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P21543 (AMYB_PAEPO) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 112. 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:
Beta/alpha-amylase

Including the following 2 domains:

  1. Beta-amylase
    EC=3.2.1.2
  2. Alpha-amylase
    EC=3.2.1.1
OrganismPaenibacillus polymyxa (Bacillus polymyxa)
Taxonomic identifier1406 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesPaenibacillaceaePaenibacillus

Protein attributes

Sequence length1196 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The precursor protein is proteolytically cleaved to produce multiform beta-amylases and a 48 kDa alpha-amylase after secretion.

Catalytic activity

Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains.

Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.

Subcellular location

Secreted.

Sequence similarities

In the N-terminal section; belongs to the glycosyl hydrolase 14 family.

In the C-terminal section; belongs to the glycosyl hydrolase 13 family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3535
Chain36 – 11961161Beta/alpha-amylase
PRO_0000001457

Regions

Repeat455 – 558104
Repeat565 – 668104
Region36 – 454419Beta-amylase
Region395 – 3962Substrate binding By similarity
Region669 – 1196528Alpha-amylase

Sites

Active site1981Proton donor By similarity
Active site3941Proton acceptor By similarity
Binding site761Substrate By similarity
Binding site1161Substrate By similarity
Binding site1241Substrate By similarity
Binding site3141Substrate By similarity
Binding site3191Substrate By similarity
Binding site3571Substrate By similarity
Binding site4231Substrate By similarity

Amino acid modifications

Disulfide bond118 ↔ 126 Ref.4

Experimental info

Mutagenesis1181C → S: 5-fold decrease in activity. Ref.4
Mutagenesis1261C → V: 20-fold decrease in activity. Ref.4
Mutagenesis3581C → S: 60-fold decrease in activity. Ref.4
Sequence conflict11M → MIGL in CAA68344. Ref.3
Sequence conflict671N → S in CAA68344. Ref.3
Sequence conflict1001N → D in CAA68344. Ref.3
Sequence conflict1541S → N in CAA68344. Ref.3
Sequence conflict1771E → Q in CAA68344. Ref.3
Sequence conflict227 – 2282NA → KS in CAA68344. Ref.3
Sequence conflict3301G → S in CAA68344. Ref.3
Sequence conflict4251N → S in CAA68344. Ref.3
Sequence conflict4931D → A in CAA68344. Ref.3
Sequence conflict5321S → L in CAA68344. Ref.3
Sequence conflict5591A → T in CAA68344. Ref.3
Sequence conflict6651A → T in CAA68344. Ref.3
Sequence conflict6811D → N in CAA68344. Ref.3
Sequence conflict6861T → A in CAA68344. Ref.3
Sequence conflict725 – 7284AFTS → VFSP in CAA68344. Ref.3
Sequence conflict7361N → K in CAA68344. Ref.3
Sequence conflict7411N → S in CAA68344. Ref.3
Sequence conflict7581S → N in CAA68344. Ref.3

Secondary structure

..................................................................................................................... 1196
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P21543 [UniParc].

Last modified May 1, 1991. Version 1.
Checksum: A41EA6B70F257064

FASTA1,196130,893
        10         20         30         40         50         60 
MTLYRSLWKK GCMLLLSLVL SLTAFIGSPS NTASAAVADD FQASVMGPLA KINDWGSFKK 

        70         80         90        100        110        120 
QLQTLKNNGV YAITTDVWWG YVESAGDNQF DWSYYKTYAN AVKEAGLKWV PIISTHKCGG 

       130        140        150        160        170        180 
NVGDDCNIPL PSWLSSKGSA DEMQFKDESG YANSEALSPL WSGTGKQYDE LYASFAENFA 

       190        200        210        220        230        240 
GYKSIIPKIY LSGGPSGELR YPSYYPAAGW SYPGRGKFQA YTETAKNAFR TAMNDKYGSL 

       250        260        270        280        290        300 
DKINAAWGTK LTSLSQINPP TDGDGFYTNG GYNSAYGKDF LSWYQSVLEK HLGVIGAAAH 

       310        320        330        340        350        360 
KNFDSVFGVR IGAKISGLHW QMNNPAMPHG TEQAGGYYDY NRLIQKFKDA DLDLTFTCLE 

       370        380        390        400        410        420 
MSDSGTAPNY SLPSTLVDTV SSIANAKGVR LNGENALPTG GSGFQKIEEK ITKFGYHGFT 

       430        440        450        460        470        480 
LLRINNLVNN DGSPTGELSG FKQYIISKAK PDNNGGTGNK VTIYYKKGFN SPYIHYRPAG 

       490        500        510        520        530        540 
GSWTAAPGVK MQDAEISGYA KITVDIGSAS QLEAAFNDGN NNWDSNNTKN YSFSTGTSTY 

       550        560        570        580        590        600 
TPGNSGNAGT ITSGAPAGAN PGDGGGTTNK VTVYYKKGFN SPYIHYRPAG GSWTAAPGVK 

       610        620        630        640        650        660 
MQDAEISGYA KITVDIGSAS QLEAAFNDGN NNWDSNNTKN YLFSTGTSTY TPGSNGAAGT 

       670        680        690        700        710        720 
IRTGAPSGSV LSVVTSTYAT DLNEVTGPIQ TEKLSGVSLN VSTSTYAPNS NGVEVTAQTE 

       730        740        750        760        770        780 
APSGAFTSMD LGTLSNPTSL NTDWSKQSIY FIMTDRFSNG DPSNDNYGGF NSNNSDQRKW 

       790        800        810        820        830        840 
HGGDFQGIIN KLDYIKNMGF TAIWITPVTM QKSEYAYHGY HTYDFYAVDG HLGTMDKLQE 

       850        860        870        880        890        900 
LVRKAHDKNI AVMVDVVVNH TGDFQPGNGF AKAPFDKADW YHHNGDITDG DYNSNNQWKI 

       910        920        930        940        950        960 
ENGDVAGLDD LNHENPATAN ELKNWIKWLL NETGIDGLRL DTVKHVPKGF LKDFDQAANT 

       970        980        990       1000       1010       1020 
FTMGEIFHGD PAYVGDYTRY LDAALDFPMY YTIKDVFGHD QSMRKIKDRY SDDRYYRDAQ 

      1030       1040       1050       1060       1070       1080 
TNGVFIDNHD VKRFLNDASG KPGANYDKWP QLKAALGFTL TSRGIPIIYQ GTEQGYSGGD 

      1090       1100       1110       1120       1130       1140 
DPANRENMNF NANHDLYQYI AKLNYVRNNH PALQNGSQRE KWVDDSFYSF QRSKNGDEAI 

      1150       1160       1170       1180       1190 
VFINNSWNSQ TRTIGNFDNL SNGTRLTNQL SNDSVQINNG SITVTLAPKE VKVFTK 

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References

[1]"Cloning and nucleotide sequence of the gene coding for enzymatically active fragments of the Bacillus polymyxa beta-amylase."
Kawazu T., Nakanishi Y., Uozumi N., Sasaki T., Yamagata H., Tsukagoshi N., Udaka S.
J. Bacteriol. 169:1564-1570(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-936, PARTIAL PROTEIN SEQUENCE.
Strain: 72.
[2]"A single gene directs synthesis of a precursor protein with beta- and alpha-amylase activities in Bacillus polymyxa."
Uozumi N., Sakurai K., Sasaki T., Takekawa S., Yamagata H., Tsukagoshi N., Udaka S.
J. Bacteriol. 171:375-382(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 689-1196, PARTIAL PROTEIN SEQUENCE.
Strain: 72.
[3]"Sequence of an active fragment of B. polymyxa beta amylase."
Rhodes C., Strasser J., Friedberg F.
Nucleic Acids Res. 15:3934-3934(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-776.
Strain: ATCC 8523 / CCM 1465 / DSM 356 / VKM B-418.
[4]"Structural and functional roles of cysteine residues of Bacillus polymyxa beta-amylase."
Uozumi N., Matsuda T., Tsukagoshi N., Udaka S.
Biochemistry 30:4594-4599(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BOND, MUTAGENESIS OF CYSTEINE RESIDUES.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M15817 Genomic DNA. Translation: AAA85446.1.
Y00150 Other DNA. Translation: CAA68344.1.
PIRA29130.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2LAANMR-A455-558[»]
2LABNMR-A565-668[»]
3VOCX-ray1.95A36-454[»]
ProteinModelPortalP21543.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM25. Carbohydrate-Binding Module Family 25.
GH13. Glycoside Hydrolase Family 13.
GH14. Glycoside Hydrolase Family 14.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.60.40.1180. 1 hit.
3.20.20.80. 2 hits.
InterProIPR006048. A-amylase_b_C.
IPR005085. CBM_fam25.
IPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR001554. Glyco_hydro_14.
IPR018238. Glyco_hydro_14_CS.
IPR000125. Glyco_hydro_14A_bac.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERPTHR10357. PTHR10357. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
PF03423. CBM_25. 2 hits.
PF01373. Glyco_hydro_14. 1 hit.
[Graphical view]
PRINTSPR00750. BETAAMYLASE.
PR00841. GLHYDLASE14A.
SMARTSM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
SM01066. CBM_25. 2 hits.
[Graphical view]
SUPFAMSSF51445. SSF51445. 2 hits.
PROSITEPS00506. BETA_AMYLASE_1. 1 hit.
PS00679. BETA_AMYLASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAMYB_PAEPO
AccessionPrimary (citable) accession number: P21543
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: October 16, 2013
This is version 112 of the entry and version 1 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