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Q08751 (NEPU2_THEVU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Neopullulanase 2
EC=3.2.1.135
Alternative name(s):
Alpha-amylase II
TVA II
Gene names
Name:tvaII
OrganismThermoactinomyces vulgaris
Taxonomic identifier2026 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Thermoactinomycetaceae › Thermoactinomyces

Protein attributes

Sequence length585 AA.
Sequence statusComplete.
Protein existenceEvidence 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

Monomer.

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   LigandCalcium
Metal-binding
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

neopullulanase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 585585Neopullulanase 2
PRO_0000054311

Sites

Active site3251Nucleophile
Active site3541Proton donor
Metal binding1431Calcium
Metal binding1451Calcium; via carbonyl oxygen
Metal binding1481Calcium
Metal binding1491Calcium
Metal binding1691Calcium; via carbonyl oxygen
Metal binding1711Calcium
Site4211Transition state stabilizer By similarity

Secondary structure

1 ..................................................................................................................................... 585
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q08751 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: E311813A05A7791A

FASTA58567,467
        10         20         30         40         50         60 
MLLEAIFHEA KGSYAYPISE TQLRVRLRAK KGDVVRCEVL YADRYASPEE ELAHALAGKA 

        70         80         90        100        110        120 
GSDERFDYFE ALLECSTKRV KYVFLLTGPQ GEAVYFGETG FSAERSKAGV FQYAYIHRSE 

       130        140        150        160        170        180 
VFTTPEWAKE AVIYQIFPER FANGDPSNDP PGTEQWAKDA RPRHDSFYGG DLKGVIDRLP 

       190        200        210        220        230        240 
YLEELGVTAL YFTPIFASPS HHKYDTADYL AIDPQFGDLP TFRRLVDEAH RRGIKIILDA 

       250        260        270        280        290        300 
VFNHAGDQFF AFRDVLQKGE QSRYKDWFFI EDFPVSKTSR TNYETFAVQV PAMPKLRTEN 

       310        320        330        340        350        360 
PEVKEYLFDV ARFWMEQGID GWRLDVANEV DHAFWREFRR LVKSLNPDAL IVGEIWHDAS 

       370        380        390        400        410        420 
GWLMGDQFDS VMNYLFRESV IRFFATGEIH AERFDAELTR ARMLYPEQAA QGLWNLLDSH 

       430        440        450        460        470        480 
DTERFLTSCG GNEAKFRLAV LFQMTYLGTP LIYYGDEIGM AGATDPDCRR PMIWEEKEQN 

       490        500        510        520        530        540 
RGLFEFYKEL IRLRHRLASL TRGNVRSWHA DKQANLYAFV RTVQDQHVGV VLNNRGEKQT 

       550        560        570        580 
VLLQVPESGG KTWLDCLTGE EVHGKQGQLK LTLRPYQGMI LWNGR

« Hide

References

[1]"A neopullulanase-type alpha-amylase gene from Thermoactinomyces vulgaris R-47."
Tonozuka T., Ohtsuka M., Mogi S., Sakai H., Ohta T., Sakano Y.
Biosci. Biotechnol. Biochem. 57:395-401(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
Strain: R-47.
[2]"Crystal structure of Thermoactinomyces vulgaris R-47 alpha-amylase II (TVAII) hydrolyzing cyclodextrins and pullulan at 2.6-A resolution."
Kamitori S., Kondo S., Okuyama K., Yokota T., Shimura Y., Tonozuka T., Sakano Y.
J. Mol. Biol. 287:907-921(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
Strain: R-47.
[3]"Crystal structures and structural comparison of Thermoactinomyces vulgaris R-47 alpha-amylase 1 (TVAI) at 1.6 A resolution and alpha-amylase 2 (TVAII) at 2.3 A resolution."
Kamitori S., Abe A., Ohtaki A., Kaji A., Tonozuka T., Sakano Y.
J. Mol. Biol. 318:443-453(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D13178 Genomic DNA. Translation: BAA02473.1.
PIRJC1486.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BVZX-ray2.60A/B1-585[»]
1G1YX-ray3.00A/B1-585[»]
1JF5X-ray3.20A/B1-585[»]
1JF6X-ray3.20A/B1-585[»]
1JI2X-ray2.30A/B1-585[»]
1JIBX-ray3.30A/B1-585[»]
1JL8X-ray3.20A/B1-585[»]
1VB9X-ray2.20A/B1-585[»]
1VFMX-ray2.90A/B1-585[»]
1VFOX-ray2.81A/B1-585[»]
1VFUX-ray3.10A/B1-585[»]
1WZKX-ray2.30A/B1-585[»]
1WZLX-ray2.00A/B1-585[»]
1WZMX-ray3.20A/B1-585[»]
2D2OX-ray2.10A/B1-585[»]
3A6OX-ray2.80A/B1-585[»]
ProteinModelPortalQ08751.
SMRQ08751. Positions 1-585.
ModBaseSearch...

Protein family/group databases

CAZyCBM34. Carbohydrate-Binding Module Family 34.
GH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.60.40.10. 1 hit.
2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProIPR006048. A-amylase_b_C.
IPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR004185. Glyco_hydro_13_lg-like_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view]
PANTHERPTHR10357. PTHR10357. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
PF02903. Alpha-amylase_N. 1 hit.
[Graphical view]
SMARTSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
SSF81296. Ig_E-set. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ08751.

Entry information

Entry nameNEPU2_THEVU
AccessionPrimary (citable) accession number: Q08751
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 3, 2013
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

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

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