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UniProtKB - P19531 (AMYM_GEOSE)
Protein
Maltogenic alpha-amylase
Gene
amyM
Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Functioni
Converts starch into maltose.
Catalytic activityi
- Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive alpha-maltose residues from the non-reducing ends of the chains. EC:3.2.1.133
Cofactori
Ca2+1 PublicationNote: Binds 3 Ca2+ ions per subunit.1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 54 | Calcium 1Combined sources1 Publication | 1 | |
Metal bindingi | 56 | Calcium 1; via carbonyl oxygenCombined sources1 Publication | 1 | |
Metal bindingi | 59 | Calcium 1Combined sources1 Publication | 1 | |
Metal bindingi | 60 | Calcium 1Combined sources1 Publication | 1 | |
Metal bindingi | 81 | Calcium 1; via carbonyl oxygenCombined sources1 Publication | 1 | |
Metal bindingi | 83 | Calcium 1Combined sources1 Publication | 1 | |
Metal bindingi | 109 | Calcium 2Combined sources1 Publication | 1 | |
Metal bindingi | 110 | Calcium 2; via carbonyl oxygenCombined sources1 Publication | 1 | |
Metal bindingi | 112 | Calcium 2Combined sources1 Publication | 1 | |
Binding sitei | 126 | SubstrateBy similarity | 1 | |
Metal bindingi | 134 | Calcium 2Combined sources1 Publication | 1 | |
Metal bindingi | 135 | Calcium 2Combined sources1 Publication | 1 | |
Metal bindingi | 164 | Calcium 3Combined sources1 Publication | 1 | |
Binding sitei | 165 | SubstrateBy similarity | 1 | |
Metal bindingi | 217 | Calcium 3; via carbonyl oxygenCombined sources1 Publication | 1 | |
Metal bindingi | 231 | Calcium 3Combined sources1 Publication | 1 | |
Binding sitei | 259 | SubstrateBy similarity | 1 | |
Active sitei | 261 | NucleophileBy similarity | 1 | |
Metal bindingi | 265 | Calcium 3; via carbonyl oxygenCombined sources1 Publication | 1 | |
Active sitei | 289 | Proton donorBy similarity | 1 | |
Binding sitei | 292 | Substrate; via amide nitrogenBy similarity | 1 | |
Binding sitei | 362 | SubstrateBy similarity | 1 | |
Sitei | 362 | Transition state stabilizerBy similarity | 1 | |
Binding sitei | 409 | SubstrateBy similarity | 1 |
GO - Molecular functioni
- alpha-amylase activity Source: InterPro
- glucan 1,4-alpha-maltohydrolase activity Source: UniProtKB-EC
- metal ion binding Source: UniProtKB-KW
- starch binding Source: InterPro
GO - Biological processi
- carbohydrate metabolic process Source: UniProtKB-KW
Keywordsi
Molecular function | Glycosidase, Hydrolase |
Biological process | Carbohydrate metabolism |
Ligand | Calcium, Metal-binding |
Enzyme and pathway databases
BRENDAi | 3.2.1.133, 623 |
Protein family/group databases
CAZyi | CBM20, Carbohydrate-Binding Module Family 20 GH13, Glycoside Hydrolase Family 13 |
Names & Taxonomyi
Protein namesi | Recommended name: Maltogenic alpha-amylase (EC:3.2.1.133)Alternative name(s): Glucan 1,4-alpha-maltohydrolase |
Gene namesi | Name:amyM |
Organismi | Geobacillus stearothermophilus (Bacillus stearothermophilus) |
Taxonomic identifieri | 1422 [NCBI] |
Taxonomic lineagei | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Geobacillus |
Pathology & Biotechi
Biotechnological usei
Used in the food industry to prevent bread from staling. Sold under the name Novamyl by Novozymes.Curated
Chemistry databases
DrugBanki | DB03971, Acarbose Derived Hexasaccharide DB03323, Maltose |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 33 | 1 PublicationAdd BLAST | 33 | |
ChainiPRO_0000001422 | 34 – 719 | Maltogenic alpha-amylaseAdd BLAST | 686 |
Interactioni
Subunit structurei
Monomer.
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P19531 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P19531 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 532 – 608 | IPT/TIGAdd BLAST | 77 | |
Domaini | 609 – 719 | CBM20PROSITE-ProRule annotationAdd BLAST | 111 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 264 – 265 | Substrate bindingBy similarity | 2 |
Sequence similaritiesi
Belongs to the glycosyl hydrolase 13 family.Curated
Keywords - Domaini
SignalFamily and domain databases
CDDi | cd05820, CBM20_novamyl, 1 hit |
Gene3Di | 2.60.40.10, 2 hits 2.60.40.1180, 1 hit |
InterProi | View protein in InterPro IPR006048, A-amylase/branching_C IPR031319, A-amylase_C IPR006046, Alpha_amylase IPR013784, Carb-bd-like_fold IPR034849, CBM20_novamyl IPR002044, CBM_fam20 IPR006047, Glyco_hydro_13_cat_dom IPR013780, Glyco_hydro_b IPR017853, Glycoside_hydrolase_SF IPR013783, Ig-like_fold IPR014756, Ig_E-set IPR002909, IPT_dom |
Pfami | View protein in Pfam PF00128, Alpha-amylase, 1 hit PF02806, Alpha-amylase_C, 1 hit PF00686, CBM_20, 1 hit PF01833, TIG, 1 hit |
PRINTSi | PR00110, ALPHAAMYLASE |
SMARTi | View protein in SMART SM00642, Aamy, 1 hit SM00632, Aamy_C, 1 hit SM01065, CBM_2, 1 hit |
SUPFAMi | SSF49452, SSF49452, 1 hit SSF51445, SSF51445, 1 hit SSF81296, SSF81296, 1 hit |
PROSITEi | View protein in PROSITE PS51166, CBM20, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P19531-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MKKKTLSLFV GLMLLIGLLF SGSLPYNPNA AEASSSASVK GDVIYQIIID
60 70 80 90 100
RFYDGDTTNN NPAKSYGLYD PTKSKWKMYW GGDLEGVRQK LPYLKQLGVT
110 120 130 140 150
TIWLSPVLDN LDTLAGTDNT GYHGYWTRDF KQIEEHFGNW TTFDTLVNDA
160 170 180 190 200
HQNGIKVIVD FVPNHSTPFK ANDSTFAEGG ALYNNGTYMG NYFDDATKGY
210 220 230 240 250
FHHNGDISNW DDRYEAQWKN FTDPAGFSLA DLSQENGTIA QYLTDAAVQL
260 270 280 290 300
VAHGADGLRI DAVKHFNSGF SKSLADKLYQ KKDIFLVGEW YGDDPGTANH
310 320 330 340 350
LEKVRYANNS GVNVLDFDLN TVIRNVFGTF TQTMYDLNNM VNQTGNEYKY
360 370 380 390 400
KENLITFIDN HDMSRFLSVN SNKANLHQAL AFILTSRGTP SIYYGTEQYM
410 420 430 440 450
AGGNDPYNRG MMPAFDTTTT AFKEVSTLAG LRRNNAAIQY GTTTQRWINN
460 470 480 490 500
DVYIYERKFF NDVVLVAINR NTQSSYSISG LQTALPNGSY ADYLSGLLGG
510 520 530 540 550
NGISVSNGSV ASFTLAPGAV SVWQYSTSAS APQIGSVAPN MGIPGNVVTI
560 570 580 590 600
DGKGFGTTQG TVTFGGVTAT VKSWTSNRIE VYVPNMAAGL TDVKVTAGGV
610 620 630 640 650
SSNLYSYNIL SGTQTSVVFT VKSAPPTNLG DKIYLTGNIP ELGNWSTDTS
660 670 680 690 700
GAVNNAQGPL LAPNYPDWFY VFSVPAGKTI QFKFFIKRAD GTIQWENGSN
710
HVATTPTGAT GNITVTWQN
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 109 | D → N in AAA22233 (Ref. 1) Curated | 1 | |
Sequence conflicti | 254 – 256 | Missing in AAA22233 (Ref. 1) Curated | 3 | |
Sequence conflicti | 371 | S → SK in AAA22233 (Ref. 1) Curated | 1 | |
Sequence conflicti | 379 – 391 | ALAFI…RGTPS → RLLSFSLRGVRPP (Ref. 1) CuratedAdd BLAST | 13 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M36539 Genomic DNA Translation: AAA22233.1 |
PIRi | S28784 |
Genome annotation databases
KEGGi | ag:AAA22233 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M36539 Genomic DNA Translation: AAA22233.1 |
PIRi | S28784 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1QHO | X-ray | 1.70 | A | 34-719 | [»] | |
1QHP | X-ray | 1.70 | A | 34-719 | [»] | |
SMRi | P19531 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Chemistry databases
DrugBanki | DB03971, Acarbose Derived Hexasaccharide DB03323, Maltose |
Protein family/group databases
CAZyi | CBM20, Carbohydrate-Binding Module Family 20 GH13, Glycoside Hydrolase Family 13 |
Genome annotation databases
KEGGi | ag:AAA22233 |
Enzyme and pathway databases
BRENDAi | 3.2.1.133, 623 |
Miscellaneous databases
EvolutionaryTracei | P19531 |
Family and domain databases
CDDi | cd05820, CBM20_novamyl, 1 hit |
Gene3Di | 2.60.40.10, 2 hits 2.60.40.1180, 1 hit |
InterProi | View protein in InterPro IPR006048, A-amylase/branching_C IPR031319, A-amylase_C IPR006046, Alpha_amylase IPR013784, Carb-bd-like_fold IPR034849, CBM20_novamyl IPR002044, CBM_fam20 IPR006047, Glyco_hydro_13_cat_dom IPR013780, Glyco_hydro_b IPR017853, Glycoside_hydrolase_SF IPR013783, Ig-like_fold IPR014756, Ig_E-set IPR002909, IPT_dom |
Pfami | View protein in Pfam PF00128, Alpha-amylase, 1 hit PF02806, Alpha-amylase_C, 1 hit PF00686, CBM_20, 1 hit PF01833, TIG, 1 hit |
PRINTSi | PR00110, ALPHAAMYLASE |
SMARTi | View protein in SMART SM00642, Aamy, 1 hit SM00632, Aamy_C, 1 hit SM01065, CBM_2, 1 hit |
SUPFAMi | SSF49452, SSF49452, 1 hit SSF51445, SSF51445, 1 hit SSF81296, SSF81296, 1 hit |
PROSITEi | View protein in PROSITE PS51166, CBM20, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | AMYM_GEOSE | |
Accessioni | P19531Primary (citable) accession number: P19531 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | February 1, 1991 |
Last sequence update: | August 15, 2003 | |
Last modified: | February 23, 2022 | |
This is version 130 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencingDocuments
- Glycosyl hydrolases
Classification of glycosyl hydrolase families and list of entries - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families