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Protein

D-phenylhydantoinase

Gene

hyuA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the stereospecific hydrolysis of the cyclic amide bond of D-hydantoin derivatives with an aromatic side chains at the 5'-position. Has no activity on dihydropyrimidines. The physiological function is unknown.1 Publication

Cofactori

Zn2+Curated1 Publication, Ni2+Curated1 Publication, Co2+Curated1 Publication, Mn2+Curated1 PublicationNote: Binds 2 divalent metal cations per subunit. Can use zinc, nickel, cobalt or manganese.Curated1 Publication

Kineticsi

Hydantoin derivatives with an aliphatic or no side chain at their 5'-position results in a much lower level of activity than those with aromatic side chains at the 5'-position.
  1. KM=7.8 mM for phenylhydantoin1 Publication
  2. KM=32.8 mM for hydroxyphenylhydantoin1 Publication
  3. KM=138 mM for hydantoin1 Publication
  1. Vmax=12.6 µmol/min/mg enzyme with hydroxyphenylhydantoin as substrate1 Publication
  2. Vmax=3.3 µmol/min/mg enzyme with phenylhydantoin as substrate1 Publication
  3. Vmax=0.15 µmol/min/mg enzyme with hydantoin as substrate1 Publication

pH dependencei

Optimum pH is 8-8.5.1 Publication

Temperature dependencei

Optimum temperature is 45-50 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi59Divalent metal cation 1By similarity1
Metal bindingi61Divalent metal cation 1By similarity1
Metal bindingi151Divalent metal cation 1; via carbamate groupBy similarity1
Metal bindingi151Divalent metal cation 2; via carbamate groupBy similarity1
Binding sitei156SubstrateBy similarity1
Metal bindingi182Divalent metal cation 2By similarity1
Metal bindingi239Divalent metal cation 2By similarity1
Binding sitei286Substrate; via amide nitrogen and carbonyl oxygenBy similarity1
Metal bindingi313Divalent metal cation 1By similarity1
Binding sitei335Substrate; via carbonyl oxygenBy similarity1

GO - Molecular functioni

  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides Source: EcoliWiki
  • identical protein binding Source: EcoCyc
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

Keywordsi

Molecular functionHydrolase
LigandMetal-binding

Enzyme and pathway databases

BioCyciEcoCyc:G7492-MONOMER
MetaCyc:G7492-MONOMER
SABIO-RKiQ46806

Names & Taxonomyi

Protein namesi
Recommended name:
D-phenylhydantoinase (EC:3.5.2.-)
Alternative name(s):
Hydantoin-utilizing enzyme HyuA
Gene namesi
Name:hyuA
Synonyms:ygeZ
Ordered Locus Names:b2873, JW2841
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13056 hyuA

Subcellular locationi

GO - Cellular componenti

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001659371 – 461D-phenylhydantoinaseAdd BLAST461

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei151N6-carboxylysineBy similarity1

Post-translational modificationi

Carbamylation allows a single lysine to coordinate two divalent metal cations.By similarity

Proteomic databases

PaxDbiQ46806
PRIDEiQ46806

Interactioni

Subunit structurei

Homotetramer.1 Publication

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4261249, 13 interactors
IntActiQ46806, 2 interactors
STRINGi316385.ECDH10B_3048

Structurei

3D structure databases

ProteinModelPortaliQ46806
SMRiQ46806
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CD3 Bacteria
COG0044 LUCA
HOGENOMiHOG000219145
InParanoidiQ46806
KOiK01464
OMAiIDPQVHF
PhylomeDBiQ46806

Family and domain databases

CDDicd01314 D-HYD, 1 hit
Gene3Di2.30.40.10, 2 hits
HAMAPiMF_01644 D_hydantoinase, 1 hit
InterProiView protein in InterPro
IPR006680 Amidohydro-rel
IPR023766 D_phenylhydantoinase
IPR011778 Hydantoinase/dihydroPyrase
IPR011059 Metal-dep_hydrolase_composite
IPR032466 Metal_Hydrolase
PfamiView protein in Pfam
PF01979 Amidohydro_1, 1 hit
SUPFAMiSSF51338 SSF51338, 2 hits
SSF51556 SSF51556, 1 hit
TIGRFAMsiTIGR02033 D-hydantoinase, 1 hit

Sequencei

Sequence statusi: Complete.

Q46806-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRVLIKNGTV VNADGQAKQD LLIESGIVRQ LGNNISPQLP YEEIDATGCY
60 70 80 90 100
VFPGGVDVHT HFNIDVGIAR SCDDFFTGTR AAACGGTTTI IDHMGFGPNG
110 120 130 140 150
CRLRHQLEVY RGYAAHKAVI DYSFHGVIQH INHAILDEIP MIVEEGLSSF
160 170 180 190 200
KLYLTYQYKL NDDEVLQALR RLHESGALTT VHPENDAAIA SKRAEFIAAG
210 220 230 240 250
LTAPRYHALS RPLECEAEAI ARMINLAQIA GNAPLYIVHL SNGLGLDYLR
260 270 280 290 300
LARANHQPVW VETCPQYLLL DERSYDTEDG MKFILSPPLR NVREQDKLWC
310 320 330 340 350
GISDGAIDVV ATDHCTFSMA QRLQISKGDF SRCPNGLPGV ENRMQLLFSS
360 370 380 390 400
GVMTGRITPE RFVELTSAMP ARLFGLWPQK GLLAPGSDGD VVIIDPRQSQ
410 420 430 440 450
QIQHRHLHDN ADYSPWEGFT CQGAIVRTLS RGETIFCDGT FTGKAGRGRF
460
LRRKPFVPPV L
Length:461
Mass (Da):51,025
Last modified:November 16, 2001 - v2
Checksum:i5525E62DB7F8DB5B
GO

Sequence cautioni

The sequence AAA83054 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28375 Genomic DNA Translation: AAA83054.1 Different initiation.
U00096 Genomic DNA Translation: AAC75911.2
AP009048 Genomic DNA Translation: BAE76939.1
PIRiA65071
RefSeqiNP_417349.4, NC_000913.3
WP_001264442.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC75911; AAC75911; b2873
BAE76939; BAE76939; BAE76939
GeneIDi947359
KEGGiecj:JW2841
eco:b2873
PATRICifig|1411691.4.peg.3861

Similar proteinsi

Entry informationi

Entry nameiPHYDA_ECOLI
AccessioniPrimary (citable) accession number: Q46806
Secondary accession number(s): Q2M9W7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 16, 2001
Last modified: March 28, 2018
This is version 125 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health