Escherichia coli K-12 substr. MG1655 Enzyme: phenylhydantoinase

Gene: hyuA Accession Numbers: G7492 (EcoCyc), b2873, ECK2869

Synonyms: ygeZ

Regulation Summary Diagram: ?

Regulation summary diagram for hyuA

Subunit composition of phenylhydantoinase = [HyuA]4
         phenylhydantoinase = HyuA

Phenylhydantoinase is a novel enzyme exhibiting activity toward hydantoin derivatives with an aromatic side chain at the 5' position, with phenylhydantoin and hydroxyphenylhydantoin having the highest activity level. It is not active on dihydropyrimidines. The enzyme has a stereospecific preference for D-enantiomers. The physiological role of the enzyme is not yet known [Kim00b].

HyuA has similarity to allantoinase enzymes [Xi00], including AllB [Kim00b]. The enzyme is a homotetramer [Kim00b].

HyuA: hydantoin-utilizing enzyme A [Kim00b]

Locations: cytosol

Map Position: [3,008,050 -> 3,009,435] (64.83 centisomes, 233°)
Length: 1386 bp / 461 aa

Molecular Weight of Polypeptide: 51.025 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0009436 , EchoBASE:EB2868 , EcoGene:EG13056 , EcoliWiki:b2873 , ModBase:Q46806 , OU-Microarray:b2873 , PortEco:hyuA , PR:PRO_000022978 , Protein Model Portal:Q46806 , RefSeq:NP_417349 , RegulonDB:G7492 , SMR:Q46806 , String:511145.b2873 , Swiss-Model:Q46806 , UniProt:Q46806

Relationship Links: InterPro:IN-FAMILY:IPR011059 , InterPro:IN-FAMILY:IPR011778 , InterPro:IN-FAMILY:IPR023766 , Pfam:IN-FAMILY:PF01979

In Paralogous Gene Group: 465 (2 members)

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

GO Terms:

Biological Process: GO:0006208 - pyrimidine nucleobase catabolic process Inferred by computational analysis [GOA01]
Molecular Function: GO:0016812 - hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides Inferred from experiment Inferred by computational analysis [GOA06, GOA01, Kim00b]
GO:0042802 - identical protein binding Inferred from experiment [Kim00b]
GO:0016787 - hydrolase activity Inferred by computational analysis [UniProtGOA11]
GO:0016810 - hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds Inferred by computational analysis [GOA01]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11]
Cellular Component: GO:0005737 - cytoplasm Inferred by computational analysis [GOA01]
GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]


Essentiality data for hyuA knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Last-Curated ? 28-Jan-2014 by Keseler I , SRI International

Enzymatic reaction of: phenylhydantoinase

EC Number: 3.5.2.-

phenylhydantoin + H2O <=> phenylureidoacetic acid

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

Reversibility of this reaction is unspecified.

Note: The enzyme may catalyze this reaction in vitro, but this reaction is not considered to be physiologically relevant.

Alternative Substrates for phenylhydantoin: 5-(p-hydroxyphenyl)hydantoin [Kim00b ]

Cofactors or Prosthetic Groups: Mn2+ [Kim00b]

Alternative Cofactors for Mn2+: Co2+ , Ni2+ , Ca2+ , Mg2+ , Fe2+

Kinetic Parameters:

Km (μM)
Vmax (µmol mg-1 min-1)

pH(opt): 8-8.5 [Kim00b]

Sequence Features

Protein sequence of phenylhydantoinase with features indicated

Feature Class Location Citations Comment
Metal-Binding-Site 59
UniProt: Divalent metal cation 1; Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 61
UniProt: Divalent metal cation 1; Non-Experimental Qualifier: by similarity;
N6-carboxylysine-Modification 151
UniProt: N6-carboxylysine; Non-Experimental Qualifier: by similarity.
Metal-Binding-Site 151
UniProt: Divalent metal cation 1; via carbamate group; Non-Experimental Qualifier: by similarity;
Amino-Acid-Sites-That-Bind 156
UniProt: Substrate; Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 182
UniProt: Divalent metal cation 2; Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 239
UniProt: Divalent metal cation 2; Non-Experimental Qualifier: by similarity;
Amino-Acid-Sites-That-Bind 286
UniProt: Substrate; via amide nitrogen and carbonyl oxygen; Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 313
UniProt: Divalent metal cation 1; Non-Experimental Qualifier: by similarity;
Amino-Acid-Sites-That-Bind 335
UniProt: Substrate; via carbonyl oxygen; Non-Experimental Qualifier: by similarity;

Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Unit:

Transcription-unit diagram


Peter D. Karp on Wed Jan 18, 2006:
Gene left-end position adjusted based on analysis performed in the 2005 E. coli annotation update [Riley06 ].
Markus Krummenacker on Tue Oct 14, 1997:
Gene object created from Blattner lab Genbank (v. M52) entry.


Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Kim00b: Kim GJ, Lee DE, Kim HS (2000). "Functional expression and characterization of the two cyclic amidohydrolase enzymes, allantoinase and a novel phenylhydantoinase, from Escherichia coli." J Bacteriol 2000;182(24);7021-8. PMID: 11092864

Riley06: Riley M, Abe T, Arnaud MB, Berlyn MK, Blattner FR, Chaudhuri RR, Glasner JD, Horiuchi T, Keseler IM, Kosuge T, Mori H, Perna NT, Plunkett G, Rudd KE, Serres MH, Thomas GH, Thomson NR, Wishart D, Wanner BL (2006). "Escherichia coli K-12: a cooperatively developed annotation snapshot--2005." Nucleic Acids Res 34(1);1-9. PMID: 16397293

UniProt10: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProt11: UniProt Consortium (2011). "UniProt version 2011-11 released on 2011-11-22 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

Xi00: Xi H, Schneider BL, Reitzer L (2000). "Purine catabolism in Escherichia coli and function of xanthine dehydrogenase in purine salvage." J Bacteriol 182(19);5332-41. PMID: 10986234

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 19.0 on Tue Oct 6, 2015, biocyc13.