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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+1 PublicationNote: Binds 2 Zn2+ ions per subunit.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi60Zinc 1Combined sources1 Publication1
Metal bindingi62Zinc 1Combined sources1 Publication1
Metal bindingi147Zinc 1; via carbamate groupCombined sources1 Publication1
Metal bindingi147Zinc 2; via carbamate groupCombined sources1 Publication1
Metal bindingi183Zinc 2Combined sources1 Publication1
Metal bindingi239Zinc 2Combined sources1 Publication1
Metal bindingi312Zinc 1Combined sources1 Publication1

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 lineageiBacteriaActinobacteriaMicrococcalesMicrococcaceaePaenarthrobacter

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001659381 – 458L-hydantoinaseAdd BLAST458

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei147N6-carboxylysineCombined sources1 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

1458
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 13Combined sources12
Beta strandi16 – 25Combined sources10
Beta strandi28 – 34Combined sources7
Beta strandi41 – 46Combined sources6
Beta strandi51 – 54Combined sources4
Beta strandi56 – 62Combined sources7
Helixi66 – 68Combined sources3
Turni69 – 71Combined sources3
Helixi75 – 85Combined sources11
Beta strandi87 – 92Combined sources6
Beta strandi96 – 98Combined sources3
Helixi103 – 116Combined sources14
Beta strandi118 – 126Combined sources9
Helixi132 – 140Combined sources9
Beta strandi145 – 151Combined sources7
Turni155 – 157Combined sources3
Helixi163 – 176Combined sources14
Beta strandi179 – 183Combined sources5
Helixi187 – 199Combined sources13
Helixi205 – 211Combined sources7
Helixi214 – 231Combined sources18
Beta strandi234 – 237Combined sources4
Helixi243 – 254Combined sources12
Beta strandi259 – 263Combined sources5
Helixi265 – 268Combined sources4
Helixi272 – 274Combined sources3
Helixi275 – 278Combined sources4
Helixi279 – 282Combined sources4
Helixi291 – 302Combined sources12
Helixi318 – 320Combined sources3
Helixi322 – 325Combined sources4
Helixi328 – 330Combined sources3
Turni338 – 340Combined sources3
Helixi341 – 348Combined sources8
Turni349 – 353Combined sources5
Helixi357 – 364Combined sources8
Helixi366 – 371Combined sources6
Turni375 – 377Combined sources3
Beta strandi378 – 380Combined sources3
Beta strandi389 – 394Combined sources6
Helixi402 – 404Combined sources3
Beta strandi406 – 408Combined sources3
Turni413 – 416Combined sources4
Beta strandi422 – 428Combined sources7
Beta strandi431 – 435Combined sources5

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP81006.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di2.30.40.10. 2 hits.
InterProiIPR017593. Allantoinase.
IPR006680. Amidohydro-rel.
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.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GKRX-ray2.60A/B/C/D1-458[»]
ProteinModelPortaliP81006.
SMRiP81006.
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.
IPR006680. Amidohydro-rel.
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.
TIGRFAMsiTIGR03178. allantoinase. 1 hit.
ProtoNetiSearch...

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 2, 2016
This is version 83 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.