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PHYDA_ECO27
ID   PHYDA_ECO27             Reviewed;         461 AA.
AC   B7UHS3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=D-phenylhydantoinase {ECO:0000255|HAMAP-Rule:MF_01644};
DE            EC=3.5.2.- {ECO:0000255|HAMAP-Rule:MF_01644};
DE   AltName: Full=Hydantoin-utilizing enzyme HyuA {ECO:0000255|HAMAP-Rule:MF_01644};
GN   Name=hyuA {ECO:0000255|HAMAP-Rule:MF_01644}; OrderedLocusNames=E2348C_3125;
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC;
RX   PubMed=18952797; DOI=10.1128/jb.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R.,
RA   Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A.,
RA   Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
CC   -!- FUNCTION: Catalyzes the stereospecific hydrolysis of the cyclic amide
CC       bond of D-hydantoin derivatives with an aromatic side chains at the 5'-
CC       position. Has no activity on dihydropyrimidines. The physiological
CC       function is unknown. {ECO:0000255|HAMAP-Rule:MF_01644}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-5-phenylhydantoin + H2O = H(+) + N-carbamoyl-D-
CC         phenylglycine; Xref=Rhea:RHEA:51664, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:140750, ChEBI:CHEBI:140758;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01644};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01644};
CC       Note=Binds 2 divalent metal cations per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01644};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01644}.
CC   -!- PTM: Carboxylation allows a single lysine to coordinate two divalent
CC       metal cations. {ECO:0000255|HAMAP-Rule:MF_01644}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Hydantoinase/dihydropyrimidinase family. {ECO:0000255|HAMAP-
CC       Rule:MF_01644}.
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DR   EMBL; FM180568; CAS10673.1; -; Genomic_DNA.
DR   RefSeq; WP_001264433.1; NC_011601.1.
DR   AlphaFoldDB; B7UHS3; -.
DR   SMR; B7UHS3; -.
DR   EnsemblBacteria; CAS10673; CAS10673; E2348C_3125.
DR   KEGG; ecg:E2348C_3125; -.
DR   HOGENOM; CLU_015572_2_0_6; -.
DR   OMA; SAETHHM; -.
DR   Proteomes; UP000008205; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0016812; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006208; P:pyrimidine nucleobase catabolic process; IEA:InterPro.
DR   CDD; cd01314; D-HYD; 1.
DR   Gene3D; 2.30.40.10; -; 1.
DR   HAMAP; MF_01644; D_hydantoinase; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR023766; D_phenylhydantoinase.
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; 2.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   TIGRFAMs; TIGR02033; D-hydantoinase; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding.
FT   CHAIN           1..461
FT                   /note="D-phenylhydantoinase"
FT                   /id="PRO_1000186907"
FT   BINDING         59
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01644"
FT   BINDING         61
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01644"
FT   BINDING         151
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01644"
FT   BINDING         151
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01644"
FT   BINDING         156
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01644"
FT   BINDING         182
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01644"
FT   BINDING         239
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01644"
FT   BINDING         286
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01644"
FT   BINDING         313
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01644"
FT   BINDING         335
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01644"
FT   MOD_RES         151
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01644"
SQ   SEQUENCE   461 AA;  50985 MW;  3AA91D2CAB3AA6CE CRC64;
     MRVLIKNGIV VNADGQAKQD LLIESGIVRQ LGTDISPQLP CEEIDASGCY VFPGGVDVHT
     HFNIDVGIAR SCDDFFTGTR AAACGGTTTI IDHMGFGPNG CRLRHQLEVY RGYAAHKAVI
     DYSFHGVIQH INHAILDEIP MMVEEGLSSF KLYLTYQYKL NDDEVLQALR RLHESGALTT
     VHPENDAAIA SKRAEFIAAG LTAPRYHALS RPLECEAEAI ARMINLAQIA GNAPLYIVHL
     SNGLGLDYLR LARANHQPVW VETCPQYLLL DERSYDTEDG MKFILSPPLR NVREQDKLWC
     GISDGAIDVV ATDHCTFSMA QRLQISKGDF SRCPNGLPGV ENRMQLLFSS GVMTGRISPE
     RFVELTSAMP ARLFGLWPQK GLLAPGSDGD VVIIDPRQSQ QIQHRHLHDN ADYSPWEGFT
     CQGAIVRTLS RGEMIFCDGT FTGKAGRGRF LRRKPFVPPV L
 
 
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