ID HYDL_PAEAU Reviewed; 458 AA. AC P81006; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 1. DT 13-SEP-2023, entry version 101. DE RecName: Full=L-hydantoinase; DE EC=3.5.2.-; DE AltName: Full=Non-ATP-dependent L-selective hydantoinase; GN Name=lhyD; OS Paenarthrobacter aurescens (Arthrobacter aurescens). OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae; OC Paenarthrobacter. OX NCBI_TaxID=43663; RN [1] RP PROTEIN SEQUENCE. RC STRAIN=DSM 3745; RX PubMed=9687026; RA May O., Habenicht A., Mattes R., Syldatk C., Siemann M.; RT "Molecular evolution of hydantoinases."; RL Biol. Chem. 379:743-747(1998). RN [2] RP PROTEIN SEQUENCE OF 1-40, CHARACTERIZATION, AND MASS SPECTROMETRY. RC STRAIN=DSM 3745; RX PubMed=9650283; DOI=10.1016/s0168-1656(98)00005-4; RA May O., Siemann M., Pietzsch M., Kiess M., Mattes R., Syldatk C.; RT "Substrate-dependent enantioselectivity of a novel hydantoinase from RT Arthrobacter aurescens DSM 3745: purification and characterization as new RT member of cyclic amidases."; RL J. Biotechnol. 61:1-13(1998). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS). RC STRAIN=DSM 3745; RX PubMed=15299588; DOI=10.1107/s0907444996007731; RA May O., Siemann M., Syldatk C., Niefind K., Schomburg D.; RT "Crystallization and preliminary X-ray analysis of a hydantoinase from RT Arthrobacter aurecens DSM 3745."; RL Acta Crystallogr. D 52:1209-1210(1996). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH ZINC IONS, SUBUNIT, RP AND CARBOXYLATION AT LYS-147. RX PubMed=12093275; DOI=10.1021/bi0157722; RA Abendroth J., Niefind K., May O., Siemann M., Syldatk C., Schomburg D.; RT "The structure of L-hydantoinase from Arthobacter aurescens leads to an RT understanding of dihydropyrimidinase substrate and enantio specificity."; RL Biochemistry 41:8589-8597(2002). CC -!- FUNCTION: Rather more predominant for the cleavage of aryl- than for CC alkyl-hydantoin derivatives. The stereoselectivity of this enzyme CC depends on the substrate used for bioconversion: strictly L-selective CC for the cleavage of D,L-5-indolylmethylhydantoin, but D-selective for CC the hydrolysis of D,L-methylthioethylhydantoin. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000269|PubMed:12093275}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:12093275}; CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:12093275}. CC -!- PTM: Carboxylation allows a single lysine to coordinate two zinc ions. CC {ECO:0000269|PubMed:12093275}. CC -!- MASS SPECTROMETRY: Mass=49680; Method=MALDI; CC Evidence={ECO:0000269|PubMed:9650283}; CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. CC Hydantoinase/dihydropyrimidinase family. {ECO:0000305}. 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 PDB; 1GKR; X-ray; 2.60 A; A/B/C/D=1-458. DR PDBsum; 1GKR; -. DR AlphaFoldDB; P81006; -. DR SMR; P81006; -. DR DrugBank; DB03801; Lysine Nz-Carboxylic Acid. DR BRENDA; 3.5.2.2; 441. DR EvolutionaryTrace; P81006; -. DR GO; GO:0004038; F:allantoinase activity; IEA:InterPro. DR GO; GO:0050897; F:cobalt ion binding; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0000256; P:allantoin catabolic process; IEA:InterPro. DR CDD; cd01315; L-HYD_ALN; 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; IPR017593; Allantoinase. DR InterPro; IPR006680; Amidohydro-rel. DR InterPro; IPR011059; Metal-dep_hydrolase_composite. DR InterPro; IPR032466; Metal_Hydrolase. DR NCBIfam; TIGR03178; allantoinase; 1. DR PANTHER; PTHR43668; ALLANTOINASE; 1. DR PANTHER; PTHR43668:SF2; ALLANTOINASE; 1. DR Pfam; PF01979; Amidohydro_1; 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; Direct protein sequencing; Hydrolase; Metal-binding; Zinc. FT CHAIN 1..458 FT /note="L-hydantoinase" FT /id="PRO_0000165938" FT BINDING 60 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:12093275, FT ECO:0007744|PDB:1GKR" FT BINDING 62 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:12093275, FT ECO:0007744|PDB:1GKR" FT BINDING 147 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /note="via carbamate group" FT /evidence="ECO:0000269|PubMed:12093275, FT ECO:0007744|PDB:1GKR" FT BINDING 147 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /note="via carbamate group" FT /evidence="ECO:0000269|PubMed:12093275, FT ECO:0007744|PDB:1GKR" FT BINDING 183 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:12093275, FT ECO:0007744|PDB:1GKR" FT BINDING 239 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:12093275, FT ECO:0007744|PDB:1GKR" FT BINDING 312 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:12093275, FT ECO:0007744|PDB:1GKR" FT MOD_RES 147 FT /note="N6-carboxylysine" FT /evidence="ECO:0000269|PubMed:12093275, FT ECO:0007744|PDB:1GKR" FT STRAND 2..13 FT /evidence="ECO:0007829|PDB:1GKR" FT STRAND 16..25 FT /evidence="ECO:0007829|PDB:1GKR" FT STRAND 28..34 FT /evidence="ECO:0007829|PDB:1GKR" FT STRAND 41..46 FT /evidence="ECO:0007829|PDB:1GKR" FT STRAND 51..54 FT /evidence="ECO:0007829|PDB:1GKR" FT STRAND 56..62 FT /evidence="ECO:0007829|PDB:1GKR" FT HELIX 66..68 FT /evidence="ECO:0007829|PDB:1GKR" FT TURN 69..71 FT /evidence="ECO:0007829|PDB:1GKR" FT HELIX 75..85 FT /evidence="ECO:0007829|PDB:1GKR" FT STRAND 87..92 FT /evidence="ECO:0007829|PDB:1GKR" FT STRAND 96..98 FT /evidence="ECO:0007829|PDB:1GKR" FT HELIX 103..116 FT /evidence="ECO:0007829|PDB:1GKR" FT STRAND 118..126 FT /evidence="ECO:0007829|PDB:1GKR" FT HELIX 132..140 FT /evidence="ECO:0007829|PDB:1GKR" FT STRAND 145..151 FT /evidence="ECO:0007829|PDB:1GKR" FT TURN 155..157 FT /evidence="ECO:0007829|PDB:1GKR" FT HELIX 163..176 FT /evidence="ECO:0007829|PDB:1GKR" FT STRAND 179..183 FT /evidence="ECO:0007829|PDB:1GKR" FT HELIX 187..199 FT /evidence="ECO:0007829|PDB:1GKR" FT HELIX 205..211 FT /evidence="ECO:0007829|PDB:1GKR" FT HELIX 214..231 FT /evidence="ECO:0007829|PDB:1GKR" FT STRAND 234..237 FT /evidence="ECO:0007829|PDB:1GKR" FT HELIX 243..254 FT /evidence="ECO:0007829|PDB:1GKR" FT STRAND 259..263 FT /evidence="ECO:0007829|PDB:1GKR" FT HELIX 265..268 FT /evidence="ECO:0007829|PDB:1GKR" FT HELIX 272..274 FT /evidence="ECO:0007829|PDB:1GKR" FT HELIX 275..278 FT /evidence="ECO:0007829|PDB:1GKR" FT HELIX 279..282 FT /evidence="ECO:0007829|PDB:1GKR" FT HELIX 291..302 FT /evidence="ECO:0007829|PDB:1GKR" FT HELIX 318..320 FT /evidence="ECO:0007829|PDB:1GKR" FT HELIX 322..325 FT /evidence="ECO:0007829|PDB:1GKR" FT HELIX 328..330 FT /evidence="ECO:0007829|PDB:1GKR" FT TURN 338..340 FT /evidence="ECO:0007829|PDB:1GKR" FT HELIX 341..348 FT /evidence="ECO:0007829|PDB:1GKR" FT TURN 349..353 FT /evidence="ECO:0007829|PDB:1GKR" FT HELIX 357..364 FT /evidence="ECO:0007829|PDB:1GKR" FT HELIX 366..371 FT /evidence="ECO:0007829|PDB:1GKR" FT TURN 375..377 FT /evidence="ECO:0007829|PDB:1GKR" FT STRAND 378..380 FT /evidence="ECO:0007829|PDB:1GKR" FT STRAND 389..394 FT /evidence="ECO:0007829|PDB:1GKR" FT HELIX 402..404 FT /evidence="ECO:0007829|PDB:1GKR" FT STRAND 406..408 FT /evidence="ECO:0007829|PDB:1GKR" FT TURN 413..416 FT /evidence="ECO:0007829|PDB:1GKR" FT STRAND 422..428 FT /evidence="ECO:0007829|PDB:1GKR" FT STRAND 431..435 FT /evidence="ECO:0007829|PDB:1GKR" SQ SEQUENCE 458 AA; 49597 MW; A0A78C492E461CFE CRC64; MFDVIVKNCR LVSSDGITEA DILVKDGKVA AISADTSDVE ASRTIDAGGK FVMPGVVDEH VHIIDMDLKN RYGRFELDSE SAAVGGITTI IEMPITFPPT TTLDAFLEKK KQAGQRLKVD FALYGGGVPG NLPEIRKMHD AGAVGFKSMM AASVPGMFDA VSDGELFEIF QEIAACGSVI VVHAENETII QALQKQIKAA GGKDMAAYEA SQPVFQENEA IQRALLLQKE AGCRLIVLHV SNPDGVELIH QAQSEGQDVH CESGPQYLNI TTDDAERIGP YMKVAPPVRS AEMNIRLWEQ LENGLIDTLG SDHGGHPVED KEPGWKDVWK AGNGALGLET SLPMMLTNGV NKGRLSLERL VEVMCEKPAK LFGIYPQKGT LQVGSDADLL ILDLDIDTKV DASQFRSLHK YSPFDGMPVT GAPVLTMVRG TVVAEKGEVL VEQGFGQFVT RRNYEASK //