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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)DescriptionActionsGraphical viewLength
Metal bindingi31Calcium 1; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi33Calcium 1Combined sources1 Publication1
Metal bindingi35Calcium 1; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi71Calcium 1Combined sources1 Publication1
Metal bindingi125Calcium 1Combined sources1 Publication1
Metal bindingi174Calcium 2Combined sources1 Publication1
Metal bindingi176Calcium 2; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi179Calcium 2Combined sources1 Publication1
Metal bindingi180Calcium 2Combined sources1 Publication1
Metal bindingi216Calcium 2; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi218Calcium 2Combined sources1 Publication1
Binding sitei296SubstrateBy similarity1
Metal bindingi305Calcium 3Combined sources1 Publication1
Metal bindingi309Calcium 3Combined sources1 Publication1
Metal bindingi310Calcium 3; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi312Calcium 3; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi317Calcium 3Combined sources1 Publication1
Binding sitei383SubstrateBy similarity1
Active sitei385NucleophileBy similarity1
Active sitei425Proton donorBy similarity1
Sitei501Transition state stabilizerBy similarity1
Binding sitei545SubstrateBy similarity1
Binding sitei549SubstrateBy similarity1

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 29Add BLAST29
ChainiPRO_000000144530 – 666Neopullulanase 1Add BLAST637

Structurei

Secondary structure

1666
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi32 – 34Combined sources3
Helixi38 – 40Combined sources3
Turni47 – 49Combined sources3
Beta strandi61 – 68Combined sources8
Beta strandi73 – 81Combined sources9
Turni82 – 84Combined sources3
Beta strandi85 – 91Combined sources7
Beta strandi93 – 97Combined sources5
Beta strandi101 – 110Combined sources10
Beta strandi117 – 125Combined sources9
Beta strandi128 – 133Combined sources6
Beta strandi136 – 140Combined sources5
Beta strandi147 – 149Combined sources3
Helixi157 – 161Combined sources5
Beta strandi164 – 167Combined sources4
Helixi169 – 171Combined sources3
Helixi177 – 179Combined sources3
Beta strandi187 – 190Combined sources4
Helixi210 – 212Combined sources3
Helixi219 – 224Combined sources6
Helixi226 – 230Combined sources5
Turni231 – 233Combined sources3
Beta strandi237 – 241Combined sources5
Beta strandi247 – 250Combined sources4
Beta strandi255 – 260Combined sources6
Turni262 – 264Combined sources3
Helixi267 – 278Combined sources12
Beta strandi280 – 284Combined sources5
Beta strandi287 – 292Combined sources6
Turni302 – 304Combined sources3
Beta strandi310 – 312Combined sources3
Turni315 – 317Combined sources3
Helixi324 – 326Combined sources3
Beta strandi329 – 331Combined sources3
Turni332 – 334Combined sources3
Beta strandi342 – 349Combined sources8
Helixi356 – 361Combined sources6
Helixi368 – 373Combined sources6
Turni375 – 377Combined sources3
Beta strandi381 – 384Combined sources4
Helixi387 – 389Combined sources3
Beta strandi397 – 399Combined sources3
Helixi400 – 416Combined sources17
Beta strandi421 – 424Combined sources4
Helixi431 – 433Combined sources3
Turni434 – 436Combined sources3
Beta strandi437 – 439Combined sources3
Beta strandi441 – 444Combined sources4
Turni446 – 449Combined sources4
Helixi450 – 457Combined sources8
Beta strandi458 – 460Combined sources3
Helixi471 – 482Combined sources12
Helixi487 – 490Combined sources4
Beta strandi494 – 497Combined sources4
Helixi505 – 508Combined sources4
Turni509 – 511Combined sources3
Helixi513 – 523Combined sources11
Beta strandi526 – 533Combined sources8
Helixi536 – 538Combined sources3
Helixi547 – 549Combined sources3
Beta strandi556 – 558Combined sources3
Helixi562 – 576Combined sources15
Helixi578 – 582Combined sources5
Beta strandi583 – 591Combined sources9
Turni592 – 595Combined sources4
Beta strandi596 – 602Combined sources7
Beta strandi607 – 613Combined sources7
Beta strandi615 – 617Combined sources3
Beta strandi619 – 623Combined sources5
Helixi625 – 628Combined sources4
Beta strandi635 – 638Combined sources4
Turni639 – 641Combined sources3
Beta strandi644 – 646Combined sources3
Beta strandi651 – 656Combined sources6
Beta strandi660 – 666Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ60053.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni500 – 501Substrate bindingBy similarity2

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

Keywords - Domaini

Signal

Family and domain databases

CDDicd02857. E_set_CDase_PDE_N. 1 hit.
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
PDB 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.
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

CDDicd02857. E_set_CDase_PDE_N. 1 hit.
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...

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: November 2, 2016
This is version 93 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.