Beta-amylase precursor - Bacillus cereus

Preferred order of sections

Names and origin

Protein names	Recommended name: Beta-amylase RuleBase RU000509 EC=3.2.1.2 RuleBase RU000509
Organism	Bacillus cereus EMBL BAA34650.1
Taxonomic identifier	1396 [NCBI]
Taxonomic lineage	Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	546 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. RuleBase RU000509
Sequence similarities	Belongs to the glycosyl hydrolase 14 family. RuleBase RU004157

Ontologies

Keywords
Biological process	Carbohydrate metabolism Polysaccharide degradation RuleBase RU000509
Domain	Signal EMBL BAA34650.1
Ligand	Calcium PDB 5BCA Metal-binding PDB 5BCA
Molecular function	Glycosidase RuleBase RU000509 EMBL BAA34650.1 Hydrolase
Technical term	3D-structure PDB 1CQY PDB 5BCA
Gene Ontology (GO)
Biological process	polysaccharide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	beta-amylase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 30

30

Potential EMBL BAA34650.1

Chain

31 – 546

516

beta-amylase EMBL BAA34650.1

PRO_5000049300

Sites

Metal binding

86

1

Calcium PDB 5BCA

Metal binding

90

1

Calcium PDB 5BCA

Metal binding

91

1

Calcium PDB 5BCA

Metal binding

171

1

Calcium PDB 5BCA

Metal binding

174

1

Calcium PDB 5BCA

Sequences

Sequence

Length

Mass (Da)

Tools

Q9Z4N9 [UniParc].

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

546

61,629

        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

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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: 8987540] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[3]	Oyama T. Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE.
[4]	"Crystal structure of beta-amylase from Bacillus cereus var. mycoides at 2.2 A resolution." Oyama T., Kusunoki M., Kishimoto Y., Takasaki Y., Nitta Y. J. Biochem. 125:1120-1130(1999) [PubMed: 10348915] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 31-546 IN COMPLEX WITH CALCIUM.
[5]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB020313 Genomic DNA. Translation: BAA34650.1.

PIR

A48961.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CQY	X-ray	1.95	A	448-546	[»]
5BCA	X-ray	2.20	A/B/C/D	31-546	[»]

ProteinModelPortal

Q9Z4N9.

SMR

Q9Z4N9. Positions 31-546.

ModBase

Search...

Protein family/group databases

CAZy

CBM20. Carbohydrate-Binding Module Family 20.
GH14. Glycoside Hydrolase Family 14.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR002044. CBM_fam20.
IPR001554. Glyco_hydro_14.
IPR018238. Glyco_hydro_14_CS.
IPR000125. Glyco_hydro_14A_bac.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
[Graphical view]

Gene3D

G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
G3DSA:2.60.40.10. Ig-like_fold. 1 hit.

Pfam

PF00686. CBM_20. 1 hit.
PF01373. Glyco_hydro_14. 1 hit.
[Graphical view]

PRINTS

PR00750. BETAAMYLASE.
PR00841. GLHYDLASE14A.

SMART

SM01065. CBM_2. 1 hit.
[Graphical view]

SUPFAM

SSF51445. Glyco_hydro_cat. 1 hit.

PROSITE

PS00506. BETA_AMYLASE_1. 1 hit.
PS00679. BETA_AMYLASE_2. 1 hit.
PS51166. CBM20. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

Q9Z4N9_BACCE

Accession

Primary (citable) accession number: Q9Z4N9

Entry history

Integrated into UniProtKB/TrEMBL:	May 1, 1999
Last sequence update:	May 1, 1999
Last modified:	January 25, 2012
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)