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Protein

Epoxide hydrolase B

Gene

MT1988

Organism
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Could be involved in detoxification of extraneous host-cell epoxides. Catalyzes the hydrolysis of small aromatic epoxide-containing substrates such as trans-1,3-diphenylpropene oxide, trans and cis-stilbene oxide, and terpenoid epoxide.1 Publication

Catalytic activityi

An epoxide + H2O = a glycol.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei104Nucleophile1 Publication1
Sitei164Contributes to the formation of an oxyanion binding site for the epoxide oxygen of substrate1 Publication1
Sitei272Contributes to the formation of an oxyanion binding site for the epoxide oxygen of substrate1 Publication1
Sitei302Plays an orienting role for the imidazole group of His-3331 Publication1
Active sitei333Proton acceptor1 Publication1

GO - Molecular functioni

  • epoxide hydrolase B activity Source: MTBBASE
  • protein homodimerization activity Source: MTBBASE
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Detoxification

Enzyme and pathway databases

BioCyciMTBCDC1551:GT3Z-6390-MONOMER.

Protein family/group databases

ESTHERimyctu-ephB. Epoxide_hydrolase.
MEROPSiS33.971.

Names & Taxonomyi

Protein namesi
Recommended name:
Epoxide hydrolase B1 Publication (EC:3.3.2.101 Publication)
Short name:
EHB1 Publication
Gene namesi
Ordered Locus Names:MT1988
OrganismiMycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Taxonomic identifieri83331 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001020 Componenti: Chromosome

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL1795155.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004385871 – 356Epoxide hydrolase BAdd BLAST356

Interactioni

Subunit structurei

Homodimer.1 Publication

GO - Molecular functioni

  • protein homodimerization activity Source: MTBBASE

Chemistry databases

BindingDBiP95276.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2E3JX-ray2.10A2-356[»]
2ZJFX-ray2.40A2-356[»]
ProteinModelPortaliP95276.
SMRiP95276.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini28 – 129AB hydrolase-1Sequence analysisAdd BLAST102

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000028073.
OrthoDBiPOG091H0A6K.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000639. Epox_hydrolase-like.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PRINTSiPR00111. ABHYDROLASE.
PR00412. EPOXHYDRLASE.
SUPFAMiSSF53474. SSF53474. 2 hits.

Sequencei

Sequence statusi: Complete.

P95276-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQVHRILNC RGTRIHAVAD SPPDQQGPLV VLLHGFPESW YSWRHQIPAL
60 70 80 90 100
AGAGYRVVAI DQRGYGRSSK YRVQKAYRIK ELVGDVVGVL DSYGAEQAFV
110 120 130 140 150
VGHDWGAPVA WTFAWLHPDR CAGVVGISVP FAGRGVIGLP GSPFGERRPS
160 170 180 190 200
DYHLELAGPG RVWYQDYFAV QDGIITEIEE DLRGWLLGLT YTVSGEGMMA
210 220 230 240 250
ATKAAVDAGV DLESMDPIDV IRAGPLCMAE GARLKDAFVY PETMPAWFTE
260 270 280 290 300
ADLDFYTGEF ERSGFGGPLS FYHNIDNDWH DLADQQGKPL TPPALFIGGQ
310 320 330 340 350
YDVGTIWGAQ AIERAHEVMP NYRGTHMIAD VGHWIQQEAP EETNRLLLDF

LGGLRP
Length:356
Mass (Da):39,297
Last modified:July 1, 1997 - v2
Checksum:i64D10EA23A0D57AF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000516 Genomic DNA. Translation: AAK46260.1.
PIRiF70636.
RefSeqiWP_003899091.1. NZ_KK341227.1.

Genome annotation databases

EnsemblBacteriaiAAK46260; AAK46260; MT1988.
KEGGimtc:MT1988.
PATRICi18126144. VBIMycTub22151_2184.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000516 Genomic DNA. Translation: AAK46260.1.
PIRiF70636.
RefSeqiWP_003899091.1. NZ_KK341227.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2E3JX-ray2.10A2-356[»]
2ZJFX-ray2.40A2-356[»]
ProteinModelPortaliP95276.
SMRiP95276.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

BindingDBiP95276.
ChEMBLiCHEMBL1795155.

Protein family/group databases

ESTHERimyctu-ephB. Epoxide_hydrolase.
MEROPSiS33.971.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK46260; AAK46260; MT1988.
KEGGimtc:MT1988.
PATRICi18126144. VBIMycTub22151_2184.

Phylogenomic databases

HOGENOMiHOG000028073.
OrthoDBiPOG091H0A6K.

Enzyme and pathway databases

BioCyciMTBCDC1551:GT3Z-6390-MONOMER.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000639. Epox_hydrolase-like.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PRINTSiPR00111. ABHYDROLASE.
PR00412. EPOXHYDRLASE.
SUPFAMiSSF53474. SSF53474. 2 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiEPHB_MYCTO
AccessioniPrimary (citable) accession number: P95276
Secondary accession number(s): F2GGS7, Q7D7R2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 30, 2016
Last sequence update: July 1, 1997
Last modified: November 30, 2016
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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.