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Protein
Submitted name:

Phosphotriesterase

Gene

GK1506

Organism
Geobacillus kaustophilus (strain HTA426)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Cofactori

a divalent metal cationUniRule annotationNote: Binds 2 divalent metal cations per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi23 – 231Divalent metal cation 1; via tele nitrogenUniRule annotation
Metal bindingi23 – 231Iron 1; via tele nitrogenCombined sources
Metal bindingi23 – 231Zinc 1; via tele nitrogenCombined sources
Metal bindingi25 – 251Divalent metal cation 1; via tele nitrogenUniRule annotation
Metal bindingi25 – 251Iron 1; via tele nitrogenCombined sources
Metal bindingi25 – 251Zinc 1; via tele nitrogenCombined sources
Metal bindingi99 – 991ManganeseCombined sources
Metal bindingi145 – 1451Divalent metal cation 1; via carbamate groupUniRule annotation
Metal bindingi145 – 1451Divalent metal cation 2; via carbamate groupUniRule annotation
Metal bindingi145 – 1451Iron 1Combined sources
Metal bindingi145 – 1451Iron 2Combined sources
Metal bindingi145 – 1451ManganeseCombined sources
Metal bindingi145 – 1451Zinc 1Combined sources
Metal bindingi145 – 1451Zinc 2Combined sources
Metal bindingi178 – 1781Divalent metal cation 2; via pros nitrogenUniRule annotation
Metal bindingi178 – 1781Iron 2; via pros nitrogenCombined sources
Metal bindingi178 – 1781Manganese; via pros nitrogenCombined sources
Metal bindingi178 – 1781Zinc 2; via pros nitrogenCombined sources
Metal bindingi206 – 2061Divalent metal cation 2; via tele nitrogenUniRule annotation
Metal bindingi206 – 2061Iron 2; via tele nitrogenCombined sources
Metal bindingi206 – 2061Manganese; via tele nitrogenCombined sources
Metal bindingi206 – 2061Zinc 2; via tele nitrogenCombined sources
Metal bindingi266 – 2661Divalent metal cation 1UniRule annotation
Metal bindingi266 – 2661Iron 1Combined sources

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

HydrolaseImported

Keywords - Ligandi

IronCombined sources, ManganeseCombined sources, Metal-bindingUniRule annotationCombined sources, ZincCombined sources

Enzyme and pathway databases

BioCyciGKAU235909:GJO7-1582-MONOMER.

Names & Taxonomyi

Protein namesi
Submitted name:
PhosphotriesteraseImported (EC:3.5.-.-Imported)
Gene namesi
Ordered Locus Names:GK1506Imported
OrganismiGeobacillus kaustophilus (strain HTA426)Imported
Taxonomic identifieri235909 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus
Proteomesi
  • UP000001172 Componenti: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei145 – 1451N6-carboxylysineUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi235909.GK1506.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3OJGX-ray1.60A1-326[»]
3ORWX-ray2.40A/B1-326[»]
3TN3X-ray1.60A/B1-326[»]
3TN4X-ray1.50A/B1-326[»]
3TN5X-ray1.75A/B1-326[»]
3TN6X-ray1.60A/B1-326[»]
3TNBX-ray1.60A/B1-326[»]
4H9TX-ray2.10A/B1-326[»]
4H9UX-ray2.10A/B1-326[»]
4H9VX-ray1.97A/B1-326[»]
4H9XX-ray2.20A/B1-326[»]
4H9YX-ray2.08A/B1-326[»]
4H9ZX-ray2.60A/B1-326[»]
4HA0X-ray1.90A/B1-326[»]
4WVXX-ray1.90A/B1-326[»]
5CH9X-ray1.90A/B1-234[»]
A/B239-326[»]
ProteinModelPortaliQ5KZU5.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5KZU5.

Family & Domainsi

Phylogenomic databases

eggNOGiENOG41080QX. Bacteria.
COG1735. LUCA.
HOGENOMiHOG000081700.
KOiK07048.
OMAiDKAVMSH.
OrthoDBiEOG628F2X.

Family and domain databases

InterProiIPR032466. Metal_Hydrolase.
IPR001559. Phosphotriesterase.
[Graphical view]
PANTHERiPTHR10819. PTHR10819. 1 hit.
PfamiPF02126. PTE. 1 hit.
[Graphical view]
SUPFAMiSSF51556. SSF51556. 1 hit.
PROSITEiPS51347. PHOSPHOTRIESTERASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5KZU5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEMVETVCG PVPVEQLGKT LIHEHFLFGY PGFQGDVTRG TFREDESLRV
60 70 80 90 100
AVEAAEKMKR HGIQTVVDPT PNDCGRNPAF LRRVAEETGL NIICATGYYY
110 120 130 140 150
EGEGAPPYFQ FRRLLGTAED DIYDMFMAEL TEGIADTGIK AGVIKLASSK
160 170 180 190 200
GRITEYEKMF FRAAARAQKE TGAVIITHTQ EGTMGPEQAA YLLEHGADPK
210 220 230 240 250
KIVIGHMCGN TDPDYHRKTL AYGVYIAFDR FGIQGMVGAP TDEERVRTLL
260 270 280 290 300
ALLRDGYEKQ IMLSHDTVNV WLGRPFTLPE PFAEMMKNWH VEHLFVNIIP
310 320
ALKNEGIRDE VLEQMFIGNP AALFSA
Length:326
Mass (Da):36,398
Last modified:February 1, 2005 - v1
Checksum:iBE870732724798F4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000043 Genomic DNA. Translation: BAD75791.1.
RefSeqiWP_011231002.1. NC_006510.1.

Genome annotation databases

EnsemblBacteriaiBAD75791; BAD75791; GK1506.
GeneIDi3183579.
KEGGigka:GK1506.
PATRICi21964305. VBIGeoKau81518_1620.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000043 Genomic DNA. Translation: BAD75791.1.
RefSeqiWP_011231002.1. NC_006510.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3OJGX-ray1.60A1-326[»]
3ORWX-ray2.40A/B1-326[»]
3TN3X-ray1.60A/B1-326[»]
3TN4X-ray1.50A/B1-326[»]
3TN5X-ray1.75A/B1-326[»]
3TN6X-ray1.60A/B1-326[»]
3TNBX-ray1.60A/B1-326[»]
4H9TX-ray2.10A/B1-326[»]
4H9UX-ray2.10A/B1-326[»]
4H9VX-ray1.97A/B1-326[»]
4H9XX-ray2.20A/B1-326[»]
4H9YX-ray2.08A/B1-326[»]
4H9ZX-ray2.60A/B1-326[»]
4HA0X-ray1.90A/B1-326[»]
4WVXX-ray1.90A/B1-326[»]
5CH9X-ray1.90A/B1-234[»]
A/B239-326[»]
ProteinModelPortaliQ5KZU5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi235909.GK1506.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD75791; BAD75791; GK1506.
GeneIDi3183579.
KEGGigka:GK1506.
PATRICi21964305. VBIGeoKau81518_1620.

Phylogenomic databases

eggNOGiENOG41080QX. Bacteria.
COG1735. LUCA.
HOGENOMiHOG000081700.
KOiK07048.
OMAiDKAVMSH.
OrthoDBiEOG628F2X.

Enzyme and pathway databases

BioCyciGKAU235909:GJO7-1582-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ5KZU5.

Family and domain databases

InterProiIPR032466. Metal_Hydrolase.
IPR001559. Phosphotriesterase.
[Graphical view]
PANTHERiPTHR10819. PTHR10819. 1 hit.
PfamiPF02126. PTE. 1 hit.
[Graphical view]
SUPFAMiSSF51556. SSF51556. 1 hit.
PROSITEiPS51347. PHOSPHOTRIESTERASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Thermoadaptation trait revealed by the genome sequence of thermophilic Geobacillus kaustophilus."
    Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H., Matsui S., Uchiyama I.
    Nucleic Acids Res. 32:6292-6303(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HTA426Imported.
  2. "Directed evolution of a thermostable quorum-quenching lactonase from the amidohydrolase superfamily."
    Chow J.Y., Xue B., Lee K.H., Tung A., Wu L., Robinson R.C., Yew W.S.
    J. Biol. Chem. 285:40911-40920(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH IRON AND ZINC.
  3. "Crystal structure of thermophilic phosphotriesterase from Geobacillus kaustophilus HTA426."
    Zheng B.S., Yu S.S., Zhang Y., Lou Z.Y., Feng Y.
    Submitted (SEP-2010) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS).
  4. "Engineering a thermostable lactonase for enhanced phosphotriesterase activity against organophosphate pesticides."
    An J., Zhang Z., Zhang Y., Feng Y., Wu G.
    Submitted (SEP-2011) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS), X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS), X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS).
  5. "Structural evidence of a productive active site architecture for an evolved quorum-quenching GKL lactonase."
    Xue B., Chow J.Y., Baldansuren A., Yap L.L., Gan Y.H., Dikanov S.A., Robinson R.C., Yew W.S.
    Biochemistry 52:2359-2370(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH IRON; MANGANESE AND ZINC.
  6. "Engineering a thermostable lactonase for enhanced phosphotriesterase activity against organophosphate pesticides."
    An J., Zhang Y., Yang G.Y., Feng Y.
    Submitted (NOV-2014) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS).
  7. "Active site loop architecture enhance the promiscuous PTE activity in lactonase from Geobacillus kaustophilus HTA426."
    Chen L.-Q.
    Submitted (JUL-2015) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-234 AND 239-326.

Entry informationi

Entry nameiQ5KZU5_GEOKA
AccessioniPrimary (citable) accession number: Q5KZU5
Entry historyi
Integrated into UniProtKB/TrEMBL: February 1, 2005
Last sequence update: February 1, 2005
Last modified: April 13, 2016
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

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.