(data stored in ACNUC7421 zone)

SWISSPROT: B2UHS5_RALPJ

ID   B2UHS5_RALPJ            Unreviewed;       471 AA.
AC   B2UHS5;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAY-2019, entry version 63.
DE   SubName: Full=Dihydropyrimidinase {ECO:0000313|EMBL:ACD29126.1};
DE            EC=3.5.2.2 {ECO:0000313|EMBL:ACD29126.1};
GN   OrderedLocusNames=Rpic_4022 {ECO:0000313|EMBL:ACD29126.1};
OS   Ralstonia pickettii (strain 12J).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=402626 {ECO:0000313|EMBL:ACD29126.1, ECO:0000313|Proteomes:UP000002566};
RN   [1] {ECO:0000313|Proteomes:UP000002566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12J {ECO:0000313|Proteomes:UP000002566};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Marsh T., Richardson P.;
RT   "Complete sequence of chromosome 2 of Ralstonia pickettii 12J.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- PTM: Carbamylation allows a single lysine to coordinate two
CC       divalent metal cations. {ECO:0000256|PIRSR:PIRSR611778-50}.
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DR   EMBL; CP001069; ACD29126.1; -; Genomic_DNA.
DR   RefSeq; WP_012430131.1; NC_010678.1.
DR   STRING; 402626.Rpic_4022; -.
DR   EnsemblBacteria; ACD29126; ACD29126; Rpic_4022.
DR   GeneID; 6285328; -.
DR   KEGG; rpi:Rpic_4022; -.
DR   PATRIC; fig|402626.5.peg.266; -.
DR   eggNOG; ENOG4105CD3; Bacteria.
DR   eggNOG; COG0044; LUCA.
DR   HOGENOM; HOG000219145; -.
DR   KO; K01464; -.
DR   OMA; YVCSPPP; -.
DR   OrthoDB; 906155at2; -.
DR   BioCyc; RPIC402626:GH94-4022-MONOMER; -.
DR   Proteomes; UP000002566; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004157; F:dihydropyrimidinase activity; IEA:UniProtKB-EC.
DR   CDD; cd01314; D-HYD; 1.
DR   Gene3D; 2.30.40.10; -; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR011778; Hydantoinase/dihydroPyrase.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51338; SSF51338; 2.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   TIGRFAMs; TIGR02033; D-hydantoinase; 1.
PE   4: Predicted;
DR   PRODOM; B2UHS5.
DR   SWISS-2DPAGE; B2UHS5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002566};
KW   Hydrolase {ECO:0000313|EMBL:ACD29126.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002566}.
FT   DOMAIN       53    445       Amidohydro-rel. {ECO:0000259|Pfam:
FT                                PF01979}.
FT   MOD_RES     154    154       N6-carboxylysine. {ECO:0000256|PIRSR:
FT                                PIRSR611778-50}.
SQ   SEQUENCE   471 AA;  51350 MW;  28AD842F0472B920 CRC64;
     MSTELDLVIR NADVVTASDR FTCDIGVRDG RIAVLGNGLP RGVRELDASG LLALPGGVDG
     HCHLDQPMPD GMRMADDFFT GTRAAICGGT TTVIPFAAQE KGGSLKAAVA DYHRRAEGRA
     VADYGFHLIV ADPTPEVLKH ELPELIHQGY TSFKVYMTYD DLKLSDREML DVLDVAKQNN
     ALVMVHAENA DCISWLTEKL VGEGRISPRF HGLSRPAAVE REATHRAITF AELVDVPILI
     VHVSGKEAIE QIRWAQSRGL QILAETCPQY LYLTAEDMGL HGDDGYEGAK CVCSPPPRDP
     ENQAAVWRAL AGGVFSVFSS DHAPFNYDDA QGKKLGGLAQ PFDHIPNGVP GIETRLPLLF
     DGIARGKLSL HQFVELTSYR PARLYGLYPR KGTIAVGADA DITLWDPERR VRITNDALHH
     AVDYTPYEGI EVTGWPVHCF SRGELLVENG KYLEPAPGRG QFLPAGAPSL V
//

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