ID   I3TRN0_TISMK            Unreviewed;       501 AA.
AC   I3TRN0;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=D-aminoacylase {ECO:0000313|EMBL:AFK55418.1};
GN   OrderedLocusNames=TMO_a0015 {ECO:0000313|EMBL:AFK55418.1};
OS   Tistrella mobilis (strain KA081020-065).
OG   Plasmid pTM1 {ECO:0000313|EMBL:AFK55418.1,
OG   ECO:0000313|Proteomes:UP000005258}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Geminicoccales;
OC   Geminicoccaceae; Tistrella.
OX   NCBI_TaxID=1110502 {ECO:0000313|EMBL:AFK55418.1, ECO:0000313|Proteomes:UP000005258};
RN   [1] {ECO:0000313|EMBL:AFK55418.1, ECO:0000313|Proteomes:UP000005258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KA081020-065 {ECO:0000313|Proteomes:UP000005258};
RC   PLASMID=Plasmid pTM1 {ECO:0000313|Proteomes:UP000005258};
RX   PubMed=22458477; DOI=10.1021/ja301735a;
RA   Xu Y., Kersten R.D., Nam S.J., Lu L., Al-Suwailem A.M., Zheng H.,
RA   Fenical W., Dorrestein P.C., Moore B.S., Qian P.Y.;
RT   "Bacterial biosynthesis and maturation of the didemnin anti-cancer
RT   agents.";
RL   J. Am. Chem. Soc. 134:8625-8632(2012).
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DR   EMBL; CP003237; AFK55418.1; -; Genomic_DNA.
DR   RefSeq; WP_014747095.1; NC_017957.2.
DR   AlphaFoldDB; I3TRN0; -.
DR   KEGG; tmo:TMO_a0015; -.
DR   PATRIC; fig|1110502.3.peg.3672; -.
DR   HOGENOM; CLU_016107_3_0_5; -.
DR   Proteomes; UP000005258; Plasmid pTM1.
DR   GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR   Gene3D; 3.30.1490.130; D-aminoacylase. Domain 3; 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; IPR013108; Amidohydro_3.
DR   InterPro; IPR023100; D-aminoacylase_insert_dom_sf.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   PANTHER; PTHR43668; ALLANTOINASE; 1.
DR   PANTHER; PTHR43668:SF2; ALLANTOINASE; 1.
DR   Pfam; PF07969; Amidohydro_3; 2.
DR   SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE   4: Predicted;
KW   Plasmid {ECO:0000313|EMBL:AFK55418.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005258}.
FT   DOMAIN          48..247
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
FT   DOMAIN          250..480
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   501 AA;  52842 MW;  6F0E2E08DD6A4FF0 CRC64;
     MADAAVFDLV IRGGRVVDPE TGHDAVADVG ITGDRIAAIG PALAAGRREI DAAGLVVAPG
     FIDLHAHGQS IPADRMQAFD GVTTALELEV GALPVGAWYD HQQAAGRVLN YGAAAAWLFA
     RKAAMIGLDL NSGLPPIAMM GAGAGDMRWS VDAATPAQTE TIVDLTRRGL DEGALGIGIP
     HGYASGAGLK EMSRICALAA AYDRPTYTHI AYMSNIDPRS SVQAYVQLIG LAGATGAHMH
     ICHLNSTSLR DIEEAAGLIR TAQAQGLPVT TEAYPYGTGS TVLSAGFFME SDFAERTGTG
     YGAIEVVSTG RRFGNRDELA AARAEAPEAL VLWHFLDTDD PHDTKLLDIS VTFPGGAIAS
     DAVPWSNPDG SLYDGDAWPL PADKSSHPRS SGTFTRFLAQ WVREREVVPL VEAMAKCSLI
     PAQIVESCSS AFRRKGRLQP GCDADIVVFD LARVQDRATF EAMHLPAEGM VHVLVNGEAV
     IADGALVTEA RPGRPIRSDP R
//