Q1R7F8 (PHYDA_ECOUT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
D-phenylhydantoinase
EC=3.5.2.-

Alternative name(s):
Hydantoin-utilizing enzyme HyuA

Gene names

Name:	hyuA
Synonyms:	ygeZ
Ordered Locus Names:	UTI89_C3258

Organism

Escherichia coli (strain UTI89 / UPEC) [Complete proteome] [HAMAP]

Taxonomic identifier

364106 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	461 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	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 By similarity. HAMAP-Rule MF_01644
Cofactor	Binds 2 divalent metal cations per subunit By similarity.
Subunit structure	Homotetramer By similarity.
Post-translational modification	Carbamylation allows a single lysine to coordinate two divalent metal cations By similarity. HAMAP-Rule MF_01644
Sequence similarities	Belongs to the DHOase family. Hydantoinase/dihydropyrimidinase subfamily.
Sequence caution	The sequence ABE08706.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Ligand	Metal-binding
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	pyrimidine nucleobase catabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides Inferred from electronic annotation. Source: HAMAP metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 461	461	D-phenylhydantoinase HAMAP-Rule MF_01644		PRO_0000317655
Sites
	Metal binding	59	1	Divalent metal cation 1 By similarity
	Metal binding	61	1	Divalent metal cation 1 By similarity
	Metal binding	151	1	Divalent metal cation 1; via carbamate group By similarity
	Metal binding	151	1	Divalent metal cation 2; via carbamate group By similarity
	Metal binding	182	1	Divalent metal cation 2 By similarity
	Metal binding	239	1	Divalent metal cation 2 By similarity
	Metal binding	313	1	Divalent metal cation 1 By similarity
	Binding site	156	1	Substrate By similarity
	Binding site	286	1	Substrate; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	335	1	Substrate; via carbonyl oxygen By similarity
Amino acid modifications
	Modified residue	151	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1R7F8 [UniParc]. Last modified February 5, 2008. Version 2. Checksum: 3C74C632FDAFB79E	FASTA	461	50,971
	10 20 30 40 50 60 MRVLIKNGIV VNADGQAKQD LLIESGIVRQ LGTDISPQLP CEEIDASGCY VFPGGVDVHT 70 80 90 100 110 120 HFNIDVGIAR SCDDFFTGTR AAACGGTTTI IDHMGFGPNG CRLRHQLEVY RGYAAHKAVI 130 140 150 160 170 180 DYSFHGVIQH INHAILDEIP MMVEEGLSSF KLYLTYQYKL NDDEVLQALR RLHESGALTT 190 200 210 220 230 240 VHPENDAAIA SKRAEFIAAG LTAPRYHALS RPLECEAEAI ARMINLAQIA GNAPLYIVHL 250 260 270 280 290 300 SNGLGLDYLR LARANHQPVW VETCPQYLLL DERSYDTEDG MKFILSPPLR NVREQDKLWC 310 320 330 340 350 360 GISDGAIDVV ATDHCTFSMA QRLQISKGDF SRCPNGLPGV ENRMQLLFSS GVMTGRISLE 370 380 390 400 410 420 RFVELTSAMP ARLFGLWPQK GILAPGSDGD VVIIDPRQSQ QIQHRHLHDN ADYSPWEGFT 430 440 450 460 CQGAIVRTLS RGETIFCDGT FTGKAGRGRF LRRKPFVPPV L

References

[1]

"Identification of genes subject to positive selection in uropathogenic strains of Escherichia coli: a comparative genomics approach." Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A., Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J., Gordon J.I. Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: UTI89 / UPEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000243 Genomic DNA. Translation: ABE08706.1. Different initiation.
RefSeq	YP_542237.1. NC_007946.1.
3D structure databases
HSSP	HSSP built from PDB template 2FTW based on UniProtKB Q86LT2.
ProteinModelPortal	Q1R7F8.
SMR	Q1R7F8. Positions 2-457.
ModBase	Search...
Protein-protein interaction databases
STRING	364106.UTI89_C3258.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABE08706; ABE08706; UTI89_C3258.
GeneID	3990084.
KEGG	eci:UTI89_C3258.
PATRIC	18456024. VBIEscCol42261_3230.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0044.
HOGENOM	HOG000219145.
KO	K01464.
OMA	FPDFAYK.
ProtClustDB	PRK08323.
Enzyme and pathway databases
BioCyc	ECOL364106:GHPQ-3281-MONOMER.
Family and domain databases
HAMAP	MF_01644. D-hydantoinase.
InterPro	IPR023766. D_phenylhydantoinase. IPR011778. Hydantoinase/dihydroPyrase. IPR011059. Metal-dep_hydrolase_composite. [Graphical view]
SUPFAM	SSF51338. Metalo_hydrolase. 1 hit.
TIGRFAMs	TIGR02033. D-hydantoinase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PHYDA_ECOUT

Accession

Primary (citable) accession number: Q1R7F8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	February 5, 2008
Last modified:	May 1, 2013
This is version 48 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program