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Q04977 (AMYM_BACLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 31, 2011. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:blmA
OrganismBacillus licheniformis
Taxonomic identifier1402 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length578 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Converts starch into maltose. In contrary to other maltogenic alpha-amylases BlmA cannot hydrolyze 1,4-alpha-glucosidic linkage next to 1,6-alpha-glucosidic linkages.

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.

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   Molecular functionGlycosidase
Hydrolase
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functioncation binding

Inferred from electronic annotation. Source: InterPro

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 – 578578Maltogenic alpha-amylase
PRO_0000054296

Sequences

Sequence LengthMass (Da)Tools
Q04977 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: F74B65F8672FAEC1

FASTA57866,924
        10         20         30         40         50         60 
MIELAAIHHQ PFNSDAYSYN GRTLHIKIRT KKDDAEHVAW FGAILTNTPA HMESERAYVA 

        70         80         90        100        110        120 
KIGRNKQPMI TGLPKCGLHS GSAIRIYLTA LMIETLFTEA MVHVRFRYRQ THVLNFRLFM 

       130        140        150        160        170        180 
RQTRLMHRLG QINRLVSNFS GAFRAGGKIC SGKPLPWGRK DPEAHDFFGG HLQGIMTSWT 

       190        200        210        220        230        240 
IWKTWGEAGI YLTPIFAAPS NHKYDTLDYC SIDPHFGDEE LFRTVVSRIH ERGMKIMLDA 

       250        260        270        280        290        300 
VFNHIGTSQE WQDVVKNGET SRYKDWFIFI LSLLKKAAMI HLRLVPRCRS SIAGTRKFRL 

       310        320        330        340        350        360 
ICLILRCTGS ANLISTAGVW MWQMKLIMRF GRNSGKPSPE KPDIFILGEI WHQADPWLRG 

       370        380        390        400        410        420 
DEFHIGHELP VHRTDDSLFF RRIDFSSQIA SRINSQKMSG MKQVKEVMLN LLDSHERILT 

       430        440        450        460        470        480 
RCGGDQRKGA RLFWHSCLLR QGRIYYPRKS GFTAAMIHCA GSAWFGKRKN RIKRCLAFMK 

       490        500        510        520        530        540 
PLIALRKQEN DVLTYGALEW KLVDDQNDFV SFSRTHEGKE LIYFFHQGRE VRRVRLRDLK 

       550        560        570 
IASDKRIYDA WTEEALHDDD VVDIQPGDFS FLGRSKFC 

« Hide

References

[1]"Catalytic properties of the cloned amylase from Bacillus licheniformis."
Kim I.C., Cha J.H., Kim J.R., Jang S.Y., Seo B.C., Cheong T.K., Lee D.S., Choi Y.D., Park K.H.
J. Biol. Chem. 267:22108-22114(1992) [PubMed: 1385394] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 27811 / CCRC 10494 / FERM P-1038.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X67133 Genomic DNA. Translation: CAA47612.1.
PIRA44326.
S25010.

3D structure databases

ProteinModelPortalQ04977.
ModBaseSearch...

Protein family/group databases

CAZyGH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR015902. Alpha_amylase.
IPR006047. Glyco_hydro_13_cat_dom.
IPR004185. Glyco_hydro_13_lg-like_dom.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 2 hits.
G3DSA:2.60.40.10. Ig-like_fold. 1 hit.
PANTHERPTHR10357. Alpha_amylase. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
PF02903. Alpha-amylase_N. 1 hit.
[Graphical view]
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
SSF81296. Ig_E-set. 1 hit.
ProtoNetSearch...

Entry information

Entry nameAMYM_BACLI
AccessionPrimary (citable) accession number: Q04977
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: May 31, 2011
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families