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Reviewed, UniProtKB/Swiss-Prot P81006 (HYDL_ARTAU)

Last modified March 3, 2009. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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 lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Micrococcaceae › Arthrobacter

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Protein attributes

Sequence length458 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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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

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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

1 ..................................................................................... 458
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P81006-1 [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

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References

[1]"Molecular evolution of hydantoinases."
May O., Habenicht A., Mattes R., Syldatk C., Siemann M.
Biol. Chem. 379:743-747(1998) [PubMed: 9687026] [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: 9650283] [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: 15299588] [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: 12093275] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH ZINC IONS, SUBUNIT, CARBAMYLATION AT LYS-147.

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Cross-references

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1GKRX-ray2.60A/B/C/D1-458[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA3.5.2.2. 21020.

Family and domain databases

InterProIPR006680. Amidohydro_1.
[Graphical view]
PfamPF01979. Amidohydro_1. 2 hits.
[Graphical view]
ProDomPD000518. DHOase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetSearch...

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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: March 3, 2009
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents