HYDA_PSEAE
ID HYDA_PSEAE Reviewed; 479 AA.
AC Q9I676;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=D-hydantoinase/dihydropyrimidinase;
DE Short=DHPase;
DE EC=3.5.2.2 {ECO:0000250|UniProtKB:Q55DL0};
GN Name=dht; OrderedLocusNames=PA0441;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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:0000250}.
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 -!- PTM: Carboxylation allows a single lysine to coordinate two zinc ions.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Hydantoinase/dihydropyrimidinase family. {ECO:0000305}.
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DR EMBL; AE004091; AAG03830.1; -; Genomic_DNA.
DR PIR; H83590; H83590.
DR RefSeq; NP_249132.1; NC_002516.2.
DR RefSeq; WP_003099919.1; NZ_QZGE01000016.1.
DR PDB; 5E5C; X-ray; 2.10 A; A/C=1-479.
DR PDB; 5YKD; X-ray; 2.17 A; A/B/C/D=1-479.
DR PDB; 6AJD; X-ray; 2.22 A; A/B=1-479.
DR PDB; 6KLK; X-ray; 1.76 A; A/B=1-479.
DR PDB; 7E3U; X-ray; 2.16 A; A/B=1-479.
DR PDBsum; 5E5C; -.
DR PDBsum; 5YKD; -.
DR PDBsum; 6AJD; -.
DR PDBsum; 6KLK; -.
DR PDBsum; 7E3U; -.
DR AlphaFoldDB; Q9I676; -.
DR SMR; Q9I676; -.
DR STRING; 287.DR97_3409; -.
DR MEROPS; M38.973; -.
DR PaxDb; Q9I676; -.
DR PRIDE; Q9I676; -.
DR EnsemblBacteria; AAG03830; AAG03830; PA0441.
DR GeneID; 882285; -.
DR KEGG; pae:PA0441; -.
DR PATRIC; fig|208964.12.peg.464; -.
DR PseudoCAP; PA0441; -.
DR HOGENOM; CLU_015572_2_2_6; -.
DR InParanoid; Q9I676; -.
DR OMA; SAETHHM; -.
DR PhylomeDB; Q9I676; -.
DR BioCyc; PAER208964:G1FZ6-445-MON; -.
DR BRENDA; 3.5.2.2; 5087.
DR SABIO-RK; Q9I676; -.
DR Proteomes; UP000002438; Chromosome.
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 3D-structure; Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..479
FT /note="D-hydantoinase/dihydropyrimidinase"
FT /id="PRO_0000287767"
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 STRAND 3..7
FT /evidence="ECO:0007829|PDB:6KLK"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:6KLK"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:6KLK"
FT STRAND 20..24
FT /evidence="ECO:0007829|PDB:6KLK"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:6KLK"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:6KLK"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:6KLK"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:6KLK"
FT HELIX 75..84
FT /evidence="ECO:0007829|PDB:6KLK"
FT STRAND 87..94
FT /evidence="ECO:0007829|PDB:6KLK"
FT HELIX 102..113
FT /evidence="ECO:0007829|PDB:6KLK"
FT STRAND 117..125
FT /evidence="ECO:0007829|PDB:6KLK"
FT HELIX 131..143
FT /evidence="ECO:0007829|PDB:6KLK"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:6KLK"
FT TURN 156..159
FT /evidence="ECO:0007829|PDB:6KLK"
FT HELIX 163..176
FT /evidence="ECO:0007829|PDB:6KLK"
FT STRAND 179..183
FT /evidence="ECO:0007829|PDB:6KLK"
FT HELIX 187..199
FT /evidence="ECO:0007829|PDB:6KLK"
FT HELIX 207..210
FT /evidence="ECO:0007829|PDB:6KLK"
FT HELIX 214..231
FT /evidence="ECO:0007829|PDB:6KLK"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:6KLK"
FT HELIX 243..253
FT /evidence="ECO:0007829|PDB:6KLK"
FT TURN 254..256
FT /evidence="ECO:0007829|PDB:6KLK"
FT STRAND 259..264
FT /evidence="ECO:0007829|PDB:6KLK"
FT HELIX 265..269
FT /evidence="ECO:0007829|PDB:6KLK"
FT HELIX 272..276
FT /evidence="ECO:0007829|PDB:6KLK"
FT HELIX 280..285
FT /evidence="ECO:0007829|PDB:6KLK"
FT HELIX 295..306
FT /evidence="ECO:0007829|PDB:6KLK"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:6KLK"
FT HELIX 322..325
FT /evidence="ECO:0007829|PDB:6KLK"
FT HELIX 326..328
FT /evidence="ECO:0007829|PDB:6KLK"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:6KLK"
FT TURN 342..344
FT /evidence="ECO:0007829|PDB:6KLK"
FT HELIX 345..353
FT /evidence="ECO:0007829|PDB:6KLK"
FT TURN 354..357
FT /evidence="ECO:0007829|PDB:6KLK"
FT HELIX 361..368
FT /evidence="ECO:0007829|PDB:6KLK"
FT HELIX 370..375
FT /evidence="ECO:0007829|PDB:6KLK"
FT TURN 379..381
FT /evidence="ECO:0007829|PDB:6KLK"
FT STRAND 393..403
FT /evidence="ECO:0007829|PDB:6KLK"
FT TURN 406..408
FT /evidence="ECO:0007829|PDB:6KLK"
FT STRAND 410..414
FT /evidence="ECO:0007829|PDB:6KLK"
FT TURN 417..420
FT /evidence="ECO:0007829|PDB:6KLK"
FT STRAND 422..432
FT /evidence="ECO:0007829|PDB:6KLK"
FT STRAND 435..439
FT /evidence="ECO:0007829|PDB:6KLK"
FT HELIX 461..471
FT /evidence="ECO:0007829|PDB:6KLK"
SQ SEQUENCE 479 AA; 52212 MW; 46582DFE22E38925 CRC64;
MSLLIRGATV VTHEESYRAD VLCANGLIQA IGENLETPSG CDVLDGGGQY LMPGGIDPHT
HMQLPFMGTV ASEDFFSGTA AGLAGGTTSI IDFVIPNPRQ SLLEAFHTWR GWAQKSAADY
GFHVAITWWS DEVAREMGEL VAQHGVNSFK HFMAYKNAIM AADDTLVASF ERCLELGAVP
TVHAENGELV FHLQQKLLAQ GLTGPEAHPL SRPPQVEGEA ASRAIRIAET LGTPLYLVHI
SSREALDEIA YARAKGQPVY GEVLAGHLLL DDSVYRHPDW ATAAGYVMSP PFRPVEHQEA
LWRGLQSGNL HTTATDHCCF CAEQKAMGRD DFSKIPNGTA GIEDRMALLW DAGVNSGRLS
MHEFVALTST NTAKIFNLFP RKGAIRVGAD ADLVLWDPQG SRTLSAATHH QRVDFNIFEG
RTVRGIPSHT ISQGKLLWAA GDLRAEPGAG RYVERPAYPS VYEVLGRRAE RQRPVAVER
