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Protein
Submitted name:

D-hydantoinase

Gene
N/A
Organism
Bacillus sp. AR9
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi58 – 581Manganese 1; via tele nitrogenCombined sources
Metal bindingi60 – 601Manganese 1; via tele nitrogenCombined sources
Metal bindingi150 – 1501Manganese 1Combined sources
Metal bindingi150 – 1501Manganese 2Combined sources
Metal bindingi183 – 1831Manganese 2; via pros nitrogenCombined sources
Metal bindingi239 – 2391Manganese 2; via tele nitrogenCombined sources
Metal bindingi315 – 3151Manganese 1Combined sources

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

HydrolaseImported

Keywords - Ligandi

ManganeseCombined sources, Metal-bindingCombined sources

Names & Taxonomyi

Protein namesi
Submitted name:
D-hydantoinaseImported (EC:3.5.2.2Imported)
OrganismiBacillus sp. AR9Imported
Taxonomic identifieri301298 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YNYX-ray2.30A/B1-461[»]
4KIRX-ray2.80A/B2-461[»]
4KQNX-ray2.80A/B2-460[»]
ProteinModelPortaliQ5DLU2.
SMRiQ5DLU2. Positions 2-460.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5DLU2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini49 – 436388Amidohydro-relInterPro annotationAdd
BLAST

Family and domain databases

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.

Q5DLU2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKWIRGGTV VTAADTYQAD VLIEGERVVA IGHQLSVNGA EEIDATGCYV
60 70 80 90 100
IPGGIDPHTH LDMPFGGTVT ADDFFTGTRA AAFGGTTSIV DFCLTKKGES
110 120 130 140 150
LKSAIATWHE KARGKAVIDY GFHLMIAEAN DQVLEELESV ISSEGITSLK
160 170 180 190 200
VFMAYKNVFQ ADDETLFKTL VKAKELGALV QVHAENGDVL DYLTKKALAE
210 220 230 240 250
GNTDPIYHAY TRPPEAEGEA TGRAIALTAL AGSQLYVVHV SCASAVQRIA
260 270 280 290 300
EAREKGWNVY GETCPQYLAL DVSIMDQPDF EGAKYVWSPP LREKWNQEVL
310 320 330 340 350
WSALKNGILQ TVGSDHCPFN FRGQKELGRG DFTKIPNGGP LIEDRLTILY
360 370 380 390 400
SEGVRQGRIS LNQFVDISST KAAKLFGMFP RKGTIAVGSD ADIVIFDPHV
410 420 430 440 450
KRTLSVETHH MNVDYNPFEG MEVYGEVVSV LSRGSFVVRD KQFVGQAGSG
460
QYIKRTTFEQ P
Length:461
Mass (Da):50,412
Last modified:March 29, 2005 - v1
Checksum:i54A202F5D9DED2F9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY650921 Genomic DNA. Translation: AAV65953.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY650921 Genomic DNA. Translation: AAV65953.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YNYX-ray2.30A/B1-461[»]
4KIRX-ray2.80A/B2-461[»]
4KQNX-ray2.80A/B2-460[»]
ProteinModelPortaliQ5DLU2.
SMRiQ5DLU2. Positions 2-460.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ5DLU2.

Family and domain databases

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...

Publicationsi

  1. "Molecular structure of D-hydantoinase from Bacillus sp. AR9: evidence for mercury inhibition."
    Radha Kishan K.V., Vohra R.M., Ganesan K., Agrawal V., Sharma V.M., Sharma R.
    J. Mol. Biol. 347:95-105(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: AR9Imported.
  2. "2.8 Angstrom Resolution Crystal Structure of D-Hydantoinase from Bacillus sp. AR9 in C2221 Space Group."
    Kumar V., Kishan K.V.R.
    Submitted (MAY-2013) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 2-460 IN COMPLEX WITH MANGANESE.
  3. "Crystal Structure of D-Hydantoinase from Bacillus sp. AR9 in C2221 space group."
    Kumar V., Kishan K.V.R.
    Submitted (MAY-2013) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 2-461 IN COMPLEX WITH MANGANESE.

Entry informationi

Entry nameiQ5DLU2_9BACI
AccessioniPrimary (citable) accession number: Q5DLU2
Entry historyi
Integrated into UniProtKB/TrEMBL: March 29, 2005
Last sequence update: March 29, 2005
Last modified: April 13, 2016
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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.