Neopullulanase - Bacillus stearothermophilus

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Reviewed, UniProtKB/Swiss-Prot P38940 (NEPU_BACST)

Last modified June 16, 2009. Version 62. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein names

Recommended name:
Neopullulanase
EC=3.2.1.135

Gene names

Name:

nplT

Organism

Bacillus stearothermophilus (Geobacillus stearothermophilus)

Taxonomic identifier

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Geobacillus

Protein attributes

Sequence length	588 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Hydrolyzes pullulan efficiently but only a small amount of starch. Endohydrolysis of 1,4-alpha-glucosidic linkages in pullulan to form panose. Cleaves also (1-6)-alpha-glucosidic linkages to form maltotriose.
Catalytic activity	Hydrolysis of pullulan to panose (6-alpha-D-glucosylmaltose).
Cofactor	Binds 1 calcium ion per subunit.
Subunit structure	Dimer.
Sequence similarities	Belongs to the glycosyl hydrolase 13 family.

Ontologies

Keywords
Ligand	Calcium Metal-binding
Molecular function	Glycosidase Hydrolase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW neopullulanase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

588

Neopullulanase

PRO_0000054310

Sites

Active site

1

Nucleophile

Active site

1

Proton donor

Active site

1

Metal binding

1

Calcium

Metal binding

1

Calcium; via carbonyl oxygen

Metal binding

1

Calcium

Metal binding

1

Calcium; via carbonyl oxygen

Metal binding

1

Calcium

Secondary structure

1

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588

Helix Strand Turn

Sequences

Sequence

Length

Mass (Da)

Tools

P38940-1 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: B2C7195D1CE34A33
Show »

588

69,145

        10         20         30         40         50         60 
MRKEAIYHRP ADNFAYAYDS ETLHLRLRTK KDDIDRVELL HGDPYDWQNG AWQFQMMPMR 

        70         80         90        100        110        120 
KTGSDELFDY WFAEVKPPYR RLRYGFVLYS GEEKLVYTEK GFYFEVPTDD TAYYFCFPFL 

       130        140        150        160        170        180 
HRVDLFEAPD WVKDTVWYQI FPERFANGNP SISPEGSRPW GSEDPTPTSF FGGDLQGIID 

       190        200        210        220        230        240 
HLDYLVDLGI TGIYLTPIFR SPSNHKYDTA DYFEVDPHFG DKETLKTLID RCHEKGIRVM 

       250        260        270        280        290        300 
LDAVFNHCGY EFAPFQDVWK NGESSKYKDW FHIHEFPLQT EPRPNYDTFR FVPQMPKLNT 

       310        320        330        340        350        360 
ANPEVKRYLL DVATYWIREF DIDGWRLDVA NEIDHEFWRE FRQEVKALKP DVYILGEIWH 

       370        380        390        400        410        420 
DAMPWLRGDQ FDAVMNYPFT DGVLRFFAKE EISARQFANQ MMHVLHSYPN NVNEAAFNLL 

       430        440        450        460        470        480 
GSHDTSRILT VCGGDIRKVK LLFLFQLTFT GSPCIYYGDE IGMTGGNDPE CRKCMVWDPM 

       490        500        510        520        530        540 
QQNKELHQHV KQLIALRKQY RSLRRGEISF LHADDEMNYL IYKKTDGDET VLVIINRSDQ 

       550        560        570        580 
KADIPIPLDA RGTWLVNLLT GERFAAEAET LCTSLPPYGF VLYAIEHW

References

[1]	"Nucleotide sequence of the neopullulanase gene from Bacillus stearothermophilus." Kuriki T., Imanaka T. J. Gen. Microbiol. 135:1521-1528(1989) [PubMed: 2482332] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-5. Strain: TRS40.
[2]	"Three-dimensional structure and substrate binding of Bacillus stearothermophilus neopullulanase." Hondoh H., Kuriki T., Matsuura Y. J. Mol. Biol. 326:177-188(2003) [PubMed: 12547200] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).

Cross-references

Sequence databases

M28138 Genomic DNA. Translation: AAA22622.1.

PIR

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1J0H	X-ray	1.90	A/B	1-588	[»]
1J0I	X-ray	2.40	A/B	1-588	[»]
1J0J	X-ray	2.80	A/B	1-588	[»]
1J0K	X-ray	3.20	A/B	1-588	[»]

ModBase

Protein family/group databases

CAZy

CBM34. Carbohydrate-Binding Module Family 34.
GH13. Glycoside Hydrolase Family 13.

Enzyme and pathway databases

BRENDA

3.2.1.135. 266715.

Family and domain databases

InterPro

IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat.
IPR004185. Glyco_hydro_13_lg-like.
IPR006589. Glyco_hydro_13_sub_cat.
IPR013781. Glyco_hydro_sg_catalytic.
IPR013783. Ig-like_fold.
[Graphical view]

Gene3D

G3DSA:2.60.40.1180. Glyco_hydro_13_b. 1 hit.
G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
G3DSA:2.60.40.10. Ig-like_fold. 1 hit.

Pfam

PF00128. Alpha-amylase. 1 hit.
PF02903. Alpha-amylase_N. 1 hit.
[Graphical view]

SMART

SM00642. Aamy. 1 hit.
[Graphical view]

ProtoNet

Entry information

Entry name

NEPU_BACST

Accession

Primary (citable) accession number: P38940

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	June 16, 2009
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents