Mechanism | Retaining a |
---|---|
Clan | GH-H |
3D Structure Status | ( β / α ) 8 barrel |
Catalytic Nucleophile/Base | Asp (experimental) |
Catalytic Proton Donor | Glu (experimental) |
Note | New: many members have been assigned to subfamilies as described by Stam et al. (2006) Protein Eng Des Sel. 19, 555-562 (PMID: 17085431) |
External resources | CAZypedia; EBI Protein of the Month; HOMSTRAD; PDB Molecule of the Month; PRINTS; |
Commercial Enzyme Provider(s) | MEGAZYME; PROZOMIX; |
Statistics | GenBank accession (1217); Uniprot accession (43); PDB accession (36); 3D entries (14); cryst (0) |
Bacteria | |||||||||||||||||||||||||||
Protein Name | EC# | Organism | GenBank | Uniprot |
| Subf | |||||||||||||||||||||
α-amylase (AliC) | 3.2.1.1 | Alicyclobacillus sp. 18711 | AWX66236.1 | A0A3P8MUS3 |
|
5 | |||||||||||||||||||||
α-amylase (Amy1;AmyA;AmyB) | 3.2.1.1 | Alkalimonas amylolytica N10 | AAQ01675.1 | Q6WUB6 |
|
5 | |||||||||||||||||||||
α-amylase domain-containing protein | Alkalimonas sp. NCh-2 | WP_345916233.1 |
|
5 | |||||||||||||||||||||||
α-amylase (Amy1;AmyQ;BAA) | 3.2.1.1 | Bacillus amyloliquefaciens | AAA22191.1 AAE12381.1 AAE13947.1 AAE37101.1 AAE59727.1 AAE62349.1 AAN20003.1 AAN27445.1 AAN99911.1 AAP02211.1 AAR63623.1 AAR76030.1 AAS26291.1 AAY72173.1 ABJ43095.1 ABJ43099.1 ABN29369.1 ACK07344.1 ACP75069.1 ACS10035.1 ACW26904.1 CAA01489.1 CAA23430.1 CAC16484.1 CAC88551.1 CAD19035.1 CAD20678.1 CAD26702.1 CAD67517.1 CAD88112.1 |
P00692 |
|
5 | |||||||||||||||||||||
α-amylase (AmyA;AmyL;AmyS;BLA) | 3.2.1.1 | Bacillus licheniformis 584 / ATCC 27811 | AAA22226.1 AAA22193.1 AAA22240.1 AAN99913.1 AAO26743.1 AAT46561.1 ACM17155.1 CAA01355.1 CAA03075.1 CAA26981.1 CAC16483.1 CAC88550.1 CAD19034.1 CAD20677.1 CAD26701.1 CAD26706.1 CAD88111.1 CAV31708.1 |
P06278 Q208A7 Q6GWE2 |
|
5 | |||||||||||||||||||||
amylase (BliAmy) | 3.2.1.1 | Bacillus licheniformis ATCC 9945a | AEM05860.1 | I3P686 |
|
5 | |||||||||||||||||||||
alkaline α-amylase (AmyK) | 3.2.1.1 | Bacillus sp. (in: firmicutes) KSM-1378 | AAR68734.1 AAN99906.1 AAR63625.1 AAV01045.1 ABE15847.1 ABI05897.1 ABY03536.1 ACS10038.1 ACW26917.1 BAA32431.1 CAD35985.1 CAD38135.1 CAV31709.1 |
O82839 |
|
5 | |||||||||||||||||||||
maltohexaose-forming amylase | 3.2.1.98 | Bacillus sp. 707 | AAA22231.1 AAE59728.1 AAE62350.1 AAP02212.1 AAR63620.1 AAS26292.1 AAY06019.1 AAY72174.1 ACK07346.1 ACP75071.1 ACS10032.1 ACW26905.1 |
P19571 |
|
5 | |||||||||||||||||||||
α-amylase (AmyK38) | 3.2.1.1 | Bacillus sp. KSM-K38 | CAC39917.1 AAN18958.1 AAV01046.1 ABA16539.1 ABI05896.1 ABY03537.1 ACS10039.1 BAB71820.1 CAD35986.1 CAD38133.1 CAJ00040.1 CAJ28078.1 |
Q93I48 |
|
5 | |||||||||||||||||||||
α-amylase (AmyS) | 3.2.1.1 | Geobacillus stearothermophilus DY5 / PHI300 / NZ-3 | AAA22235.2 AAA22227.1 AAA22241.1 AAE13948.1 AAE37102.1 AAE59725.1 AAE62347.1 AAN20004.1 AAN27446.1 AAP02209.1 AAR63624.1 AAS26289.1 AAY06018.1 AAY72171.1 ABJ43096.1 ABN29370.1 ACK07342.1 ACP75067.1 ACW26902.1 CAA26547.1 CAC16485.1 CAC88549.1 CAD19033.1 CAD20676.1 CAD26700.1 CAD67515.1 |
P06279 |
|
5 | |||||||||||||||||||||
maltotetraose-forming amylase | Geobacillus stearothermophilus STB04 | AIV43245.1 |
|
5 | |||||||||||||||||||||||
α-amylase B (AmyB) | 3.2.1.1 | Halothermothrix orenii H 168 | ACL70573.1 ACB11224.1 |
B2CCC1 B8CZ54 |
|
5 | |||||||||||||||||||||
α-amylase | 3.2.1.1 | Sutcliffiella halmapala | CAD26699.1 AAE12377.1 AAE59724.1 AAE59730.1 AAE62346.1 AAE62352.1 AAP02208.1 AAP02214.1 AAS26288.1 AAS26294.1 AAY06017.1 AAY72170.1 AAY72176.1 ACK07341.1 ACP75066.1 ACS10037.1 ACW26901.1 CAC88548.1 CAD19032.1 CAD20675.1 CAD67514.1 |
|
5 | ||||||||||||||||||||||
α-amylase (Amy63) | 3.2.1.1 | Vibrio alginolyticus 129-63 | ALP73597.1 | A0A0S2UQL4 |
|
5 | |||||||||||||||||||||
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