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Protein

Beta-amylase

Gene

spoII

Organism
Bacillus cereus
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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.UniRule annotation

GO - Molecular functioni

  1. beta-amylase activity Source: UniProtKB-EC
  2. starch binding Source: InterPro

GO - Biological processi

  1. polysaccharide catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

GlycosidaseUniRule annotationImported, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradationUniRule annotation

Protein family/group databases

CAZyiCBM20. Carbohydrate-Binding Module Family 20.
GH14. Glycoside Hydrolase Family 14.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-amylaseUniRule annotation (EC:3.2.1.2UniRule annotation)
Gene namesi
Name:spoIIImported
ORF Names:BG07_5271Imported
OrganismiBacillus cereusImported
Taxonomic identifieri1396 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3030 PotentialImportedAdd
BLAST
Chaini31 – 546516beta-amylaseImportedPRO_5000049300Add
BLAST

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CQYX-ray1.95A448-546[»]
ProteinModelPortaliQ9Z4N9.
SMRiQ9Z4N9. Positions 31-546.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Z4N9.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 14 family.UniRule annotation

Keywords - Domaini

SignalImported

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR002044. CBM_fam20.
IPR001554. Glyco_hydro_14.
IPR018238. Glyco_hydro_14_CS.
IPR000125. Glyco_hydro_14A_bac.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
[Graphical view]
PfamiPF00686. CBM_20. 1 hit.
PF01373. Glyco_hydro_14. 1 hit.
[Graphical view]
PRINTSiPR00750. BETAAMYLASE.
PR00841. GLHYDLASE14A.
SMARTiSM01065. CBM_2. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00506. BETA_AMYLASE_1. 1 hit.
PS00679. BETA_AMYLASE_2. 1 hit.
PS51166. CBM20. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9Z4N9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKNQFQYCCI VILSVVMLFV SLLIPQASSA AVNGKGMNPD YKAYLMAPLK
60 70 80 90 100
KIPEVTNWET FENDLRWAKQ NGFYAITVDF WWGDMEKNGD QQFDFSYAQR
110 120 130 140 150
FAQSVKNAGM KMIPIISTHQ CGGNVGDDCN VPIPSWVWNQ KSDDSLYFKS
160 170 180 190 200
ETGTVNKETL NPLASDVIRK EYGELYTAFA AAMKPYKDVI AKIYLSGGPA
210 220 230 240 250
GELRYPSYTT SDGTGYPSRG KFQAYTEFAK SKFRLWVLNK YGSLNEVNKA
260 270 280 290 300
WGTKLISELA ILPPSDGEQF LMNGYLSMYG KDYLEWYQGI LENHTKLIGE
310 320 330 340 350
LAHNAFDTTF QVPIGAKIAG VHWQYNNPTI PHGAEKPAGY NDYSHLLDAF
360 370 380 390 400
KSAKLDVTFT CLEMTDKGSY PEYSMPKTLV QNIATLANEK GIVLNGENAL
410 420 430 440 450
SIGNEEEYKR VAEMAFNYNF AGFTLLRYQD VMYNNSLMGK FKDLLGVTPV
460 470 480 490 500
MQTIVVKNVP TTIGDTVYIT GNRAELGSWD TKQYPIQLYY DSHSNDWRGN
510 520 530 540
VVLPAERNIE FKAFIKSKDG TVKSWQTIQQ SWNPVPLKTT SHTSSW
Length:546
Mass (Da):61,629
Last modified:May 1, 1999 - v1
Checksum:iA8F7CFC96ED6979B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP009651 Genomic DNA. Translation: AJI18153.1.
AB020313 Genomic DNA. Translation: BAA34650.1.
PIRiA48961.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP009651 Genomic DNA. Translation: AJI18153.1.
AB020313 Genomic DNA. Translation: BAA34650.1.
PIRiA48961.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CQYX-ray1.95A448-546[»]
ProteinModelPortaliQ9Z4N9.
SMRiQ9Z4N9. Positions 31-546.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM20. Carbohydrate-Binding Module Family 20.
GH14. Glycoside Hydrolase Family 14.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Z4N9.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR002044. CBM_fam20.
IPR001554. Glyco_hydro_14.
IPR018238. Glyco_hydro_14_CS.
IPR000125. Glyco_hydro_14A_bac.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
[Graphical view]
PfamiPF00686. CBM_20. 1 hit.
PF01373. Glyco_hydro_14. 1 hit.
[Graphical view]
PRINTSiPR00750. BETAAMYLASE.
PR00841. GLHYDLASE14A.
SMARTiSM01065. CBM_2. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00506. BETA_AMYLASE_1. 1 hit.
PS00679. BETA_AMYLASE_2. 1 hit.
PS51166. CBM20. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Kinetic study of active site structure of beta-amylase from Bacillus cereus var. mycoides."
    Nitta Y., Shirakawa M., Takasaki Y.
    Biosci. Biotechnol. Biochem. 60:823-827(1996)
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "Cloning, sequencing, and expression of a beta-amylase gene from Bacillus cereus var. mycoides and characterization of its products."
    Yamaguchi T., Matsumoto Y., Shirakawa M., Kibe M., Hibino T., Kozaki S., Takasaki Y., Nitta Y.
    Biosci. Biotechnol. Biochem. 60:1255-1259(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  3. Oyama T.
    Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  4. "Structure of Separated Starch-Binding Domain of Bacillus cereus B-amylase."
    Yoon H.J., Hirata A., Adachi M., Sekine A., Utsumi S., Mikami B.
    Submitted (AUG-1999) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 448-546.
  5. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: Al HakamImported.

Entry informationi

Entry nameiQ9Z4N9_BACCE
AccessioniPrimary (citable) accession number: Q9Z4N9
Entry historyi
Integrated into UniProtKB/TrEMBL: May 1, 1999
Last sequence update: May 1, 1999
Last modified: April 1, 2015
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

External Data

Dasty 3

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 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.