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P81006 (HYDL_ARTAU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
L-hydantoinase

EC=3.5.2.-
Alternative name(s):
Non-ATP-dependent L-selective hydantoinase
Gene names
Name:lhyD
OrganismArthrobacter aurescens
Taxonomic identifier43663 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrococcaceaeArthrobacter

Protein attributes

Sequence length458 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Rather more predominant for the cleavage of aryl- than for alkyl-hydantoin derivatives. The stereoselectivity of this enzyme depends on the substrate used for bioconversion: strictly L-selective for the cleavage of D,L-5-indolylmethylhydantoin, but D-selective for the hydrolysis of D,L-methylthioethylhydantoin.

Cofactor

Binds 2 zinc ions per subunit.

Subunit structure

Homotetramer. Ref.4

Post-translational modification

Carbamylation allows a single lysine to coordinate two zinc ions.

Sequence similarities

Belongs to the DHOase family. Hydantoinase/dihydropyrimidinase subfamily.

Mass spectrometry

Molecular mass is 49680 Da from positions 1 - 458. Determined by MALDI. Ref.2

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 458458L-hydantoinase
PRO_0000165938

Sites

Metal binding601Zinc 1
Metal binding621Zinc 1
Metal binding1471Zinc 1; via carbamate group
Metal binding1471Zinc 2; via carbamate group
Metal binding1831Zinc 2
Metal binding2391Zinc 2
Metal binding3121Zinc 1

Amino acid modifications

Modified residue1471N6-carboxylysine

Secondary structure

..................................................................................... 458
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P81006 [UniParc].

Last modified July 15, 1998. Version 1.
Checksum: A0A78C492E461CFE

FASTA45849,597
        10         20         30         40         50         60 
MFDVIVKNCR LVSSDGITEA DILVKDGKVA AISADTSDVE ASRTIDAGGK FVMPGVVDEH 

        70         80         90        100        110        120 
VHIIDMDLKN RYGRFELDSE SAAVGGITTI IEMPITFPPT TTLDAFLEKK KQAGQRLKVD 

       130        140        150        160        170        180 
FALYGGGVPG NLPEIRKMHD AGAVGFKSMM AASVPGMFDA VSDGELFEIF QEIAACGSVI 

       190        200        210        220        230        240 
VVHAENETII QALQKQIKAA GGKDMAAYEA SQPVFQENEA IQRALLLQKE AGCRLIVLHV 

       250        260        270        280        290        300 
SNPDGVELIH QAQSEGQDVH CESGPQYLNI TTDDAERIGP YMKVAPPVRS AEMNIRLWEQ 

       310        320        330        340        350        360 
LENGLIDTLG SDHGGHPVED KEPGWKDVWK AGNGALGLET SLPMMLTNGV NKGRLSLERL 

       370        380        390        400        410        420 
VEVMCEKPAK LFGIYPQKGT LQVGSDADLL ILDLDIDTKV DASQFRSLHK YSPFDGMPVT 

       430        440        450 
GAPVLTMVRG TVVAEKGEVL VEQGFGQFVT RRNYEASK 

« Hide

References

[1]"Molecular evolution of hydantoinases."
May O., Habenicht A., Mattes R., Syldatk C., Siemann M.
Biol. Chem. 379:743-747(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
Strain: DSM 3745.
[2]"Substrate-dependent enantioselectivity of a novel hydantoinase from Arthrobacter aurescens DSM 3745: purification and characterization as new member of cyclic amidases."
May O., Siemann M., Pietzsch M., Kiess M., Mattes R., Syldatk C.
J. Biotechnol. 61:1-13(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-40, CHARACTERIZATION, MASS SPECTROMETRY.
Strain: DSM 3745.
[3]"Crystallization and preliminary X-ray analysis of a hydantoinase from Arthrobacter aurecens DSM 3745."
May O., Siemann M., Syldatk C., Niefind K., Schomburg D.
Acta Crystallogr. D 52:1209-1210(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
Strain: DSM 3745.
[4]"The structure of L-hydantoinase from Arthobacter aurescens leads to an understanding of dihydropyrimidinase substrate and enantio specificity."
Abendroth J., Niefind K., May O., Siemann M., Syldatk C., Schomburg D.
Biochemistry 41:8589-8597(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH ZINC IONS, SUBUNIT, CARBAMYLATION AT LYS-147.

Cross-references

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GKRX-ray2.60A/B/C/D1-458[»]
ProteinModelPortalP81006.
SMRP81006. Positions 1-451.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA3.5.2.2. 441.

Family and domain databases

Gene3D2.30.40.10. 2 hits.
InterProIPR017593. Allantoinase.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
SUPFAMSSF51338. SSF51338. 2 hits.
TIGRFAMsTIGR03178. allantoinase. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP81006.

Entry information

Entry nameHYDL_ARTAU
AccessionPrimary (citable) accession number: P81006
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: April 16, 2014
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references