ID A3PEX5_PROM0 Unreviewed; 264 AA. AC A3PEX5; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 03-APR-2007, sequence version 1. DT 02-SEP-2026, entry version 96. DE RecName: Full=D-aminoacyl-tRNA deacylase {ECO:0000256|HAMAP-Rule:MF_02048}; DE EC=3.1.1.96 {ECO:0000256|HAMAP-Rule:MF_02048}; GN Name=tatD {ECO:0000313|EMBL:ABO18300.1}; GN Synonyms=dtd3 {ECO:0000256|HAMAP-Rule:MF_02048}; GN OrderedLocusNames=P9301_16771 {ECO:0000313|EMBL:ABO18300.1}; OS Prochlorococcus marinus (strain MIT 9301). OC Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Synechococcales; OC Prochlorococcaceae; Prochlorococcus. OX NCBI_TaxID=167546 {ECO:0000313|EMBL:ABO18300.1, ECO:0000313|Proteomes:UP000001430}; RN [1] {ECO:0000313|EMBL:ABO18300.1, ECO:0000313|Proteomes:UP000001430} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MIT 9301 {ECO:0000313|EMBL:ABO18300.1, RC ECO:0000313|Proteomes:UP000001430}; RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231; RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., RA Richardson P., Chisholm S.W.; RT "Patterns and implications of gene gain and loss in the evolution of RT Prochlorococcus."; RL PLoS Genet. 3:2515-2528(2007). CC -!- FUNCTION: Catalyzes the hydrolysis of D-tyrosyl-tRNA(Tyr). CC {ECO:0000256|HAMAP-Rule:MF_02048}. CC -!- CATALYTIC ACTIVITY: CC Reaction=D-tyrosyl-tRNA(Tyr) + H2O = D-tyrosine + tRNA(Tyr); CC Xref=Rhea:RHEA:25347, Rhea:RHEA-COMP:9707, Rhea:RHEA-COMP:9872, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:58570, ChEBI:CHEBI:78442, CC ChEBI:CHEBI:78723; Evidence={ECO:0000256|HAMAP-Rule:MF_02048}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a D-aminoacyl-tRNA + H2O = a tRNA + a D-alpha-amino acid + CC H(+); Xref=Rhea:RHEA:13953, Rhea:RHEA-COMP:10123, Rhea:RHEA- CC COMP:10124, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:59871, CC ChEBI:CHEBI:78442, ChEBI:CHEBI:79333; EC=3.1.1.96; CC Evidence={ECO:0000256|HAMAP-Rule:MF_02048}; CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000256|HAMAP-Rule:MF_02048}; CC Note=Binds 2 divalent metal cations per subunit. {ECO:0000256|HAMAP- CC Rule:MF_02048}; CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. CC TatD-type hydrolase family. DTD3 subfamily. {ECO:0000256|HAMAP- CC Rule:MF_02048}. 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; CP000576; ABO18300.1; -; Genomic_DNA. DR RefSeq; WP_011863597.1; NC_009091.1. DR AlphaFoldDB; A3PEX5; -. DR STRING; 167546.P9301_16771; -. DR KEGG; pmg:P9301_16771; -. DR eggNOG; COG0084; Bacteria. DR HOGENOM; CLU_031506_4_0_3; -. DR OrthoDB; 9810005at2; -. DR Proteomes; UP000001430; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0051500; F:D-tyrosyl-tRNA(Tyr) deacylase activity; IEA:RHEA. DR GO; GO:0004536; F:DNA nuclease activity; IEA:InterPro. DR GO; GO:0019478; P:D-amino acid catabolic process; IEA:UniProtKB-UniRule. DR CDD; cd01310; TatD_DNAse; 1. DR FunFam; 3.20.20.140:FF:000005; TatD family hydrolase; 1. DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1. DR HAMAP; MF_02048; Deacylase_DTD3; 1. DR InterPro; IPR033665; Deacylase_DTD3. DR InterPro; IPR032466; Metal_Hydrolase. DR InterPro; IPR001130; TatD-like. DR InterPro; IPR015991; TatD/YcfH-like. DR NCBIfam; TIGR00010; YchF/TatD family DNA exonuclease; 1. DR PANTHER; PTHR46124; D-AMINOACYL-TRNA DEACYLASE; 1. DR PANTHER; PTHR46124:SF2; D-AMINOACYL-TRNA DEACYLASE; 1. DR Pfam; PF01026; TatD_DNase; 1. DR PIRSF; PIRSF005902; DNase_TatD; 1. DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1. PE 3: Inferred from homology; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_02048}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_02048}; Reference proteome {ECO:0000313|Proteomes:UP000001430}. FT BINDING 10 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02048, FT ECO:0000256|PIRSR:PIRSR005902-1" FT BINDING 12 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02048, FT ECO:0000256|PIRSR:PIRSR005902-1" FT BINDING 97 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02048, FT ECO:0000256|PIRSR:PIRSR005902-1" FT BINDING 97 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02048" FT BINDING 132 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02048, FT ECO:0000256|PIRSR:PIRSR005902-1" FT BINDING 159 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02048, FT ECO:0000256|PIRSR:PIRSR005902-1" FT BINDING 209 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02048, FT ECO:0000256|PIRSR:PIRSR005902-1" SQ SEQUENCE 264 AA; 30175 MW; 797954D223473712 CRC64; MSNIELIDSH CHLIFENFER DLEDVVSRLR SKGIKKLVHA CCELTEIPKL KKISHEFNEI YYSVGLHPLE AKKWEQSSKS LLRKSALEDR RVVAIGELGL DFFKNENKTQ QIEALIPQME LAYELKLPVI IHCRDAANEM IEICSDLSNK GKCPDGVLHC WTGTPNEMKQ FLDLGFYISF SGIVTFPKAH EIHECAKIVP NDKYLIETDS PFLAPVPHRG KRNEPAFVEN VAKFMADLRS TELNTIAKES SKNAEDLFKF DLLI //