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Protein
Submitted name:

Alpha/beta hydrolase fold protein

Gene

aidH

Organism
Ochrobactrum sp. T63
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  • hydrolase activity, acting on ester bonds Source: CACAO

GO - Biological processi

  • metabolic process Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

HydrolaseImported

Protein family/group databases

ESTHERi9rhiz-d2j2t6. AHL-acylase.

Names & Taxonomyi

Protein namesi
Submitted name:
Alpha/beta hydrolase fold proteinImported
Gene namesi
Name:aidHImported
OrganismiOchrobactrum sp. T63Imported
Taxonomic identifieri680275 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeOchrobactrum

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4G5XX-ray1.29A/B1-271[»]
4G8BX-ray1.30A/B1-271[»]
4G8CX-ray1.11A/B1-271[»]
4G8DX-ray1.35A/B1-271[»]
4G9EX-ray1.09A/B1-271[»]
4G9GX-ray1.35A/B1-271[»]
ProteinModelPortaliD2J2T6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000639. Epox_hydrolase-like.
[Graphical view]
PfamiPF12697. Abhydrolase_6. 1 hit.
[Graphical view]
PRINTSiPR00111. ABHYDROLASE.
PR00412. EPOXHYDRLASE.
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequencei

Sequence statusi: Complete.

D2J2T6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTINYHELET SHGRIAVRES EGEGAPLLMI HGNSSSGAIF APQLEGEIGK
60 70 80 90 100
KWRVIAPDLP GHGKSTDAID PDRSYSMEGY ADAMTEVMQQ LGIADAVVFG
110 120 130 140 150
WSLGGHIGIE MIARYPEMRG LMITGTPPVA REEVGQGFKS GPDMALAGQE
160 170 180 190 200
IFSERDVESY ARSTCGEPFE ASLLDIVART DGRARRIMFE KFGSGTGGNQ
210 220 230 240 250
RDIVAEAQLP IAVVNGRDEP FVELDFVSKV KFGNLWEGKT HVIDNAGHAP
260 270
FREAPAEFDA YLARFIRDCT Q
Length:271
Mass (Da):29,549
Last modified:February 9, 2010 - v1
Checksum:i992896298C1E9BEB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GQ849010 Genomic DNA. Translation: ACZ73823.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GQ849010 Genomic DNA. Translation: ACZ73823.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4G5XX-ray1.29A/B1-271[»]
4G8BX-ray1.30A/B1-271[»]
4G8CX-ray1.11A/B1-271[»]
4G8DX-ray1.35A/B1-271[»]
4G9EX-ray1.09A/B1-271[»]
4G9GX-ray1.35A/B1-271[»]
ProteinModelPortaliD2J2T6.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERi9rhiz-d2j2t6. AHL-acylase.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000639. Epox_hydrolase-like.
[Graphical view]
PfamiPF12697. Abhydrolase_6. 1 hit.
[Graphical view]
PRINTSiPR00111. ABHYDROLASE.
PR00412. EPOXHYDRLASE.
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "AidH, an alpha/beta-hydrolase fold family member from an Ochrobactrum sp. strain, is a novel N-acylhomoserine lactonase."
    Mei G.Y., Yan X.X., Turak A., Luo Z.Q., Zhang L.Q.
    Appl. Environ. Microbiol. 76:4933-4942(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: T63Imported.
  2. "High-resolution structures of AidH complexes provide insights into a novel catalytic mechanism for N-acyl homoserine lactonase."
    Gao A., Mei G.Y., Liu S., Wang P., Tang Q., Liu Y.P., Wen H., An X.M., Zhang L.Q., Yan X.X., Liang D.C.
    Acta Crystallogr. D 69:82-91(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.09 ANGSTROMS).

Entry informationi

Entry nameiD2J2T6_9RHIZ
AccessioniPrimary (citable) accession number: D2J2T6
Entry historyi
Integrated into UniProtKB/TrEMBL: February 9, 2010
Last sequence update: February 9, 2010
Last modified: June 24, 2015
This is version 18 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

External Data

Dasty 3

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 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.