HYDL_PAEAU
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 03-AUG-2022, entry version 96.
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; Actinobacteria; Micrococcales; Micrococcaceae; 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}.
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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 Gene3D; 2.30.40.10; -; 1.
DR InterPro; IPR017593; Allantoinase.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; SSF51338; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR03178; allantoinase; 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
