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Protein

Neopullulanase 1

Gene

tvaI

Organism
Thermoactinomyces vulgaris
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

Hydrolysis of pullulan to panose (6-alpha-D-glucosylmaltose).1 Publication

Cofactori

Ca2+1 PublicationNote: Binds 3 Ca2+ ions per subunit.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi31 – 311Calcium 1; via carbonyl oxygenCombined sources1 Publication
Metal bindingi33 – 331Calcium 1Combined sources1 Publication
Metal bindingi35 – 351Calcium 1; via carbonyl oxygenCombined sources1 Publication
Metal bindingi71 – 711Calcium 1Combined sources1 Publication
Metal bindingi125 – 1251Calcium 1Combined sources1 Publication
Metal bindingi174 – 1741Calcium 2Combined sources1 Publication
Metal bindingi176 – 1761Calcium 2; via carbonyl oxygenCombined sources1 Publication
Metal bindingi179 – 1791Calcium 2Combined sources1 Publication
Metal bindingi180 – 1801Calcium 2Combined sources1 Publication
Metal bindingi216 – 2161Calcium 2; via carbonyl oxygenCombined sources1 Publication
Metal bindingi218 – 2181Calcium 2Combined sources1 Publication
Binding sitei296 – 2961SubstrateBy similarity
Metal bindingi305 – 3051Calcium 3Combined sources1 Publication
Metal bindingi309 – 3091Calcium 3Combined sources1 Publication
Metal bindingi310 – 3101Calcium 3; via carbonyl oxygenCombined sources1 Publication
Metal bindingi312 – 3121Calcium 3; via carbonyl oxygenCombined sources1 Publication
Metal bindingi317 – 3171Calcium 3Combined sources1 Publication
Binding sitei383 – 3831SubstrateBy similarity
Active sitei385 – 3851NucleophileBy similarity
Active sitei425 – 4251Proton donorBy similarity
Sitei501 – 5011Transition state stabilizerBy similarity
Binding sitei545 – 5451SubstrateBy similarity
Binding sitei549 – 5491SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Calcium, Chloride, Metal-binding

Protein family/group databases

CAZyiCBM34. Carbohydrate-Binding Module Family 34.
GH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
Neopullulanase 1 (EC:3.2.1.1351 Publication)
Alternative name(s):
Alpha-amylase I
TVA I
Gene namesi
Name:tvaI
OrganismiThermoactinomyces vulgaris
Taxonomic identifieri2026 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesThermoactinomycetaceaeThermoactinomyces

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929Add
BLAST
Chaini30 – 666637Neopullulanase 1PRO_0000001445Add
BLAST

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi32 – 343Combined sources
Helixi38 – 403Combined sources
Turni47 – 493Combined sources
Beta strandi61 – 688Combined sources
Beta strandi73 – 819Combined sources
Turni82 – 843Combined sources
Beta strandi85 – 917Combined sources
Beta strandi93 – 975Combined sources
Beta strandi101 – 11010Combined sources
Beta strandi117 – 1259Combined sources
Beta strandi128 – 1336Combined sources
Beta strandi136 – 1405Combined sources
Beta strandi147 – 1493Combined sources
Helixi157 – 1615Combined sources
Beta strandi164 – 1674Combined sources
Helixi169 – 1713Combined sources
Helixi177 – 1793Combined sources
Beta strandi187 – 1904Combined sources
Helixi210 – 2123Combined sources
Helixi219 – 2246Combined sources
Helixi226 – 2305Combined sources
Turni231 – 2333Combined sources
Beta strandi237 – 2415Combined sources
Beta strandi247 – 2504Combined sources
Beta strandi255 – 2606Combined sources
Turni262 – 2643Combined sources
Helixi267 – 27812Combined sources
Beta strandi280 – 2845Combined sources
Beta strandi287 – 2926Combined sources
Turni302 – 3043Combined sources
Beta strandi310 – 3123Combined sources
Turni315 – 3173Combined sources
Helixi324 – 3263Combined sources
Beta strandi329 – 3313Combined sources
Turni332 – 3343Combined sources
Beta strandi342 – 3498Combined sources
Helixi356 – 3616Combined sources
Helixi368 – 3736Combined sources
Turni375 – 3773Combined sources
Beta strandi381 – 3844Combined sources
Helixi387 – 3893Combined sources
Beta strandi397 – 3993Combined sources
Helixi400 – 41617Combined sources
Beta strandi421 – 4244Combined sources
Helixi431 – 4333Combined sources
Turni434 – 4363Combined sources
Beta strandi437 – 4393Combined sources
Beta strandi441 – 4444Combined sources
Turni446 – 4494Combined sources
Helixi450 – 4578Combined sources
Beta strandi458 – 4603Combined sources
Helixi471 – 48212Combined sources
Helixi487 – 4904Combined sources
Beta strandi494 – 4974Combined sources
Helixi505 – 5084Combined sources
Turni509 – 5113Combined sources
Helixi513 – 52311Combined sources
Beta strandi526 – 5338Combined sources
Helixi536 – 5383Combined sources
Helixi547 – 5493Combined sources
Beta strandi556 – 5583Combined sources
Helixi562 – 57615Combined sources
Helixi578 – 5825Combined sources
Beta strandi583 – 5919Combined sources
Turni592 – 5954Combined sources
Beta strandi596 – 6027Combined sources
Beta strandi607 – 6137Combined sources
Beta strandi615 – 6173Combined sources
Beta strandi619 – 6235Combined sources
Helixi625 – 6284Combined sources
Beta strandi635 – 6384Combined sources
Turni639 – 6413Combined sources
Beta strandi644 – 6463Combined sources
Beta strandi651 – 6566Combined sources
Beta strandi660 – 6667Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ60053.
SMRiQ60053. Positions 30-666.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ60053.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni500 – 5012Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR004185. Glyco_hydro_13_lg-like_dom.
IPR013780. Glyco_hydro_b.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 2 hits.
PfamiPF00128. Alpha-amylase. 1 hit.
PF02903. Alpha-amylase_N. 1 hit.
[Graphical view]
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF81296. SSF81296. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q60053-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIKLLKPMSL SILLVFILSF SFPFPTAKAA ANDNNVEWNG LFHDQGPLFD
60 70 80 90 100
NAPEPTSTQS VTLKLRTFKG DITSANIKYW DTADNAFHWV PMVWDSNDPT
110 120 130 140 150
GTFDYWKGTI PASPSIKYYR FQINDGTSTA WYNGNGPSST EPNADDFYII
160 170 180 190 200
PNFKTPDWLK NGVMYQIFPD RFYNGDSSND VQTGSYTYNG TPTEKKAWGS
210 220 230 240 250
SVYADPGYDN SLVFFGGDLA GIDQKLGYIK KTLGANILYL NPIFKAPTNH
260 270 280 290 300
KYDTQDYMAV DPAFGDNSTL QTLINDIHST ANGPKGYLIL DGVFNHTGDS
310 320 330 340 350
HPWFDKYNNF SSQGAYESQS SPWYNYYTFY TWPDSYASFL GFNSLPKLNY
360 370 380 390 400
GNSGSAVRGV IYNNSNSVAK TYLNPPYSVD GWRLDAAQYV DANGNNGSDV
410 420 430 440 450
TNHQIWSEFR NAVKGVNSNA AIIGEYWGNA NPWTAQGNQW DAATNFDGFT
460 470 480 490 500
QPVSEWITGK DYQNNSASIS TTQFDSWLRG TRANYPTNVQ QSMMNFLSNH
510 520 530 540 550
DITRFATRSG GDLWKTYLAL IFQMTYVGTP TIYYGDEYGM QGGADPDNRR
560 570 580 590 600
SFDWSQATPS NSAVALTQKL ITIRNQYPAL RTGSFMTLIT DDTNKIYSYG
610 620 630 640 650
RFDNVNRIAV VLNNDSVSHT VNVPVWQLSM PNGSTVTDKI TGHSYTVQNG
660
MVTVAVDGHY GAVLAQ
Length:666
Mass (Da):74,296
Last modified:November 1, 1996 - v1
Checksum:iE99B15AA392AB6CB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13177 Genomic DNA. Translation: BAA02471.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13177 Genomic DNA. Translation: BAA02471.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ60053.
SMRiQ60053. Positions 30-666.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM34. Carbohydrate-Binding Module Family 34.
GH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ60053.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR004185. Glyco_hydro_13_lg-like_dom.
IPR013780. Glyco_hydro_b.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 2 hits.
PfamiPF00128. Alpha-amylase. 1 hit.
PF02903. Alpha-amylase_N. 1 hit.
[Graphical view]
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF81296. SSF81296. 1 hit.
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, CATALYTIC ACTIVITY, FUNCTION.
    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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 30-666 IN COMPLEX WITH CALCIUM, COFACTOR.
    Strain: R-47.

Entry informationi

Entry nameiNEPU1_THEVU
AccessioniPrimary (citable) accession number: Q60053
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.