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Reviewed, UniProtKB/Swiss-Prot P32818 (AMYM_BACAD)

Last modified June 16, 2009. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Maltogenic alpha-amylase
    EC=3.2.1.133
Alternative name(s):
    Glucan 1,4-alpha-maltohydrolase
OrganismBacillus acidopullulyticus
Taxonomic identifier28030 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length586 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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 1 calcium ion per subunit By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   LigandCalcium
Metal-binding
   Molecular functionGlycosidase
Hydrolase
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functioncalcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

glucan 1,4-alpha-maltohydrolase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 586586Maltogenic alpha-amylase
PRO_0000054295

Sites

Active site3281Nucleophile By similarity
Active site3571Proton donor By similarity
Active site4241 By similarity
Metal binding1471Calcium By similarity
Metal binding1521Calcium By similarity
Metal binding1531Calcium By similarity
Metal binding1721Calcium; via carbonyl oxygen By similarity
Metal binding1741Calcium By similarity

Sequences

Sequence LengthMass (Da)Tools
P32818-1 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: EEC050711DCD627A

FASTA58668,520
        10         20         30         40         50         60 
MFREAIYHRP KDNYAYACAN GELHIRIRTK KDDMKEVTLV YGDTYEFDDN KWTYSTAHMK 

        70         80         90        100        110        120 
KTGSDQLFDY WLASVTPRYK RLRYGFIVND RKDSTCFTEK GFYPEPPVND ISYYFSFPYV 

       130        140        150        160        170        180 
NQADIFQAPE WVKDTVWYQI FPERFANGNK DNDPDGTLPW GSREPEIDNF FGGDLEGVIE 

       190        200        210        220        230        240 
HIDYLKELGI GGIYFTPIFK AHSNHKYDTI DYMEIDPQFG TKETLKKLID VCHKNGIKVM 

       250        260        270        280        290        300 
LDAVFNHSGV FFPPFQDVVE KGKNSKYQDW FHIREFPLVM EPRPNYDTFG FTSSMPKFKT 

       310        320        330        340        350        360 
ENPEVKEYLL EVGRYWVREF DIDGWRLDVA NEVSHAFWRE FRREVKAIKP DLYILGEIWH 

       370        380        390        400        410        420 
DSLPWLRGDQ FDAVMNYPLS TNIVNLFANQ SVSVKEFVEN MSHVIHMYPD TVNEAAFNLV 

       430        440        450        460        470        480 
GSHDTPRILT QCGEDVERLK QVFVLLLTFI GTPCIYYGDE IGLTGGQDPG CRKCMEWNPD 

       490        500        510        520        530        540 
QQNRELLQHV RKLIQLRSEN PLLANEGELT FVPPKNEEDP CLAYTKSNEE KTIMIIINKS 

       550        560        570        580 
KNSVEYPLSF DAAEQTVKNL WNQEQLILQN GQTLELKAND FKILEF 

« Hide

References

[1]"Molecular genetics analysis of a maltogenic amylase gene of Bacillus acidopullulyticus."
Kelly A.P., Diderichsen B., Jorgensen S.T., McConnell D.J.
Submitted (APR-1993) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

Z22520 Genomic DNA. Translation: CAA80246.1.
PIRS34731.

3D structure databases

HSSPHSSP built from PDB template 1J0H based on UniProtKB P38940.
ModBaseSearch...

Protein family/group databases

CAZyCBM34. Carbohydrate-Binding Module Family 34.
GH13. Glycoside Hydrolase Family 13.

Enzyme and pathway databases

BRENDA3.2.1.133. 97501.

Family and domain databases

InterProIPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat.
IPR004185. Glyco_hydro_13_lg-like.
IPR006589. Glyco_hydro_13_sub_cat.
IPR013781. Glyco_hydro_sg_catalytic.
IPR013783. Ig-like_fold.
[Graphical view]
Gene3DG3DSA:2.60.40.1180. Glyco_hydro_13_b. 1 hit.
G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
G3DSA:2.60.40.10. Ig-like_fold. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
PF02903. Alpha-amylase_N. 1 hit.
[Graphical view]
SMARTSM00642. Aamy. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAMYM_BACAD
AccessionPrimary (citable) accession number: P32818
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: June 16, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents