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P19531 (AMYM_GEOSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Maltogenic alpha-amylase

EC=3.2.1.133
Alternative name(s):
Glucan 1,4-alpha-maltohydrolase
Gene names
Name:amyM
OrganismGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifier1422 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Protein attributes

Sequence length719 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Converts starch into maltose.

Catalytic activity

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.

Cofactor

Binds 3 calcium ions per subunit.

Subunit structure

Monomer.

Biotechnological use

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

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

Contains 1 CBM20 (carbohydrate binding type-20) domain.

Contains 1 IPT/TIG domain.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionglucan 1,4-alpha-maltohydrolase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

starch binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3333 Ref.1
Chain34 – 719686Maltogenic alpha-amylase
PRO_0000001422

Regions

Domain532 – 60877IPT/TIG
Domain609 – 719111CBM20

Sites

Active site2611Nucleophile By similarity
Active site2891Proton donor By similarity
Metal binding541Calcium 1
Metal binding561Calcium 1; via carbonyl oxygen
Metal binding591Calcium 1
Metal binding601Calcium 1
Metal binding811Calcium 1; via carbonyl oxygen
Metal binding831Calcium 1
Metal binding1091Calcium 2
Metal binding1101Calcium 2; via carbonyl oxygen
Metal binding1121Calcium 2
Metal binding1341Calcium 2
Metal binding1351Calcium 2
Metal binding1641Calcium 3
Metal binding2171Calcium 3; via carbonyl oxygen
Metal binding2311Calcium 3
Metal binding2651Calcium 3; via carbonyl oxygen
Site3621Transition state stabilizer By similarity

Experimental info

Sequence conflict1091D → N in AAA22233. Ref.1
Sequence conflict254 – 2563Missing in AAA22233. Ref.1
Sequence conflict3711S → SK in AAA22233. Ref.1
Sequence conflict379 – 39113ALAFI…RGTPS → RLLSFSLRGVRPP Ref.1

Secondary structure

............................................................................................................................... 719
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P19531 [UniParc].

Last modified August 15, 2003. Version 2.
Checksum: B40B61AD964F7D89

FASTA71978,676
        10         20         30         40         50         60 
MKKKTLSLFV GLMLLIGLLF SGSLPYNPNA AEASSSASVK GDVIYQIIID RFYDGDTTNN 

        70         80         90        100        110        120 
NPAKSYGLYD PTKSKWKMYW GGDLEGVRQK LPYLKQLGVT TIWLSPVLDN LDTLAGTDNT 

       130        140        150        160        170        180 
GYHGYWTRDF KQIEEHFGNW TTFDTLVNDA HQNGIKVIVD FVPNHSTPFK ANDSTFAEGG 

       190        200        210        220        230        240 
ALYNNGTYMG NYFDDATKGY FHHNGDISNW DDRYEAQWKN FTDPAGFSLA DLSQENGTIA 

       250        260        270        280        290        300 
QYLTDAAVQL VAHGADGLRI DAVKHFNSGF SKSLADKLYQ KKDIFLVGEW YGDDPGTANH 

       310        320        330        340        350        360 
LEKVRYANNS GVNVLDFDLN TVIRNVFGTF TQTMYDLNNM VNQTGNEYKY KENLITFIDN 

       370        380        390        400        410        420 
HDMSRFLSVN SNKANLHQAL AFILTSRGTP SIYYGTEQYM AGGNDPYNRG MMPAFDTTTT 

       430        440        450        460        470        480 
AFKEVSTLAG LRRNNAAIQY GTTTQRWINN DVYIYERKFF NDVVLVAINR NTQSSYSISG 

       490        500        510        520        530        540 
LQTALPNGSY ADYLSGLLGG NGISVSNGSV ASFTLAPGAV SVWQYSTSAS APQIGSVAPN 

       550        560        570        580        590        600 
MGIPGNVVTI DGKGFGTTQG TVTFGGVTAT VKSWTSNRIE VYVPNMAAGL TDVKVTAGGV 

       610        620        630        640        650        660 
SSNLYSYNIL SGTQTSVVFT VKSAPPTNLG DKIYLTGNIP ELGNWSTDTS GAVNNAQGPL 

       670        680        690        700        710 
LAPNYPDWFY VFSVPAGKTI QFKFFIKRAD GTIQWENGSN HVATTPTGAT GNITVTWQN 

« Hide

References

[1]"Cloning of a maltogenic alpha-amylase from Bacillus stearothermophilus."
Diderichsen B., Christiansen L.
FEMS Microbiol. Lett. 56:53-60(1988)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 34-45.
Strain: C599.
[2]"X-ray structure of Novamyl, the five-domain ''maltogenic'' alpha-amylase from Bacillus stearothermophilus: maltose and acarbose complexes at 1.7-A resolution."
Dauter Z., Dauter M., Brzozowski A.M., Christensen S., Borchert T.V., Beier L., Wilson K.S., Davies G.J.
Biochemistry 38:8385-8392(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), SEQUENCE REVISION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M36539 Genomic DNA. Translation: AAA22233.1.
PIRS28784.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QHOX-ray1.70A34-719[»]
1QHPX-ray1.70A34-719[»]
ProteinModelPortalP19531.
SMRP19531. Positions 34-719.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM20. Carbohydrate-Binding Module Family 20.
GH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA3.2.1.133. 623.

Family and domain databases

Gene3D2.60.40.10. 2 hits.
2.60.40.1180. 1 hit.
3.20.20.80. 2 hits.
InterProIPR006048. A-amylase_b_C.
IPR006046. Alpha_amylase.
IPR013784. Carb-bd-like_fold.
IPR002044. CBM_fam20.
IPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
[Graphical view]
PANTHERPTHR10357. PTHR10357. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
PF00686. CBM_20. 1 hit.
PF01833. TIG. 1 hit.
[Graphical view]
PRINTSPR00110. ALPHAAMYLASE.
SMARTSM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
SM01065. CBM_2. 1 hit.
[Graphical view]
SUPFAMSSF49452. SSF49452. 1 hit.
SSF51445. SSF51445. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEPS51166. CBM20. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP19531.

Entry information

Entry nameAMYM_GEOSE
AccessionPrimary (citable) accession number: P19531
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: August 15, 2003
Last modified: November 13, 2013
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries