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P81006

- HYDL_ARTAU

UniProt

P81006 - HYDL_ARTAU

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Protein

L-hydantoinase

Gene
lhyD
Organism
Arthrobacter aurescens
Status
Reviewed - Annotation score: 5 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

Binds 2 zinc 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

  1. allantoinase activity Source: InterPro
  2. cobalt ion binding Source: InterPro
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. allantoin catabolic process Source: InterPro
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-carboxylysine

Post-translational modificationi

Carbamylation allows a single lysine to coordinate two zinc ions.

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

3D structure databases

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

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

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MFDVIVKNCR LVSSDGITEA DILVKDGKVA AISADTSDVE ASRTIDAGGK    50
FVMPGVVDEH VHIIDMDLKN RYGRFELDSE SAAVGGITTI IEMPITFPPT 100
TTLDAFLEKK KQAGQRLKVD FALYGGGVPG NLPEIRKMHD AGAVGFKSMM 150
AASVPGMFDA VSDGELFEIF QEIAACGSVI VVHAENETII QALQKQIKAA 200
GGKDMAAYEA SQPVFQENEA IQRALLLQKE AGCRLIVLHV SNPDGVELIH 250
QAQSEGQDVH CESGPQYLNI TTDDAERIGP YMKVAPPVRS AEMNIRLWEQ 300
LENGLIDTLG SDHGGHPVED KEPGWKDVWK AGNGALGLET SLPMMLTNGV 350
NKGRLSLERL VEVMCEKPAK LFGIYPQKGT LQVGSDADLL ILDLDIDTKV 400
DASQFRSLHK YSPFDGMPVT GAPVLTMVRG TVVAEKGEVL VEQGFGQFVT 450
RRNYEASK 458
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:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1GKR X-ray 2.60 A/B/C/D 1-458 [» ]
ProteinModelPortali P81006.
SMRi P81006. Positions 1-451.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BRENDAi 3.5.2.2. 441.

Miscellaneous databases

EvolutionaryTracei P81006.

Family and domain databases

Gene3Di 2.30.40.10. 2 hits.
InterProi IPR017593. Allantoinase.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view ]
SUPFAMi SSF51338. SSF51338. 2 hits.
TIGRFAMsi TIGR03178. allantoinase. 1 hit.
ProtoNeti Search...

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: April 16, 2014
This is version 73 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

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