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P81006

- HYDL_ARTAU

UniProt

P81006 - HYDL_ARTAU

Protein

L-hydantoinase

Gene

lhyD

Organism
Arthrobacter aurescens
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 74 (01 Oct 2014)
      Sequence version 1 (15 Jul 1998)
      Previous versions | rss
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    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

    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 – 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.
    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

    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: October 1, 2014
    This is version 74 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