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Q9Z4N9 (Q9Z4N9_BACCE) Unreviewed, UniProtKB/TrEMBL

Last modified October 16, 2013. Version 77. Feed History...

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

Names and origin

Protein namesRecommended name:
Beta-amylase RuleBase RU000509

EC=3.2.1.2 RuleBase RU000509
OrganismBacillus cereus EMBL BAA34650.1
Taxonomic identifier1396 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length546 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Sequence similarities

Belongs to the glycosyl hydrolase 14 family. RuleBase RU004157

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Potential EMBL BAA34650.1
Chain31 – 546516beta-amylase EMBL BAA34650.1
PRO_5000049300

Sites

Metal binding861Calcium
Metal binding901Calcium
Metal binding911Calcium
Metal binding1711Calcium
Metal binding1741Calcium

Sequences

Sequence LengthMass (Da)Tools
Q9Z4N9 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: A8F7CFC96ED6979B

FASTA54661,629
        10         20         30         40         50         60 
MKNQFQYCCI VILSVVMLFV SLLIPQASSA AVNGKGMNPD YKAYLMAPLK KIPEVTNWET 

        70         80         90        100        110        120 
FENDLRWAKQ NGFYAITVDF WWGDMEKNGD QQFDFSYAQR FAQSVKNAGM KMIPIISTHQ 

       130        140        150        160        170        180 
CGGNVGDDCN VPIPSWVWNQ KSDDSLYFKS ETGTVNKETL NPLASDVIRK EYGELYTAFA 

       190        200        210        220        230        240 
AAMKPYKDVI AKIYLSGGPA GELRYPSYTT SDGTGYPSRG KFQAYTEFAK SKFRLWVLNK 

       250        260        270        280        290        300 
YGSLNEVNKA WGTKLISELA ILPPSDGEQF LMNGYLSMYG KDYLEWYQGI LENHTKLIGE 

       310        320        330        340        350        360 
LAHNAFDTTF QVPIGAKIAG VHWQYNNPTI PHGAEKPAGY NDYSHLLDAF KSAKLDVTFT 

       370        380        390        400        410        420 
CLEMTDKGSY PEYSMPKTLV QNIATLANEK GIVLNGENAL SIGNEEEYKR VAEMAFNYNF 

       430        440        450        460        470        480 
AGFTLLRYQD VMYNNSLMGK FKDLLGVTPV MQTIVVKNVP TTIGDTVYIT GNRAELGSWD 

       490        500        510        520        530        540 
TKQYPIQLYY DSHSNDWRGN VVLPAERNIE FKAFIKSKDG TVKSWQTIQQ SWNPVPLKTT 


SHTSSW 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB020313 Genomic DNA. Translation: BAA34650.1.
PIRA48961.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CQYX-ray1.95A448-546[»]
ProteinModelPortalQ9Z4N9.
SMRQ9Z4N9. Positions 31-546.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM20. Carbohydrate-Binding Module Family 20.
GH14. Glycoside Hydrolase Family 14.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.60.40.10. 1 hit.
3.20.20.80. 1 hit.
InterProIPR002044. 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]
PfamPF00686. CBM_20. 1 hit.
PF01373. Glyco_hydro_14. 1 hit.
[Graphical view]
PRINTSPR00750. BETAAMYLASE.
PR00841. GLHYDLASE14A.
SMARTSM01065. CBM_2. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
PROSITEPS00506. BETA_AMYLASE_1. 1 hit.
PS00679. BETA_AMYLASE_2. 1 hit.
PS51166. CBM20. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9Z4N9.

Entry information

Entry nameQ9Z4N9_BACCE
AccessionPrimary (citable) accession number: Q9Z4N9
Entry history
Integrated into UniProtKB/TrEMBL: May 1, 1999
Last sequence update: May 1, 1999
Last modified: October 16, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)