HYDA_PSEPU
ID HYDA_PSEPU Reviewed; 495 AA.
AC Q59699; O54406;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=D-hydantoinase/dihydropyrimidinase {ECO:0000303|PubMed:9434154};
DE Short=DHPase {ECO:0000303|PubMed:9434154};
DE EC=3.5.2.2 {ECO:0000250|UniProtKB:Q55DL0};
GN Name=dht {ECO:0000303|PubMed:9434154};
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-18 AND 492-494,
RP FUNCTION, INDUCTION, AND NOMENCLATURE.
RC STRAIN=ATCC 950 / BCRC 12857 / NBRC 13696 / Stanier 91;
RX PubMed=9434154; DOI=10.1016/s0167-4781(97)00097-3;
RA Chien H.R., Jih Y.L., Yang W.Y., Hsu W.H.;
RT "Identification of the open reading frame for the Pseudomonas putida D-
RT hydantoinase gene and expression of the gene in Escherichia coli.";
RL Biochim. Biophys. Acta 1395:68-77(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=DSM 84 / IMG 1513;
RX PubMed=8161181; DOI=10.1128/aem.60.3.888-895.1994;
RA Lapointe G., Viau S., Leblanc D., Robert N., Morin A.;
RT "Cloning, sequencing, and expression in Escherichia coli of the D-
RT hydantoinase gene from Pseudomonas putida and distribution of homologous
RT genes in other microorganisms.";
RL Appl. Environ. Microbiol. 60:888-895(1994).
CC -!- FUNCTION: Catalyzes the hydrolysis of dihydropyrimidines and of the
CC structurally related DL-5-mono-substituted hydantoins, to produce N-
CC carbamoyl-D-amino acids. {ECO:0000305|PubMed:8161181,
CC ECO:0000305|PubMed:9434154}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouracil + H2O = 3-(carbamoylamino)propanoate + H(+);
CC Xref=Rhea:RHEA:16121, ChEBI:CHEBI:11892, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15901; EC=3.5.2.2;
CC Evidence={ECO:0000250|UniProtKB:Q55DL0};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q55DL0};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q55DL0};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q55DL0}.
CC -!- INDUCTION: By lactose. {ECO:0000269|PubMed:9434154}.
CC -!- PTM: Carboxylation allows a single lysine to coordinate two zinc ions.
CC {ECO:0000250|UniProtKB:Q55DL0}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Hydantoinase/dihydropyrimidinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA21752.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U84197; AAC00209.1; -; Genomic_DNA.
DR EMBL; L24157; AAA21752.1; ALT_FRAME; Genomic_DNA.
DR AlphaFoldDB; Q59699; -.
DR SMR; Q59699; -.
DR STRING; 1240350.AMZE01000004_gene2437; -.
DR MEROPS; M38.973; -.
DR eggNOG; COG0044; Bacteria.
DR BRENDA; 3.5.2.2; 5092.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004157; F:dihydropyrimidinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd01314; D-HYD; 1.
DR Gene3D; 2.30.40.10; -; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR011778; Hydantoinase/dihydroPyrase.
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; TIGR02033; D-hydantoinase; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase; Metal-binding; Zinc.
FT CHAIN 1..495
FT /note="D-hydantoinase/dihydropyrimidinase"
FT /id="PRO_0000165935"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9P903"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9P903"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /note="via carbamate group"
FT /evidence="ECO:0000250|UniProtKB:Q9P903"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /note="via carbamate group"
FT /evidence="ECO:0000250|UniProtKB:Q9P903"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9P903"
FT BINDING 183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9P903"
FT BINDING 239
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9P903"
FT BINDING 289
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9P903"
FT BINDING 316
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9P903"
FT BINDING 337
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9P903"
FT MOD_RES 150
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000250|UniProtKB:Q9P903"
FT CONFLICT 304
FT /note="G -> R (in Ref. 2; AAA21752)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 495 AA; 53507 MW; FBC65F6DFA62F972 CRC64;
MSLLIRGATV VTHEESYPAD VLCVDGLIRA IGPNLEPPTD CEILDGSGQY LMPGGIDPHT
HMQLPFMGTV ASEDFFSGTA AGLAGGTTSI IDFVIPNPQQ SLLEAFHTWR GWAQKSASDY
GFHVAITWWS EQVAEEMGEL VAKHGVNSFK HFMAYKNAIM AADDTLVASF ERCLQLGAVP
TVHAENGELV YHLQKKLLAQ GMTGPEAHPL SRPSQVEGEA ASRAIRIAET IGTPLYVVHI
SSREALDEIT YARAKGQPVY GEVLPGHLLL DDSVYRDPDW ATAAGYVMSP PFRPREHQEA
LWRGLQSGNL HTTATDHCCF CAEQKAMGRD DFSRIPNGTA GIEDRMAVLW DAGVNSGRLS
MHEFVALTST NTAKIFNLFP RKGAIRVGAD ADLVLWDPQG TRTLSAQTHH QRVDFNIFEG
RTVRGVPSHT ISQGKVLWAD GDLRRRGRGG AVCGTAGVSV GVRGAGATRR TAAPDARSAL
RPLGLLRSPS PASQI
