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Protein

D-hydantoinase

Gene
N/A
Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the stereospecific hydrolysis of the cyclic amide bond of D-hydantoin. Has no activity on dihydropyrimidines.

Cofactori

Zn2+2 Publications, Ni2+2 Publications, Co2+2 Publications, Mn2+2 PublicationsNote: Binds 2 Zn2+ ions per subunit. Can also use Ni2+, Co2+ or Mn2+.2 Publications

Activity regulationi

Completely inhibited by p-chloromercuribenzoate and partially inhibited by metal chelating agents.1 Publication

Temperature dependencei

The optimal activity is at pH 8.8 for manganese-containing form and pH 8.5 for cobalt-containing form. The oligomer is thermostable and retains full initial activity at 40-60 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi58Zinc 1Combined sources1 Publication1
Metal bindingi60Zinc 1Combined sources1 Publication1
Metal bindingi150Zinc 1; via carbamate groupCombined sources1 Publication1
Metal bindingi150Zinc 2; via carbamate groupCombined sources1 Publication1
Binding sitei155SubstrateBy similarity1
Metal bindingi183Zinc 2Combined sources1 Publication1
Metal bindingi239Zinc 2Combined sources1 Publication1
Binding sitei288Substrate; via amide nitrogen and carbonyl oxygenBy similarity1
Metal bindingi315Zinc 1Combined sources1 Publication1
Binding sitei337Substrate; via carbonyl oxygenBy similarity1

GO - Molecular functioni

Keywordsi

Molecular functionHydrolase
LigandMetal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.5.2.2 623

Names & Taxonomyi

Protein namesi
Recommended name:
D-hydantoinase (EC:3.5.2.-)
OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifieri1422 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Subcellular locationi

GO - Cellular componenti

Pathology & Biotechi

Chemistry databases

DrugBankiDB03801 Lysine Nz-Carboxylic Acid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001659331 – 471D-hydantoinaseAdd BLAST471

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei150N6-carboxylysine1 Publication1

Post-translational modificationi

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

Interactioni

Subunit structurei

Homotetramer.1 Publication

Structurei

Secondary structure

1471
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ45515
SMRiQ45515
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ45515

Family & Domainsi

Sequence similaritiesi

Family and domain databases

CDDicd01314 D-HYD, 1 hit
Gene3Di2.30.40.10, 1 hit
InterProiView protein in InterPro
IPR006680 Amidohydro-rel
IPR011778 Hydantoinase/dihydroPyrase
IPR011059 Metal-dep_hydrolase_composite
IPR032466 Metal_Hydrolase
PfamiView protein in Pfam
PF01979 Amidohydro_1, 1 hit
SUPFAMiSSF51338 SSF51338, 1 hit
SSF51556 SSF51556, 1 hit
TIGRFAMsiTIGR02033 D-hydantoinase, 1 hit

Sequencei

Sequence statusi: Complete.

Q45515-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTKLIKNGTI VTATDIYEAD LLIQDGKIAV IGRNLDESGA EVIDATGCYV
60 70 80 90 100
FPGGIDPHTH LDMPFGGTVT KDDFESGTIA AAFGGTTTII DFCLTNKGEP
110 120 130 140 150
LKKAIETWHN KATGKAVIDY GFHLMISEIT DDVLEELPKV IEEEGITSFK
160 170 180 190 200
VFMAYKDVFQ ADDGTLYRTL VAAKELGALV MVHAENGDVI DYLTKKALED
210 220 230 240 250
GHTDPIYHAL TRPPELEGEA TGRACQLTEL AGSQLYVVHV SCAQAVEKIA
260 270 280 290 300
EARNKGLNVW GETCPQYLVL DQSYLEKPNF EGAKYVWSPP LREKWHQEVL
310 320 330 340 350
WNALKNGQLQ TLGSDQCSFD FKGQKELGRG DFTKIPNGGP IIEDRVSILF
360 370 380 390 400
SEGVKKGRIT LNQFVDIVST RIAKLFGLFP KKGTIAVGAD ADLVIFDPTV
410 420 430 440 450
ERVISAETHH MAVDYNPFEG MKVTGEPVSV LCRGEFVVRD KQFVGKPGYG
460 470
QYVKRAKYGA LMADQDVVKM S
Length:471
Mass (Da):51,725
Last modified:November 1, 1996 - v1
Checksum:iFB75A507727292FB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S73773 Genomic DNA Translation: AAC60487.1
PIRiJC2310

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S73773 Genomic DNA Translation: AAC60487.1
PIRiJC2310

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K1DX-ray3.01A/B/C/D/E/F/G/H1-459[»]
ProteinModelPortaliQ45515
SMRiQ45515
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

DrugBankiDB03801 Lysine Nz-Carboxylic Acid

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.5.2.2 623

Miscellaneous databases

EvolutionaryTraceiQ45515

Family and domain databases

CDDicd01314 D-HYD, 1 hit
Gene3Di2.30.40.10, 1 hit
InterProiView protein in InterPro
IPR006680 Amidohydro-rel
IPR011778 Hydantoinase/dihydroPyrase
IPR011059 Metal-dep_hydrolase_composite
IPR032466 Metal_Hydrolase
PfamiView protein in Pfam
PF01979 Amidohydro_1, 1 hit
SUPFAMiSSF51338 SSF51338, 1 hit
SSF51556 SSF51556, 1 hit
TIGRFAMsiTIGR02033 D-hydantoinase, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiHYDA_GEOSE
AccessioniPrimary (citable) accession number: Q45515
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: November 7, 2018
This is version 96 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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