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Protein
Submitted name:

Esterase/lipase

Gene

estE5

Organism
uncultured bacterium
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

BRENDAi3.1.1.79. 744.

Protein family/group databases

ESTHERi9bact-Q0GMU2. Hormone-sensitive_lipase_like_1.

Names & Taxonomyi

Protein namesi
Submitted name:
Esterase/lipaseImported
Gene namesi
Name:estE5Imported
Organismiuncultured bacteriumImported
Taxonomic identifieri77133 [NCBI]
Taxonomic lineageiBacteriaenvironmental samples

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3FAKX-ray1.90A1-297[»]
3G9TX-ray1.96A1-297[»]
3G9UX-ray2.20A1-297[»]
3G9ZX-ray2.20A1-297[»]
3H17X-ray2.50A1-297[»]
3H18X-ray2.40A1-297[»]
3H19X-ray2.30A1-297[»]
3H1AX-ray2.50A1-297[»]
3H1BX-ray2.10A1-297[»]
3L1HX-ray2.40A1-297[»]
3L1IX-ray2.20A1-297[»]
3L1JX-ray2.00A1-297[»]
3V9AX-ray2.07A1-297[»]
ProteinModelPortaliQ0GMU2.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ0GMU2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini70 – 271202Abhydrolase_3InterPro annotationAdd
BLAST

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR013094. AB_hydrolase_3.
IPR002168. Lipase_GDXG_HIS_AS.
IPR033140. Lipase_GDXG_put_SER_AS.
[Graphical view]
PfamiPF07859. Abhydrolase_3. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS01173. LIPASE_GDXG_HIS. 1 hit.
PS01174. LIPASE_GDXG_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q0GMU2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGPEIVKLK KILREKAVPP GTEVPLDVMR KGMEKVAFKA ADDIQVEQVT
60 70 80 90 100
VAGCAAEWVR APGCQAGKAI LYLHGGGYVM GSINTHRSMV GEISRASQAA
110 120 130 140 150
ALLLDYRLAP EHPFPAAVED GVAAYRWLLD QGFKPQHLSI SGDSAGGGLV
160 170 180 190 200
LAVLVSARDQ GLPMPASAIP ISPWADMTCT NDSFKTRAEA DPMVAPGGIN
210 220 230 240 250
KMAARYLNGA DAKHPYASPN FANLKGLPPL LIHVGRDEVL LDDSIKLDAK
260 270 280 290
AKADGVKSTL EIWDDMIHVW HAFHPMLPEG KQAIVRVGEF MREQWAA
Length:297
Mass (Da):31,916
Last modified:October 3, 2006 - v1
Checksum:iD17646B4436A2B5E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ842023 Genomic DNA. Translation: ABI18351.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ842023 Genomic DNA. Translation: ABI18351.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3FAKX-ray1.90A1-297[»]
3G9TX-ray1.96A1-297[»]
3G9UX-ray2.20A1-297[»]
3G9ZX-ray2.20A1-297[»]
3H17X-ray2.50A1-297[»]
3H18X-ray2.40A1-297[»]
3H19X-ray2.30A1-297[»]
3H1AX-ray2.50A1-297[»]
3H1BX-ray2.10A1-297[»]
3L1HX-ray2.40A1-297[»]
3L1IX-ray2.20A1-297[»]
3L1JX-ray2.00A1-297[»]
3V9AX-ray2.07A1-297[»]
ProteinModelPortaliQ0GMU2.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERi9bact-Q0GMU2. Hormone-sensitive_lipase_like_1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.1.1.79. 744.

Miscellaneous databases

EvolutionaryTraceiQ0GMU2.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR013094. AB_hydrolase_3.
IPR002168. Lipase_GDXG_HIS_AS.
IPR033140. Lipase_GDXG_put_SER_AS.
[Graphical view]
PfamiPF07859. Abhydrolase_3. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS01173. LIPASE_GDXG_HIS. 1 hit.
PS01174. LIPASE_GDXG_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Kim S., Kim M., Yeo Y., Yoon S., Koo B.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "Structural and functional analysis of a novel EstE5 belonging to the subfamily of hormone-sensitive lipase."
    Nam K.H., Kim M.Y., Kim S.J., Priyadarshi A., Lee W.H., Hwang K.Y.
    Biochem. Biophys. Res. Commun. 379:553-556(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  3. "The crystal structure of an HSL-homolog EstE5 complex with PMSF reveals a unique configuration that inhibits the nucleophile Ser144 in catalytic triads."
    Nam K.H., Kim S.J., Priyadarshi A., Kim H.S., Hwang K.Y.
    Biochem. Biophys. Res. Commun. 389:247-250(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS).
  4. "Structural and biological characterization of EstE5."
    Hwang K.Y., Nam K.H.
    Submitted (FEB-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS).
  5. "Crystal structure of EstE5, was soaked by organic solvent."
    Hwang K.Y., Nam K.H.
    Submitted (APR-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS).
  6. "Structural insights into the noninvasive inhibition of HSL-homolog EstE5 by organic solvents and metal ions."
    Nam K.H., Hwang K.Y.
    Submitted (DEC-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS).
  7. "Crystal structure of Esterase/Lipase from uncultured bacterium."
    Kim I.J., Nam K.H.
    Submitted (DEC-2011) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS).

Entry informationi

Entry nameiQ0GMU2_9BACT
AccessioniPrimary (citable) accession number: Q0GMU2
Entry historyi
Integrated into UniProtKB/TrEMBL: October 3, 2006
Last sequence update: October 3, 2006
Last modified: July 6, 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.