PubMed=24710170;
RA   Takasuka T.E., Acheson J.F., Bianchetti C.M., Prom B.M.,
RA   Bergeman L.F., Book A.J., Currie C.R., Fox B.G.;
RT   "Biochemical Properties and Atomic Resolution Structure of a
RT   Proteolytically Processed beta-Mannanase from Cellulolytic
RT   Streptomyces sp. SirexAA-E.";
RL   PLoS ONE 9:E94166-E94166(2014).
CC   -!- CATALYTIC ACTIVITY: Carbamoyl phosphate + L-aspartate = phosphate
CC       + N-carbamoyl-L-aspartate.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; (S)-dihydroorotate from bicarbonate: step 2/3.
CC   -!- SIMILARITY: Belongs to the ATCase/OTCase family.
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DR   EMBL; CP002993; AEN08820.1; -; Genomic_DNA.
DR   RefSeq; YP_004801360.1; NC_015953.1.
DR   ProteinModelPortal; G2N9D5; -.
DR   EnsemblBacteria; AEN08820; AEN08820; SACTE_0891.
DR   GeneID; 11103393; -.
DR   KEGG; ssx:SACTE_0891; -.
DR   KO; K00609; -.
DR   BioCyc; SSP862751:GHMW-895-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.
SQ   SEQUENCE   335 AA;  36035 MW;  31AD7AF45010CA9A CRC64;
     MLRSPGGNPR HLISAADLTR DDAVLILDTA EEMARVADRP IKKLPTLRGR TVVNLFFEDS
     TRTRISFEAA AKRLSADVIN FSAKGSSVSK GESLKDTALT LEAMGADAVV IRHGSSGAPY
     RLATSGWIDG AVVNAGDGTH EHPTQALLDA FTIRRRLVGA DAGLGKDLDG RRVTIVGDIL
     HSRVARSNVH LLTTLGAQVT LVAPPTLVPV GVERWPCEVS YSLDDVLPAS DAVMMLRVQR
     ERMNAAYFPT EREYSRRYGL DGLRMAKMPE HAVVMHPGPM NRGMEITAEV ADSGRCTAVE
     QVANGVSVRM AVLYLLLGGS ETALPSAAAR TEENK
//
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