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Protein

D-hydantoinase

Gene
N/A
Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

Enzyme 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

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-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

Complete GO annotation...

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
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 11Combined sources9
Beta strandi16 – 23Combined sources8
Beta strandi25 – 34Combined sources10
Beta strandi49 – 52Combined sources4
Beta strandi54 – 59Combined sources6
Beta strandi66 – 68Combined sources3
Helixi74 – 83Combined sources10
Beta strandi86 – 93Combined sources8
Helixi101 – 112Combined sources12
Turni113 – 115Combined sources3
Beta strandi117 – 125Combined sources9
Helixi131 – 142Combined sources12
Beta strandi148 – 155Combined sources8
Turni156 – 159Combined sources4
Helixi163 – 176Combined sources14
Beta strandi179 – 183Combined sources5
Helixi187 – 199Combined sources13
Helixi206 – 210Combined sources5
Helixi214 – 231Combined sources18
Beta strandi234 – 237Combined sources4
Helixi243 – 254Combined sources12
Beta strandi258 – 263Combined sources6
Helixi265 – 269Combined sources5
Helixi272 – 275Combined sources4
Helixi281 – 285Combined sources5
Helixi296 – 306Combined sources11
Beta strandi307 – 309Combined sources3
Turni321 – 324Combined sources4
Helixi325 – 328Combined sources4
Helixi332 – 334Combined sources3
Turni342 – 344Combined sources3
Helixi345 – 352Combined sources8
Helixi354 – 356Combined sources3
Helixi361 – 368Combined sources8
Helixi370 – 375Combined sources6
Turni379 – 381Combined sources3
Beta strandi393 – 403Combined sources11
Turni406 – 408Combined sources3
Beta strandi411 – 414Combined sources4
Turni417 – 420Combined sources4
Beta strandi422 – 432Combined sources11
Beta strandi435 – 439Combined sources5

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...

Miscellaneous databases

EvolutionaryTraceiQ45515.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

CDDicd01314. D-HYD. 1 hit.
Gene3Di2.30.40.10. 2 hits.
InterProiIPR006680. Amidohydro-rel.
IPR011778. Hydantoinase/dihydroPyrase.
IPR011059. Metal-dep_hydrolase_composite.
IPR032466. Metal_Hydrolase.
[Graphical view]
PfamiPF01979. Amidohydro_1. 1 hit.
[Graphical view]
SUPFAMiSSF51338. SSF51338. 2 hits.
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.

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...

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. 2 hits.
InterProiIPR006680. Amidohydro-rel.
IPR011778. Hydantoinase/dihydroPyrase.
IPR011059. Metal-dep_hydrolase_composite.
IPR032466. Metal_Hydrolase.
[Graphical view]
PfamiPF01979. Amidohydro_1. 1 hit.
[Graphical view]
SUPFAMiSSF51338. SSF51338. 2 hits.
SSF51556. SSF51556. 1 hit.
TIGRFAMsiTIGR02033. D-hydantoinase. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiHYDA_GEOSE
AccessioniPrimary (citable) accession number: Q45515
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 90 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

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 one 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.