Glycoside Hydrolase Family 37

Known Activitiesα,α-trehalase (EC 3.2.1.28).
Mechanism Inverting
ClanGH-G
3D Structure Status( α / α ) 6
Catalytic Nucleophile/BaseGlu (inferred)
Catalytic Proton DonorAsp (inferred)
External resourcesCAZypedia; InterPro; PFAM; PRINTS; PROSITE;
Commercial Enzyme Provider(s)MEGAZYME;
Statistics GenBank accession (898); Uniprot accession (489); PDB accession (4); 3D entries (1); cryst (0)
Bacteria
Protein Name EC#OrganismGenBankUniprotPDB/3D
 trehalase (TreF) 3.2.1.28 Escherichia coli K-12 MG1655 AAB18495.1
AAC76544.1
NP_417976.1
P37196  
 α,α-trehalase (periplasmic) (TreA;OsmA) (Tre37A) 3.2.1.28 Escherichia coli K-12 MG1655 AAC74281.1
BAA36054.1
CAA33878.1
NP_415715.1
P13482.1 2JF4[A]
2JG0[A]
2JJB[A,B,C,D]
2WYN[A,B,C,D]
 trehalase (TreH) 3.2.1.28 Nostoc punctiforme IAM M-15 BAG70920.1
BAG85338.1
B5MF70
B6ZIV1
 
 trehalase (TreA;Rmar_0119) (periplasmic) 3.2.1.28 Rhodothermus marinus DSM 4252 ABC59065.1
ACY47027.1
D0MCR7  
Eukaryota
Protein Name EC#OrganismGenBankUniprotPDB/3D
 α,α-trehalase 3.2.1.28 Apis mellifera BAF81545.1 A8J4S9  
 trehalase (AtTre1;At4g24040/T19F6.30) (plasma membrane-bound) 3.2.1.28 Arabidopsis thaliana AAB63620.1
AAF22127.1
AAR23702.1
AEE84844.1
BAC43016.1
CAB51647.1
CAB69265.1
CAB81322.1
NP_194135.1
O22986
Q9SEH9
Q9SU50
 
 α,α-trehalase (TreB;AN5635.2) 3.2.1.28 Aspergillus nidulans FGSC A4 AAB99831.1
EAA62728.1
O42777.1  
 neutral trehalase (Nth1;BbNTH1) 3.2.1.28 Beauveria bassiana ARSEF2860 ABM16911.1    
 trehalase (Treh1) 3.2.1.28 Bombyx mori AAC60507.1
BAA02909.1
BAA13042.1
P32358.1  
 trehalase 2 (Treh2;Treh-2) 3.2.1.28 Bombyx mori KINSHU X SHOWA BAE45249.1 Q3MV18  
 trehalase (Ntc1) 3.2.1.28 Candida albicans 3153A CAA64476.1 P52494  
 neutral trehalase (Nth1) 3.2.1.28 Cryptococcus neoformans var. grubii H99 DAA05786.1 Q059G5  
 trehalase 1 (Tre1) 3.2.1.28 Glycine max AAD22970.1 Q9XEY7  
 trehalase (TreA;TreH) 3.2.1.28 Homo sapiens AAB50778.1
AAI09207.1
ABA67142.1
BAA24381.1
BAD96860.1
BAD96863.1
BAG52455.1
NP_009111.1
O43280.1  
 neutral trehalase (Nth1) 3.2.1.28 Kluyveromyces lactis CAA57181.1 P49381  
 neutral trehalase (TreA;KLLA0E17325g) 3.2.1.28 Kluyveromyces lactis NRRL Y-1140 CAG99815.1    
 trehalase 3.2.1.28 Magnaporthe grisea 4091-5-8 AAB88889.1 O42622  
 neutral trehalase (NTH1;MG09471.4) 3.2.1.28 Magnaporthe grisea 70-15 EAA53721.1
XP_364626.1
   
 neutral trehalase (NTH1) 3.2.1.28 Magnaporthe grisea GUY11 AAN46743.1 O42622  
 neutral trehalase (Ntl) 3.2.1.28 Metarhizium acridum CQM102 AAS67888.1
AAS67889.1
Q6Q5X7  
 neutral trehalase (NTL) 3.2.1.28 Metarhizium anisopliae var. anisopliae 2575 AAT68667.1 Q9HDE9  
 neutral trehalase (Nthi;Ntl1) 3.2.1.28 Metarhizium anisopliae var. anisopliae ME1 CAC17619.1
CAC17620.1
Q9HDE9  
 trehalase 3.2.1.28 Mus musculus AAF61430.1
AAH19214.1
AAK97631.1
AAT24328.1
BAB25963.1
NP_067456.1
Q8VCS8
Q9JLT2.1
 
 trehalase (TreB) 3.2.1.28 Neurospora crassa AAC01744.1 O42783
O42783.2
 
 trehalase (Tre-1) (soluble) 3.2.1.28 Nilaparvata lugens ACN85420.1 C0LZJ6  
 trehalase 1 (Treh-1) 3.2.1.28 Omphisa fuscidentalis ABO20846.1 A3RLQ5  
 trehalase (TreH;TreA) 3.2.1.28 Oryctolagus cuniculus AAA63460.1 P19813.1  
 neutral trehalase 1 (Nth1;Nth;YDR001c;YD8119.07c) 3.2.1.28 Saccharomyces cerevisiae S288c AAA66896.1
AAN20051.1
AAV19867.1
CAA46718.1
CAA88061.1
NP_010284.1
P32356.3
Q05216
 
 neutral trehalase 2 (Nth2;YBR001c;YBR0106) 3.2.1.28 Saccharomyces cerevisiae S288c CAA81270.1
CAA84937.1
NP_009555.1
P35172.1  
 neutral trehalase (Ntp1;SPBC660.07) 3.2.1.28 Schizosaccharomyces pombe 972h- CAA11904.1
CAA22527.1
NP_595086.1
O42893.1  
 trehalase 2 (Tre-2;Treh-2) 3.2.1.28 Spodoptera exigua ABU95354.1 A7XZC0  
 trehalase-1 (Tre-1) 3.2.1.28 Spodoptera exigua ABY86218.1 B0M0J3  
 trehalase (SfTre2) 3.2.1.28 Spodoptera frugiperda ACF94698.1 B5ATV4  
 trehalase (SfTre1) (midgut) 3.2.1.28 Spodoptera frugiperda ABE27189.1 Q0ZIF5  
 trehalase 3.2.1.28 Tenebrio molitor BAA01951.1 P32359.1  

Footnotes

Experimental characterization exclusively covers enzyme activities at present. If you are aware of any missing experimental characterization that should be mentioned here, we encourage you to send your comment and support of the experimental evidence, including an electronic copy or appropriate link to the support material (i.e., article(s), thesis, database, etc), to cazy@afmb.univ-mrs.fr.





Last update: 2012-01-31 © Copyright 1998-2012
AFMB - CNRS - Universités Aix-Marseille I & II