Glycoside Hydrolase Family 14

Known Activitiesβ-amylase (EC 3.2.1.2)
Mechanism Inverting
3D Structure Status( β / α ) 8
Catalytic Nucleophile/BaseGlu (experimental)
Catalytic Proton DonorGlu (experimental)
External resourcesHOMSTRAD; InterPro; PFAM; PRINTS; PROSITE;
Commercial Enzyme Provider(s)MEGAZYME;
Statistics GenBank accession (536); Uniprot accession (295); PDB accession (44); 3D entries (5); cryst (1)
All (296) Bacteria (31) Eukaryota (265) Structure (5 - 1 cryst) Characterized (29)
Bacteria
Protein Name EC#OrganismGenBankUniprotPDB/3D
 β-amylase (SpoII) 3.2.1.2 Bacillus cereus VAR. MYCOIDES BAA34650.1
BAA75890.1
P36924.2
Q9Z4N9
1B90[A]
1B9Z[A]
1ITC[A]
1ITD
1ITJ
1J0Y[A,B,C,D]
1J0Z[A,B,C,D]
1J10[A,B,C,D]
1J11[A,B,C,D]
1J12[A,B,C,D]
1J18[A]
1VEM[A]
1VEN[A]
1VEO[A]
1VEP[A]
5BCA[A,B,C,D]
 β-amylase 3.2.1.2 Bacillus circulans NCIB 11033 CAA68578.1 P06547.1  
 β-amylase (BamM) 3.2.1.2 Bacillus megaterium DSM 319 ADF37268.1
CAB61483.1
Q9RM92  
 multidomain α-amylase / β-amylase 3.2.1.2 Paenibacillus polymyxa AAA85446.1
CAA68344.1
P21543.1 cryst
 β-amylase 3.2.1.2 Paenibacillus sp. KCTC8848P AAK69489.1 Q934J0  
 β-amylase 3.2.1.2 Thermoanaerobacterium thermosulfurigenes EM1 AAA23204.1 P19584.1  
Eukaryota
Protein Name EC#OrganismGenBankUniprotPDB/3D
 β-amylase 3.2.1.2 Achlya bisexualis AAK31632.1 Q8LPX0  
 β-amylase (Ram1;Atβ-Amy;BAM5;BMY1;At4g15210) 3.2.1.2 Arabidopsis thaliana AAA32737.1
AAB34026.1
AAL11567.1
AAM98288.1
AEE83568.1
AEE83569.1
BAA07842.1
BAE98501.1
BAH19577.1
CAB10300.1
CAB78563.1
NP_567460.1
P25853.1
Q0WWJ7
 
 β-amylase (BAM2;BMY9At4g00490) 3.2.1.2 Arabidopsis thaliana AAC13634.1
AEE81889.1
CAB80858.1
CAW93885.1
CAW99422.1
CBD02717.1
NP_191958.2
O65258  
 β-amylase (ct-Bmy;BAM3;BMY8;At4g17090) 3.2.1.2 Arabidopsis thaliana AAK96508.1
AAL31225.1
AAM65134.1
AAO00663.1
AAO00664.1
ACX05372.1
AEE83848.1
CAB46051.1
CAB58423.1
CAB80980.1
NP_567523.1
O23553
Q941A5
Q9SMW0
 
 β-amylase (BAM1;BMY7;TR-BAMY;At3g23920) 3.2.1.2 Arabidopsis thaliana AAK56281.1
AAL67089.1
AAL77747.1
AAM20167.1
AEE76832.1
BAB03009.1
BAE98433.1
NP_189034.1
Q9LIR6  
 β-amylase 3.2.1.2 Calystegia sepium AAG44882.1 Q9FQ07  
 β-amylase 3.2.1.2 Castanea crenata AAK30294.1 Q9AT14  
 β-amylase (Bmy1) 3.2.1.2 Glycine max AAA33941.1
AAY40266.1
AAZ38831.1
AAZ38832.1
BAA09462.1
BAA20453.1
BAD93288.1
BAD93289.1
BAD93290.1
BAD93291.1
CAA50551.1
P10538.3
Q42795
1BFN[A]
1BTC[A]
1BYA[A]
1BYB[A]
1BYC[A]
1BYD[A]
1Q6C[A]
1Q6D[A]
1Q6E[A]
1Q6F[A]
1Q6G[A]
1UKO[A,B,C,D]
1UKP[A,B,C,D]
1V3H[A]
1V3I[A]
1WDP[A]
1WDQ[A]
1WDR[A]
1WDS[A]
2DQX[A]
 β-amylase (Bmy1) 3.2.1.2 Hordeum vulgare AAC67245.1
AAC67246.1
AAG25637.1
AAG25638.1
AAR18251.1
ACF05414.1
ACF05415.1
ACN24987.1
ADB54608.1
BAA04815.1
BAA08741.1
BAA09793.1
BAB39391.1
BAF93949.1
BAF93959.1
CAA36556.1
CAC16789.1
CAX51376.1
P16098.1
P82993
Q9AVJ8
Q9FSI3
Q9FUK6
Q9FUK7
Q9SB23
Q9SBH7
1B1Y[A]
2XFF[A]
2XFR[A]
2XFY[A]
2XG9[A]
2XGB[A]
2XGI[A]
 β-amylase (Bmy1;AmyB;β-Amy) 3.2.1.2 Ipomoea batatas AAM27213.1
BAA00828.1
BAA02286.1
P10537.4
Q8LRT8
1FA2[A]
 β-amylase (BMY1;BA1) 3.2.1.2 Medicago sativa AAD04188.1 O22585.1  
 β-amylase (Bamy2;OsBamy2;Os03g0141200) 3.2.1.2 Oryza sativa Japonica Group BAF10840.1
BAG91188.1
Q10RZ1  
 β-amylase (Bamy1;OsBamy1;Os10g0465700) 3.2.1.2 Oryza sativa Japonica Group AAK27799.1
AAP54185.1
BAF26712.1
BAG90332.1
CAW93915.1
CAW99452.1
CBD02742.1
NP_921898.1
Q9AV88  
 β-amylase (RsBamy1) 3.2.1.2 Raphanus sativus BAH20736.1 C8KH73  
 β-amylase 3.2.1.2 Saprolegnia ferax ATCC36051 AAK57827.1 Q94G72  
 β-amylase 3.2.1.2 Saprolegnia parasitica CBS 540.67 AAL73210.1 Q8W266  
 β-amylase (Bmy1) 3.2.1.2 Secale cereale CAA77817.1 Q08335  
 β-amylase (PCT-BMYI) 3.2.1.2 Solanum tuberosum AAK84008.1
CAD61986.1
CAW93938.1
CAW99475.1
CBD02761.1
Q94EU9  
 β-amylase 3.2.1.2 Solanum tuberosum AAW04779.1
CAW99445.1
CBD02737.1
   
 β-amylase 3.2.1.2 Triticum aestivum CAA76131.1 Q9ZR48  
 β-amylase 3.2.1.2 Triticum aestivum CAA67128.1 P93594  
 β-amylase (Bmy1) 3.2.1.2 Vigna unguiculata CAA12395.1 O64407.1  
 β-amylase (Bmy1) 3.2.1.2 Zea mays AAD15902.1
CAA81091.1
P55005
Q9SYS1
 

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
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