(data stored in SCRATCH zone)

SWISSPROT: A0A0H2ZKY9_PSEAB

ID   A0A0H2ZKY9_PSEAB        Unreviewed;       479 AA.
AC   A0A0H2ZKY9;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   08-MAY-2019, entry version 19.
DE   SubName: Full=Dihydropyrimidinase {ECO:0000313|EMBL:ABJ15408.1};
GN   Name=dhT {ECO:0000313|EMBL:ABJ15408.1};
GN   OrderedLocusNames=PA14_05770 {ECO:0000313|EMBL:ABJ15408.1};
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963 {ECO:0000313|EMBL:ABJ15408.1, ECO:0000313|Proteomes:UP000000653};
RN   [1] {ECO:0000313|EMBL:ABJ15408.1, ECO:0000313|Proteomes:UP000000653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14 {ECO:0000313|EMBL:ABJ15408.1,
RC   ECO:0000313|Proteomes:UP000000653};
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   -!- PTM: Carbamylation allows a single lysine to coordinate two
CC       divalent metal cations. {ECO:0000256|PIRSR:PIRSR611778-50}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000438; ABJ15408.1; -; Genomic_DNA.
DR   RefSeq; WP_003099919.1; NC_008463.1.
DR   SMR; A0A0H2ZKY9; -.
DR   EnsemblBacteria; ABJ15408; ABJ15408; PA14_05770.
DR   KEGG; pau:PA14_05770; -.
DR   KO; K01464; -.
DR   OMA; IDPQVHF; -.
DR   BioCyc; PAER208963:G1G74-478-MONOMER; -.
DR   Proteomes; UP000000653; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
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; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   TIGRFAMs; TIGR02033; D-hydantoinase; 1.
PE   4: Predicted;
DR   PRODOM; A0A0H2ZKY9.
DR   SWISS-2DPAGE; A0A0H2ZKY9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000653}.
FT   DOMAIN       50    436       Amidohydro-rel. {ECO:0000259|Pfam:
FT                                PF01979}.
FT   MOD_RES     150    150       N6-carboxylysine. {ECO:0000256|PIRSR:
FT                                PIRSR611778-50}.
SQ   SEQUENCE   479 AA;  52212 MW;  46582DFE22E38925 CRC64;
     MSLLIRGATV VTHEESYRAD VLCANGLIQA IGENLETPSG CDVLDGGGQY LMPGGIDPHT
     HMQLPFMGTV ASEDFFSGTA AGLAGGTTSI IDFVIPNPRQ SLLEAFHTWR GWAQKSAADY
     GFHVAITWWS DEVAREMGEL VAQHGVNSFK HFMAYKNAIM AADDTLVASF ERCLELGAVP
     TVHAENGELV FHLQQKLLAQ GLTGPEAHPL SRPPQVEGEA ASRAIRIAET LGTPLYLVHI
     SSREALDEIA YARAKGQPVY GEVLAGHLLL DDSVYRHPDW ATAAGYVMSP PFRPVEHQEA
     LWRGLQSGNL HTTATDHCCF CAEQKAMGRD DFSKIPNGTA GIEDRMALLW DAGVNSGRLS
     MHEFVALTST NTAKIFNLFP RKGAIRVGAD ADLVLWDPQG SRTLSAATHH QRVDFNIFEG
     RTVRGIPSHT ISQGKLLWAA GDLRAEPGAG RYVERPAYPS VYEVLGRRAE RQRPVAVER
//

If you have problems or comments...

PBIL Back to PBIL home page