ID Q9AGH8_ALCFA Unreviewed; 484 AA. AC Q9AGH8; DT 01-JUN-2001, integrated into UniProtKB/TrEMBL. DT 01-JUN-2001, sequence version 1. DT 27-MAR-2024, entry version 95. DE SubName: Full=D-aminoacylase {ECO:0000313|EMBL:AAK15530.1}; DE EC=3.5.1.81 {ECO:0000313|EMBL:AAK15530.1}; OS Alcaligenes faecalis. OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Alcaligenes. OX NCBI_TaxID=511 {ECO:0000313|EMBL:AAK15530.1}; RN [1] {ECO:0000313|EMBL:AAK15530.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=12381838; DOI=10.1110/ps.0220902; RA Hsu C.S., Lai W.L., Chang W.W., Liaw S.H., Tsai Y.C.; RT "Structural-based mutational analysis of D-aminoacylase from Alcaligenes RT faecalis DA1."; RL Protein Sci. 11:2545-2550(2002). RN [2] {ECO:0007829|PDB:1M7J} RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH ZINC. RX PubMed=12454005; DOI=10.1074/jbc.M210795200; RA Liaw S.H., Chen S.J., Ko T.P., Hsu C.S., Chen C.J., Wang A.H., Tsai Y.C.; RT "Crystal structure of D-aminoacylase from Alcaligenes faecalis DA1. A novel RT subset of amidohydrolases and insights into the enzyme mechanism."; RL J. Biol. Chem. 278:4957-4962(2003). RN [3] {ECO:0007829|PDB:1RJP, ECO:0007829|PDB:1RJQ} RP X-RAY CRYSTALLOGRAPHY (1.43 ANGSTROMS) IN COMPLEX WITH COPPER AND ZINC. RX PubMed=14736882; DOI=10.1074/jbc.M308849200; RA Lai W.L., Chou L.Y., Ting C.Y., Kirby R., Tsai Y.C., Wang A.H., Liaw S.H.; RT "The functional role of the binuclear metal center in D-aminoacylase: one- RT metal activation and second-metal attenuation."; RL J. Biol. Chem. 279:13962-13967(2004). 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; AF332548; AAK15530.1; -; Genomic_DNA. DR PDB; 1M7J; X-ray; 1.50 A; A=1-484. DR PDB; 1RJP; X-ray; 1.80 A; A=1-484. DR PDB; 1RJQ; X-ray; 1.80 A; A=1-484. DR PDB; 1RJR; X-ray; 2.10 A; A=1-484. DR PDB; 1RK5; X-ray; 1.80 A; A=1-484. DR PDB; 1RK6; X-ray; 1.43 A; A=1-484. DR PDB; 1V4Y; X-ray; 1.65 A; A=1-484. DR PDB; 1V51; X-ray; 1.60 A; A=1-484. DR PDBsum; 1M7J; -. DR PDBsum; 1RJP; -. DR PDBsum; 1RJQ; -. DR PDBsum; 1RJR; -. DR PDBsum; 1RK5; -. DR PDBsum; 1RK6; -. DR PDBsum; 1V4Y; -. DR PDBsum; 1V51; -. DR AlphaFoldDB; Q9AGH8; -. DR SMR; Q9AGH8; -. DR BRENDA; 3.5.1.81; 232. DR EvolutionaryTrace; Q9AGH8; -. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0047420; F:N-acyl-D-amino-acid deacylase activity; IEA:UniProtKB-EC. DR CDD; cd01297; D-aminoacylase; 1. 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; PTHR11647:SF99; D-PHENYLHYDANTOINASE-RELATED; 1. DR PANTHER; PTHR11647; HYDRANTOINASE/DIHYDROPYRIMIDINASE FAMILY MEMBER; 1. DR Pfam; PF07969; Amidohydro_3; 1. DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1. DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:1M7J, ECO:0007829|PDB:1RJP}; KW Hydrolase {ECO:0000313|EMBL:AAK15530.1}; KW Metal-binding {ECO:0007829|PDB:1M7J, ECO:0007829|PDB:1RJP}; KW Zinc {ECO:0007829|PDB:1M7J, ECO:0007829|PDB:1RJP}. FT DOMAIN 53..333 FT /note="Amidohydrolase 3" FT /evidence="ECO:0000259|Pfam:PF07969" FT BINDING 68 FT /ligand="Cu(2+)" FT /ligand_id="ChEBI:CHEBI:29036" FT /evidence="ECO:0007829|PDB:1RJP, ECO:0007829|PDB:1RK5" FT BINDING 68 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:1M7J, ECO:0007829|PDB:1RJR" FT BINDING 70 FT /ligand="Cu(2+)" FT /ligand_id="ChEBI:CHEBI:29036" FT /evidence="ECO:0007829|PDB:1RK5" FT BINDING 70 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:1M7J, ECO:0007829|PDB:1RJR" FT BINDING 78 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:1V51" FT BINDING 97 FT /ligand="Cu(2+)" FT /ligand_id="ChEBI:CHEBI:29036" FT /evidence="ECO:0007829|PDB:1RJP, ECO:0007829|PDB:1RK5" FT BINDING 97 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:1M7J, ECO:0007829|PDB:1RJR" FT BINDING 97 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:1M7J, ECO:0007829|PDB:1RJP" FT BINDING 118 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:1V51" FT BINDING 177 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0007829|PDB:1V51" FT BINDING 202 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0007829|PDB:1V51" FT BINDING 206 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0007829|PDB:1V51" FT BINDING 214 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0007829|PDB:1V51" FT BINDING 221 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:1M7J, ECO:0007829|PDB:1RJP" FT BINDING 244 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="6" FT /evidence="ECO:0007829|PDB:1V51" FT BINDING 251 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:1M7J, ECO:0007829|PDB:1RJP" FT BINDING 322 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="7" FT /evidence="ECO:0007829|PDB:1V51" FT BINDING 326 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="7" FT /evidence="ECO:0007829|PDB:1V51" FT BINDING 367 FT /ligand="Cu(2+)" FT /ligand_id="ChEBI:CHEBI:29036" FT /evidence="ECO:0007829|PDB:1RJP" FT BINDING 367 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:1M7J, ECO:0007829|PDB:1V4Y" FT BINDING 389 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="8" FT /evidence="ECO:0007829|PDB:1V51" FT BINDING 393 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="8" FT /evidence="ECO:0007829|PDB:1V51" FT BINDING 474 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="9" FT /evidence="ECO:0007829|PDB:1V51" SQ SEQUENCE 484 AA; 52001 MW; 634119A6CB75155E CRC64; MSQPDATPFD YILSGGTVID GTNAPGRLAD VGVRGDRIAA VGDLSASSAR RRIDVAGKVV SPGFIDSHTH DDNYLLKHRD MTPKISQGVT TVVTGNCGIS LAPLAHANPP APLDLLDEGG SFRFARFSDY LEALRAAPPA VNAACMVGHS TLRAAVMPDL RREATADEIQ AMQALADDAL ASGAIGISTG AFYPPAAHAS TEEIIEVCRP LITHGGVYAT HMRDEGEHIV QALEETFRIG RELDVPVVIS HHKVMGKLNF GRSKETLALI EAAMASQDVS LDAYPYVAGS TMLKQDRVLL AGRTLITWCK PYPELSGRDL EEIAAERGKS KYDVVPELQP AGAIYFMMDE PDVQRILAFG PTMIGSDGLP HDERPHPRLW GTFPRVLGHY SRDLGLFPLE TAVWKMTGLT AAKFGLAERG QVQPGYYADL VVFDPATVAD SATFEHPTER AAGIHSVYVN GAAVWEDQSF TGQHAGRVLN RAGA //