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Reviewed, UniProtKB/Swiss-Prot Q60053 (NEPU1_THEVU)

Last modified June 16, 2009. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Neopullulanase 1
    EC=3.2.1.135
Alternative name(s):
    Alpha-amylase I
    TVA I
Gene names
Name: tvaI
OrganismThermoactinomyces vulgaris
Taxonomic identifier2026 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Thermoactinomycetaceae › Thermoactinomyces

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Protein attributes

Sequence length666 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Endohydrolysis of 1,4-alpha-glucosidic linkages in pullulan to form panose. Also hydrolyzes cyclodextrins.

Catalytic activity

Hydrolysis of pullulan to panose (6-alpha-D-glucosylmaltose).

Cofactor

Binds 3 calcium ions per subunit.

Subcellular location

Secreted.

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

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Ontologies

Keywords
   Biological processCarbohydrate metabolism
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Chloride
Metal-binding
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncalcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

chloride ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

neopullulanase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929
Chain30 – 666637Neopullulanase 1
PRO_0000001445

Sites

Active site3851Nucleophile
Active site4251Proton donor
Active site5011
Metal binding311Calcium 1; via carbonyl oxygen
Metal binding331Calcium 1
Metal binding351Calcium 1; via carbonyl oxygen
Metal binding711Calcium 1
Metal binding1251Calcium 1
Metal binding1741Calcium 2
Metal binding1761Calcium 2; via carbonyl oxygen
Metal binding1791Calcium 2
Metal binding1801Calcium 2
Metal binding2161Calcium 2; via carbonyl oxygen
Metal binding2181Calcium 2
Metal binding3051Calcium 3
Metal binding3091Calcium 3
Metal binding3101Calcium 3; via carbonyl oxygen
Metal binding3121Calcium 3; via carbonyl oxygen
Metal binding3171Calcium 3

Secondary structure

1 ............................................................................................................................... 666
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q60053-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: E99B15AA392AB6CB

FASTA66674,296
        10         20         30         40         50         60 
MIKLLKPMSL SILLVFILSF SFPFPTAKAA ANDNNVEWNG LFHDQGPLFD NAPEPTSTQS 

        70         80         90        100        110        120 
VTLKLRTFKG DITSANIKYW DTADNAFHWV PMVWDSNDPT GTFDYWKGTI PASPSIKYYR 

       130        140        150        160        170        180 
FQINDGTSTA WYNGNGPSST EPNADDFYII PNFKTPDWLK NGVMYQIFPD RFYNGDSSND 

       190        200        210        220        230        240 
VQTGSYTYNG TPTEKKAWGS SVYADPGYDN SLVFFGGDLA GIDQKLGYIK KTLGANILYL 

       250        260        270        280        290        300 
NPIFKAPTNH KYDTQDYMAV DPAFGDNSTL QTLINDIHST ANGPKGYLIL DGVFNHTGDS 

       310        320        330        340        350        360 
HPWFDKYNNF SSQGAYESQS SPWYNYYTFY TWPDSYASFL GFNSLPKLNY GNSGSAVRGV 

       370        380        390        400        410        420 
IYNNSNSVAK TYLNPPYSVD GWRLDAAQYV DANGNNGSDV TNHQIWSEFR NAVKGVNSNA 

       430        440        450        460        470        480 
AIIGEYWGNA NPWTAQGNQW DAATNFDGFT QPVSEWITGK DYQNNSASIS TTQFDSWLRG 

       490        500        510        520        530        540 
TRANYPTNVQ QSMMNFLSNH DITRFATRSG GDLWKTYLAL IFQMTYVGTP TIYYGDEYGM 

       550        560        570        580        590        600 
QGGADPDNRR SFDWSQATPS NSAVALTQKL ITIRNQYPAL RTGSFMTLIT DDTNKIYSYG 

       610        620        630        640        650        660 
RFDNVNRIAV VLNNDSVSHT VNVPVWQLSM PNGSTVTDKI TGHSYTVQNG MVTVAVDGHY 


GAVLAQ

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References

[1]"Comparison of primary structures and substrate specificities of two pullulan-hydrolyzing alpha-amylases, TVA I and TVA II, from Thermoactinomyces vulgaris R-47."
Tonozuka T., Mogi S., Shimura Y., Ibuka A., Sakai H., Matsuzawa H., Sakano Y., Ohta T.
Biochim. Biophys. Acta 1252:35-42(1995) [PubMed: 7548164] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
Strain: R-47.
[2]"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: 12051850] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
Strain: R-47.
+Additional computationally mapped references.

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Cross-references

Sequence databases

D13177 Genomic DNA. Translation: BAA02471.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1IZJX-ray2.20A30-666[»]
1IZKX-ray2.20A30-666[»]
1JI1X-ray1.60A/B30-666[»]
1UH2X-ray2.00A30-666[»]
1UH3X-ray2.60A30-666[»]
1UH4X-ray1.80A30-666[»]
2D0FX-ray2.08A30-666[»]
2D0GX-ray2.60A30-666[»]
2D0HX-ray2.10A30-666[»]
ModBaseSearch...

Protein family/group databases

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

Enzyme and pathway databases

BRENDA3.2.1.135. 18584.

Family and domain databases

InterProIPR013780. 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]
Gene3DG3DSA: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.
PfamPF00128. Alpha-amylase. 1 hit.
PF02903. Alpha-amylase_N. 1 hit.
[Graphical view]
SMARTSM00642. Aamy. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameNEPU1_THEVU
AccessionPrimary (citable) accession number: Q60053
Entry history
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: November 1, 1996
Last modified: June 16, 2009
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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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