Amylase - Bacillus sp.

Preferred order of sections

Names and origin

Protein names	Submitted name: Amylase EMBL BAA32431.1
Organism	Bacillus sp. EMBL BAA32431.1
Taxonomic identifier	1409 [NCBI]
Taxonomic lineage	Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	516 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Ontologies

Keywords
Ligand	Calcium PDB 1W9X PDB 2DIE Metal-binding PDB 1W9X PDB 2DIE
Technical term	3D-structure PDB 1W9X PDB 2DIE
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	calcium ion binding Inferred from electronic annotation. Source: InterPro hydrolase activity, hydrolyzing O-glycosyl compounds Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Sites

Metal binding

137

1

Calcium 1 PDB 1W9X PDB 2DIE

Metal binding

194

1

Calcium 2 PDB 1W9X PDB 2DIE

Metal binding

217

1

Calcium 2; via carbonyl oxygen PDB 1W9X PDB 2DIE

Metal binding

219

1

Calcium 2 PDB 1W9X PDB 2DIE

Metal binding

230

1

Calcium 1 PDB 1W9X PDB 2DIE

Metal binding

236

1

Calcium 1 PDB 1W9X PDB 2DIE

Metal binding

238

1

Calcium 2 PDB 1W9X PDB 2DIE

Metal binding

240

1

Calcium 2 PDB 1W9X

Metal binding

271

1

Calcium 1; via carbonyl oxygen PDB 1W9X PDB 2DIE

Metal binding

336

1

Calcium 3; via carbonyl oxygen PDB 1W9X PDB 2DIE

Metal binding

338

1

Calcium 3; via carbonyl oxygen PDB 2DIE

Metal binding

439

1

Calcium 3; via carbonyl oxygen PDB 1W9X PDB 2DIE

Metal binding

440

1

Calcium 3 PDB 2DIE

Metal binding

463

1

Calcium 3 PDB 1W9X PDB 2DIE

Binding site

197

1

Glucose PDB 1W9X

Binding site

225

1

Glucose PDB 1W9X

Binding site

234

1

Glucose PDB 1W9X

Binding site

270

1

Glucose PDB 1W9X

Sequences

Sequence

Length

Mass (Da)

Tools

O82839 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: D90A8C90ECC182F8
Show »

FASTA

516

58,842

        10         20         30         40         50         60 
MKLHNRIISV LLTLLLAVAV LFPYMTEPAQ AHHNGTNGTM MQYFEWHLPN DGNHWNRLRD 

        70         80         90        100        110        120 
DAANLKSKGI TAVWIPPAWK GTSQNDVGYG AYDLYDLGEF NQKGTVRTKY GTRSQLQGAV 

       130        140        150        160        170        180 
TSLKNNGIQV YGDVVMNHKG GADGTEMVNA VEVNRSNRNQ EISGEYTIEA WTKFDFPGRG 

       190        200        210        220        230        240 
NTHSNFKWRW YHFDGTDWDQ SRQLQNKIYK FRGTGKAWDW EVDIENGNYD YLMYADIDMD 

       250        260        270        280        290        300 
HPEVINELRN WGVWYTNTLN LDGFRIDAVK HIKYSYTRDW LTHVRNTTGK PMFAVAEFWK 

       310        320        330        340        350        360 
NDLAAIENYL NKTSWNHSVF DVPLHYNLYN ASNSGGYFDM RNILNGSVVQ KHPIHAVTFV 

       370        380        390        400        410        420 
DNHDSQPGEA LESFVQSWFK PLAYALILTR EQGYPSVFYG DYYGIPTHGV PSMKSKIDPL 

       430        440        450        460        470        480 
LQARQTYAYG TQHDYFDHHD IIGWTREGDS SHPNSGLATI MSDGPGGNKW MYVGKHKAGQ 

       490        500        510 
VWRDITGNRS GTVTINADGW GNFTVNGGAV SVWVKQ

« Hide

References

[1]	"Improved thermostability of a Bacillus alpha-amylase by deletion of an arginine-glycine residue is caused by enhanced calcium binding." Igarashi K., Hatada Y., Ikawa K., Araki H., Ozawa T., Kobayashi T., Ozaki K., Ito S. Biochem. Biophys. Res. Commun. 248:372-377(1998) [PubMed: 9675143] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: KSM-1378 EMBL BAA32431.1.
[2]	"Ancestral sequence evolutionary trace and crystal structure analyses of alkaline alpha-amylase from Bacillus sp. KSM-1378 to clarify the alkaline adaptation process of proteins." Shirai T., Igarashi K., Ozawa T., Hagihara H., Kobayashi T., Ozaki K., Ito S. Proteins 66:600-610(2007) [PubMed: 17154418] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 32-516 IN COMPLEX WITH CALCIUM.
[3]	"Structure of a Bacillus halmapalus family 13 alpha-amylase, BHA, in complex with an acarbose-derived nonasaccharide at 2.1 A resolution." Davies G.J., Brzozowski A.M., Dauter Z., Rasmussen M.D., Borchert T.V., Wilson K.S. Acta Crystallogr. D Biol. Crystallogr. 61:190-193(2005) [PubMed: 15681870] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 36-515 IN COMPLEX WITH CALCIUM AND GLUCOSE.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB008763 Genomic DNA. Translation: BAA32431.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1W9X	X-ray	2.10	A	36-515	[»]
2DIE	X-ray	2.10	A	32-516	[»]

ProteinModelPortal

O82839.

SMR

O82839. Positions 36-516.

ModBase

Search...

Protein family/group databases

CAZy

GH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR013776. A-amylase_thermo.
IPR015237. Alpha-amylase_C_pro.
IPR015902. Alpha_amylase.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]

Gene3D

G3DSA:2.60.40.1180. Glyco_hydro_13_b. 1 hit.
G3DSA:3.20.20.80. Glyco_hydro_cat. 2 hits.

PANTHER

PTHR10357. Alpha_amylase. 1 hit.

Pfam

PF00128. Alpha-amylase. 1 hit.
PF09154. DUF1939. 1 hit.
[Graphical view]

PIRSF

PIRSF001021. Alph-amls_thrmst. 1 hit.

SMART

SM00642. Aamy. 1 hit.
[Graphical view]

SUPFAM

SSF51445. Glyco_hydro_cat. 1 hit.

ProtoNet

Search...

Entry information

Entry name

O82839_BACSP

Accession

Primary (citable) accession number: O82839

Entry history

Integrated into UniProtKB/TrEMBL:	November 1, 1998
Last sequence update:	November 1, 1998
Last modified:	July 27, 2011
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)