ID B2TEV8_PARPJ Unreviewed; 473 AA. AC B2TEV8; DT 01-JUL-2008, integrated into UniProtKB/TrEMBL. DT 01-JUL-2008, sequence version 1. DT 27-MAR-2024, entry version 85. DE SubName: Full=Dihydropyrimidinase {ECO:0000313|EMBL:ACD18629.1}; DE EC=3.5.2.2 {ECO:0000313|EMBL:ACD18629.1}; GN OrderedLocusNames=Bphyt_4250 {ECO:0000313|EMBL:ACD18629.1}; OS Paraburkholderia phytofirmans (strain DSM 17436 / LMG 22146 / PsJN) OS (Burkholderia phytofirmans). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Paraburkholderia. OX NCBI_TaxID=398527 {ECO:0000313|EMBL:ACD18629.1, ECO:0000313|Proteomes:UP000001739}; RN [1] {ECO:0000313|EMBL:ACD18629.1, ECO:0000313|Proteomes:UP000001739} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17436 / LMG 22146 / PsJN RC {ECO:0000313|Proteomes:UP000001739}; RX PubMed=21551308; DOI=10.1128/JB.05055-11; RA Weilharter A., Mitter B., Shin M.V., Chain P.S., Nowak J., Sessitsch A.; RT "Complete genome sequence of the plant growth-promoting endophyte RT Burkholderia phytofirmans strain PsJN."; RL J. Bacteriol. 193:3383-3384(2011). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|ARBA:ARBA00001947}; CC -!- PTM: Carbamylation allows a single lysine to coordinate two divalent CC metal cations. {ECO:0000256|PIRSR:PIRSR611778-50}. CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. CC Hydantoinase/dihydropyrimidinase family. CC {ECO:0000256|ARBA:ARBA00008829}. 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; CP001053; ACD18629.1; -; Genomic_DNA. DR RefSeq; WP_012426145.1; NC_010676.1. DR AlphaFoldDB; B2TEV8; -. DR STRING; 398527.Bphyt_4250; -. DR MEROPS; M38.973; -. DR KEGG; bpy:Bphyt_4250; -. DR eggNOG; COG0044; Bacteria. DR HOGENOM; CLU_015572_2_2_4; -. DR OrthoDB; 5687299at2; -. DR Proteomes; UP000001739; 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; 3.20.20.140; Metal-dependent hydrolases; 1. DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1. DR InterPro; IPR006680; Amidohydro-rel. DR InterPro; IPR011778; Hydantoinase/dihydroPyrase. DR InterPro; IPR011059; Metal-dep_hydrolase_composite. DR InterPro; IPR032466; Metal_Hydrolase. DR NCBIfam; TIGR02033; D-hydantoinase; 1. DR PANTHER; PTHR11647:SF99; D-PHENYLHYDANTOINASE-RELATED; 1. DR PANTHER; PTHR11647; HYDRANTOINASE/DIHYDROPYRIMIDINASE FAMILY MEMBER; 1. DR Pfam; PF01979; Amidohydro_1; 1. DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 2. DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1. PE 3: Inferred from homology; KW Hydrolase {ECO:0000313|EMBL:ACD18629.1}. FT DOMAIN 50..437 FT /note="Amidohydrolase-related" FT /evidence="ECO:0000259|Pfam:PF01979" FT MOD_RES 150 FT /note="N6-carboxylysine" FT /evidence="ECO:0000256|PIRSR:PIRSR611778-50" SQ SEQUENCE 473 AA; 50711 MW; 9EE75817D091C889 CRC64; MSVLIRGGVV VNADGETRAD VLCEKGRIVA VGTGLAAGAD TEVIDAGGQY VMPGGIDPHT HMQLPFMGTV TADDFFTGTA AGLAGGTTTI MDFVIPSPQE SLMGAFKKWR GWAEQACSDY TFHVAVTWWD ESVHADMGTL VNQHGVNSFK HFMAYKNAIM ADDEILVKSF RRALELGAVP TVHAENGELV FQLQQELLQA GVTGPQAHPL SRPPVVETEA VQRAIAIANV MNTPLYIVHV SCAESVEAIA LARSRGQRVF GEALAGHLVI DDSVYTHPDF DFAAGHVMSP PFRSKAHQAA LWNGLQAGSL HTTATDHCTF CAAQKATGRD DFTRIPNGCG GVEDRMSVIW DTGVNGGRLT PSEFVKVTSA NVAQIFNMYP RKGVIAVGAD ADVVVWDPEA TRTISARTQH ARGGFNVFEG RVVRGNPSHT VSNGKVVYAQ GDLRAVKGAG RYVERKPFGP IFDALQRKRQ SAA //