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Protein

Maltogenic alpha-amylase

Gene

amyM

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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.

Cofactori

Ca2+1 PublicationNote: Binds 3 Ca2+ ions per subunit.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi54Calcium 1Combined sources1 Publication1
Metal bindingi56Calcium 1; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi59Calcium 1Combined sources1 Publication1
Metal bindingi60Calcium 1Combined sources1 Publication1
Metal bindingi81Calcium 1; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi83Calcium 1Combined sources1 Publication1
Metal bindingi109Calcium 2Combined sources1 Publication1
Metal bindingi110Calcium 2; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi112Calcium 2Combined sources1 Publication1
Binding sitei126SubstrateBy similarity1
Metal bindingi134Calcium 2Combined sources1 Publication1
Metal bindingi135Calcium 2Combined sources1 Publication1
Metal bindingi164Calcium 3Combined sources1 Publication1
Binding sitei165SubstrateBy similarity1
Metal bindingi217Calcium 3; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi231Calcium 3Combined sources1 Publication1
Binding sitei259SubstrateBy similarity1
Active sitei261NucleophileBy similarity1
Metal bindingi265Calcium 3; via carbonyl oxygenCombined sources1 Publication1
Active sitei289Proton donorBy similarity1
Binding sitei292Substrate; via amide nitrogenBy similarity1
Binding sitei362SubstrateBy similarity1
Sitei362Transition state stabilizerBy similarity1
Binding sitei409SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.2.1.133. 623.

Protein family/group databases

CAZyiCBM20. 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
OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifieri1422 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Pathology & Biotechi

Biotechnological usei

Used in the food industry to prevent bread from staling. Sold under the name Novamyl by Novozymes.Curated

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 331 PublicationAdd BLAST33
ChainiPRO_000000142234 – 719Maltogenic alpha-amylaseAdd BLAST686

Proteomic databases

PRIDEiP19531.

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1719
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi44 – 47Combined sources4
Helixi49 – 51Combined sources3
Helixi57 – 59Combined sources3
Helixi63 – 65Combined sources3
Helixi84 – 89Combined sources6
Helixi91 – 97Combined sources7
Beta strandi101 – 104Combined sources4
Beta strandi108 – 110Combined sources3
Helixi121 – 123Combined sources3
Beta strandi126 – 133Combined sources8
Turni135 – 137Combined sources3
Helixi140 – 152Combined sources13
Beta strandi156 – 161Combined sources6
Beta strandi165 – 170Combined sources6
Turni177 – 180Combined sources4
Beta strandi182 – 184Combined sources3
Beta strandi187 – 190Combined sources4
Beta strandi192 – 194Combined sources3
Turni196 – 198Combined sources3
Helixi213 – 218Combined sources6
Turni224 – 226Combined sources3
Beta strandi227 – 232Combined sources6
Helixi237 – 252Combined sources16
Beta strandi257 – 260Combined sources4
Helixi263 – 265Combined sources3
Helixi268 – 281Combined sources14
Beta strandi285 – 288Combined sources4
Helixi300 – 309Combined sources10
Beta strandi313 – 315Combined sources3
Helixi317 – 327Combined sources11
Helixi334 – 347Combined sources14
Helixi351 – 353Combined sources3
Helixi366 – 369Combined sources4
Helixi373 – 384Combined sources12
Beta strandi387 – 393Combined sources7
Helixi396 – 398Combined sources3
Turni405 – 408Combined sources4
Helixi420 – 434Combined sources15
Helixi436 – 440Combined sources5
Beta strandi442 – 448Combined sources7
Beta strandi450 – 459Combined sources10
Beta strandi462 – 469Combined sources8
Beta strandi476 – 478Combined sources3
Beta strandi487 – 490Combined sources4
Turni493 – 498Combined sources6
Beta strandi503 – 506Combined sources4
Beta strandi513 – 515Combined sources3
Beta strandi520 – 525Combined sources6
Beta strandi533 – 542Combined sources10
Beta strandi547 – 553Combined sources7
Beta strandi561 – 564Combined sources4
Beta strandi571 – 574Combined sources4
Beta strandi576 – 582Combined sources7
Beta strandi589 – 597Combined sources9
Beta strandi605 – 609Combined sources5
Beta strandi611 – 623Combined sources13
Beta strandi632 – 639Combined sources8
Helixi640 – 642Combined sources3
Turni643 – 645Combined sources3
Turni663 – 666Combined sources4
Beta strandi667 – 675Combined sources9
Beta strandi679 – 687Combined sources9
Beta strandi693 – 695Combined sources3
Beta strandi701 – 704Combined sources4
Beta strandi707 – 716Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QHOX-ray1.70A34-719[»]
1QHPX-ray1.70A34-719[»]
ProteinModelPortaliP19531.
SMRiP19531.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19531.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini532 – 608IPT/TIGAdd BLAST77
Domaini609 – 719CBM20PROSITE-ProRule annotationAdd BLAST111

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni264 – 265Substrate bindingBy similarity2

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated
Contains 1 CBM20 (carbohydrate binding type-20) domain.PROSITE-ProRule annotation
Contains 1 IPT/TIG domain.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
2.60.40.1180. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR006048. A-amylase/branching_C.
IPR031319. A-amylase_C.
IPR006046. Alpha_amylase.
IPR013784. Carb-bd-like_fold.
IPR002044. CBM_fam20.
IPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013780. Glyco_hydro_b.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 3 hits.
PfamiPF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
PF00686. CBM_20. 1 hit.
PF01833. TIG. 1 hit.
[Graphical view]
PRINTSiPR00110. ALPHAAMYLASE.
SMARTiSM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
SM01065. CBM_2. 1 hit.
[Graphical view]
SUPFAMiSSF49452. SSF49452. 1 hit.
SSF51445. SSF51445. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS51166. CBM20. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P19531-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:719
Mass (Da):78,676
Last modified:August 15, 2003 - v2
Checksum:iB40B61AD964F7D89
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti109D → N in AAA22233 (Ref. 1) Curated1
Sequence conflicti254 – 256Missing in AAA22233 (Ref. 1) Curated3
Sequence conflicti371S → SK in AAA22233 (Ref. 1) Curated1
Sequence conflicti379 – 391ALAFI…RGTPS → RLLSFSLRGVRPP (Ref. 1) CuratedAdd BLAST13

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M36539 Genomic DNA. Translation: AAA22233.1.
PIRiS28784.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M36539 Genomic DNA. Translation: AAA22233.1.
PIRiS28784.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QHOX-ray1.70A34-719[»]
1QHPX-ray1.70A34-719[»]
ProteinModelPortaliP19531.
SMRiP19531.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM20. Carbohydrate-Binding Module Family 20.
GH13. Glycoside Hydrolase Family 13.

Proteomic databases

PRIDEiP19531.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.2.1.133. 623.

Miscellaneous databases

EvolutionaryTraceiP19531.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
2.60.40.1180. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR006048. A-amylase/branching_C.
IPR031319. A-amylase_C.
IPR006046. Alpha_amylase.
IPR013784. Carb-bd-like_fold.
IPR002044. CBM_fam20.
IPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013780. Glyco_hydro_b.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 3 hits.
PfamiPF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
PF00686. CBM_20. 1 hit.
PF01833. TIG. 1 hit.
[Graphical view]
PRINTSiPR00110. ALPHAAMYLASE.
SMARTiSM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
SM01065. CBM_2. 1 hit.
[Graphical view]
SUPFAMiSSF49452. SSF49452. 1 hit.
SSF51445. SSF51445. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS51166. CBM20. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAMYM_GEOSE
AccessioniPrimary (citable) accession number: P19531
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: August 15, 2003
Last modified: November 2, 2016
This is version 114 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, Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.