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Protein

L-hydantoinase

Gene

lhyD

Organism
Arthrobacter aurescens
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.

Cofactori

Zn2+Note: Binds 2 Zn2+ ions per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi60 – 601Zinc 1
Metal bindingi62 – 621Zinc 1
Metal bindingi147 – 1471Zinc 1; via carbamate group
Metal bindingi147 – 1471Zinc 2; via carbamate group
Metal bindingi183 – 1831Zinc 2
Metal bindingi239 – 2391Zinc 2
Metal bindingi312 – 3121Zinc 1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.5.2.2. 441.

Names & Taxonomyi

Protein namesi
Recommended name:
L-hydantoinase (EC:3.5.2.-)
Alternative name(s):
Non-ATP-dependent L-selective hydantoinase
Gene namesi
Name:lhyD
OrganismiArthrobacter aurescens
Taxonomic identifieri43663 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrococcaceaeArthrobacter

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 458458L-hydantoinasePRO_0000165938Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei147 – 1471N6-carboxylysine1 Publication

Post-translational modificationi

Carbamylation allows a single lysine to coordinate two zinc ions.1 Publication

Interactioni

Subunit structurei

Homotetramer.1 Publication

Structurei

Secondary structure

1
458
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 1312Combined sources
Beta strandi16 – 2510Combined sources
Beta strandi28 – 347Combined sources
Beta strandi41 – 466Combined sources
Beta strandi51 – 544Combined sources
Beta strandi56 – 627Combined sources
Helixi66 – 683Combined sources
Turni69 – 713Combined sources
Helixi75 – 8511Combined sources
Beta strandi87 – 926Combined sources
Beta strandi96 – 983Combined sources
Helixi103 – 11614Combined sources
Beta strandi118 – 1269Combined sources
Helixi132 – 1409Combined sources
Beta strandi145 – 1517Combined sources
Turni155 – 1573Combined sources
Helixi163 – 17614Combined sources
Beta strandi179 – 1835Combined sources
Helixi187 – 19913Combined sources
Helixi205 – 2117Combined sources
Helixi214 – 23118Combined sources
Beta strandi234 – 2374Combined sources
Helixi243 – 25412Combined sources
Beta strandi259 – 2635Combined sources
Helixi265 – 2684Combined sources
Helixi272 – 2743Combined sources
Helixi275 – 2784Combined sources
Helixi279 – 2824Combined sources
Helixi291 – 30212Combined sources
Helixi318 – 3203Combined sources
Helixi322 – 3254Combined sources
Helixi328 – 3303Combined sources
Turni338 – 3403Combined sources
Helixi341 – 3488Combined sources
Turni349 – 3535Combined sources
Helixi357 – 3648Combined sources
Helixi366 – 3716Combined sources
Turni375 – 3773Combined sources
Beta strandi378 – 3803Combined sources
Beta strandi389 – 3946Combined sources
Helixi402 – 4043Combined sources
Beta strandi406 – 4083Combined sources
Turni413 – 4164Combined sources
Beta strandi422 – 4287Combined sources
Beta strandi431 – 4355Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GKRX-ray2.60A/B/C/D1-458[»]
ProteinModelPortaliP81006.
SMRiP81006. Positions 1-451.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP81006.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di2.30.40.10. 2 hits.
InterProiIPR017593. Allantoinase.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
SUPFAMiSSF51338. SSF51338. 2 hits.
TIGRFAMsiTIGR03178. allantoinase. 1 hit.

Sequencei

Sequence statusi: Complete.

P81006-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFDVIVKNCR LVSSDGITEA DILVKDGKVA AISADTSDVE ASRTIDAGGK
60 70 80 90 100
FVMPGVVDEH VHIIDMDLKN RYGRFELDSE SAAVGGITTI IEMPITFPPT
110 120 130 140 150
TTLDAFLEKK KQAGQRLKVD FALYGGGVPG NLPEIRKMHD AGAVGFKSMM
160 170 180 190 200
AASVPGMFDA VSDGELFEIF QEIAACGSVI VVHAENETII QALQKQIKAA
210 220 230 240 250
GGKDMAAYEA SQPVFQENEA IQRALLLQKE AGCRLIVLHV SNPDGVELIH
260 270 280 290 300
QAQSEGQDVH CESGPQYLNI TTDDAERIGP YMKVAPPVRS AEMNIRLWEQ
310 320 330 340 350
LENGLIDTLG SDHGGHPVED KEPGWKDVWK AGNGALGLET SLPMMLTNGV
360 370 380 390 400
NKGRLSLERL VEVMCEKPAK LFGIYPQKGT LQVGSDADLL ILDLDIDTKV
410 420 430 440 450
DASQFRSLHK YSPFDGMPVT GAPVLTMVRG TVVAEKGEVL VEQGFGQFVT

RRNYEASK
Length:458
Mass (Da):49,597
Last modified:July 15, 1998 - v1
Checksum:iA0A78C492E461CFE
GO

Mass spectrometryi

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

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GKRX-ray2.60A/B/C/D1-458[»]
ProteinModelPortaliP81006.
SMRiP81006. Positions 1-451.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.5.2.2. 441.

Miscellaneous databases

EvolutionaryTraceiP81006.

Family and domain databases

Gene3Di2.30.40.10. 2 hits.
InterProiIPR017593. Allantoinase.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
SUPFAMiSSF51338. SSF51338. 2 hits.
TIGRFAMsiTIGR03178. allantoinase. 1 hit.
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiHYDL_ARTAU
AccessioniPrimary (citable) accession number: P81006
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: November 26, 2014
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.