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D2J2T6

- D2J2T6_9RHIZ

UniProt

D2J2T6 - D2J2T6_9RHIZ

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Protein
Submitted name: Alpha/beta hydrolase fold protein
Gene
aidH
Organism
Ochrobactrum sp. T63
Status
Unreviewed - Annotation score: 1 out of 5 - Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. hydrolase activity Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

HydrolaseImported

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:
PDBe
RCSB PDB
PDBj
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.

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]
PRINTSiPR00111. ABHYDROLASE.
PR00412. EPOXHYDRLASE.
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequencei

Sequence statusi: Complete.

D2J2T6-1 [UniParc]FASTAAdd to Basket

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MTINYHELET SHGRIAVRES EGEGAPLLMI HGNSSSGAIF APQLEGEIGK    50
KWRVIAPDLP GHGKSTDAID PDRSYSMEGY ADAMTEVMQQ LGIADAVVFG 100
WSLGGHIGIE MIARYPEMRG LMITGTPPVA REEVGQGFKS GPDMALAGQE 150
IFSERDVESY ARSTCGEPFE ASLLDIVART DGRARRIMFE KFGSGTGGNQ 200
RDIVAEAQLP IAVVNGRDEP FVELDFVSKV KFGNLWEGKT HVIDNAGHAP 250
FREAPAEFDA YLARFIRDCT Q 271
Length:271
Mass (Da):29,549
Last modified:February 9, 2010 - v1
Checksum:i992896298C1E9BEB
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
GQ849010 Genomic DNA. Translation: ACZ73823.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
GQ849010 Genomic DNA. Translation: ACZ73823.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4G5X X-ray 1.29 A/B 1-271 [» ]
4G8B X-ray 1.30 A/B 1-271 [» ]
4G8C X-ray 1.11 A/B 1-271 [» ]
4G8D X-ray 1.35 A/B 1-271 [» ]
4G9E X-ray 1.09 A/B 1-271 [» ]
4G9G X-ray 1.35 A/B 1-271 [» ]
ProteinModelPortali D2J2T6.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.40.50.1820. 1 hit.
InterProi IPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000639. Epox_hydrolase-like.
[Graphical view ]
PRINTSi PR00111. ABHYDROLASE.
PR00412. EPOXHYDRLASE.
SUPFAMi SSF53474. SSF53474. 1 hit.
ProtoNeti Search...

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 11, 2014
This is version 12 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureImported

External Data

Dasty 3

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