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Protein

Neopullulanase 2

Gene

tvaII

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

Functioni

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.1 Publication

Catalytic activityi

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

Cofactori

Ca2+1 PublicationNote: Binds 1 Ca2+ ion per subunit.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi143CalciumCombined sources1 Publication1
Metal bindingi145Calcium; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi148CalciumCombined sources1 Publication1
Metal bindingi149CalciumCombined sources1 Publication1
Metal bindingi169Calcium; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi171CalciumCombined sources1 Publication1
Binding sitei244SubstrateBy similarity1
Binding sitei323SubstrateBy similarity1
Active sitei325NucleophileBy similarity1
Active sitei354Proton donorBy similarity1
Sitei421Transition state stabilizerBy similarity1
Binding sitei465SubstrateBy similarity1
Binding sitei469SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Calcium, Metal-binding

Protein family/group databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Neopullulanase 2 (EC:3.2.1.1351 Publication)
Alternative name(s):
Alpha-amylase II
TVA II
Gene namesi
Name:tvaII
OrganismiThermoactinomyces vulgaris
Taxonomic identifieri2026 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesThermoactinomycetaceaeThermoactinomyces

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000543111 – 585Neopullulanase 2Add BLAST585

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1585
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 5Combined sources3
Turni12 – 14Combined sources3
Beta strandi15 – 19Combined sources5
Beta strandi22 – 30Combined sources9
Turni31 – 33Combined sources3
Beta strandi35 – 42Combined sources8
Beta strandi48 – 50Combined sources3
Beta strandi53 – 56Combined sources4
Beta strandi58 – 62Combined sources5
Beta strandi64 – 74Combined sources11
Beta strandi76 – 78Combined sources3
Beta strandi80 – 87Combined sources8
Beta strandi89 – 91Combined sources3
Beta strandi93 – 97Combined sources5
Beta strandi100 – 104Combined sources5
Helixi105 – 108Combined sources4
Beta strandi111 – 113Combined sources3
Helixi118 – 120Combined sources3
Helixi127 – 130Combined sources4
Beta strandi133 – 136Combined sources4
Helixi138 – 140Combined sources3
Helixi146 – 148Combined sources3
Helixi172 – 177Combined sources6
Helixi179 – 185Combined sources7
Beta strandi189 – 192Combined sources4
Beta strandi199 – 202Combined sources4
Beta strandi207 – 212Combined sources6
Turni214 – 216Combined sources3
Helixi219 – 230Combined sources12
Turni231 – 233Combined sources3
Beta strandi235 – 240Combined sources6
Helixi250 – 258Combined sources9
Helixi259 – 261Combined sources3
Helixi265 – 267Combined sources3
Beta strandi270 – 274Combined sources5
Beta strandi278 – 280Combined sources3
Beta strandi285 – 289Combined sources5
Beta strandi294 – 296Combined sources3
Helixi301 – 316Combined sources16
Beta strandi321 – 324Combined sources4
Helixi327 – 329Combined sources3
Helixi332 – 345Combined sources14
Beta strandi350 – 353Combined sources4
Helixi360 – 362Combined sources3
Beta strandi364 – 367Combined sources4
Beta strandi369 – 372Combined sources4
Helixi374 – 384Combined sources11
Helixi391 – 402Combined sources12
Helixi407 – 410Combined sources4
Beta strandi414 – 417Combined sources4
Helixi425 – 428Combined sources4
Turni429 – 431Combined sources3
Helixi433 – 445Combined sources13
Beta strandi446 – 453Combined sources8
Helixi456 – 458Combined sources3
Helixi467 – 469Combined sources3
Helixi476 – 478Combined sources3
Helixi481 – 496Combined sources16
Helixi498 – 502Combined sources5
Beta strandi504 – 511Combined sources8
Turni512 – 515Combined sources4
Beta strandi516 – 523Combined sources8
Beta strandi526 – 533Combined sources8
Beta strandi535 – 537Combined sources3
Beta strandi539 – 544Combined sources6
Helixi547 – 549Combined sources3
Beta strandi551 – 555Combined sources5
Turni556 – 558Combined sources3
Beta strandi561 – 563Combined sources3
Beta strandi568 – 573Combined sources6
Beta strandi578 – 582Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliQ08751.
SMRiQ08751.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ08751.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni420 – 421Substrate bindingBy similarity2

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

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.
IPR032091. Malt_amylase_C.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 2 hits.
PfamiPF00128. Alpha-amylase. 1 hit.
PF02903. Alpha-amylase_N. 1 hit.
PF16657. Malt_amylase_C. 1 hit.
[Graphical view]
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF81296. SSF81296. 1 hit.

Sequencei

Sequence statusi: Complete.

Q08751-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLEAIFHEA KGSYAYPISE TQLRVRLRAK KGDVVRCEVL YADRYASPEE
60 70 80 90 100
ELAHALAGKA GSDERFDYFE ALLECSTKRV KYVFLLTGPQ GEAVYFGETG
110 120 130 140 150
FSAERSKAGV FQYAYIHRSE VFTTPEWAKE AVIYQIFPER FANGDPSNDP
160 170 180 190 200
PGTEQWAKDA RPRHDSFYGG DLKGVIDRLP YLEELGVTAL YFTPIFASPS
210 220 230 240 250
HHKYDTADYL AIDPQFGDLP TFRRLVDEAH RRGIKIILDA VFNHAGDQFF
260 270 280 290 300
AFRDVLQKGE QSRYKDWFFI EDFPVSKTSR TNYETFAVQV PAMPKLRTEN
310 320 330 340 350
PEVKEYLFDV ARFWMEQGID GWRLDVANEV DHAFWREFRR LVKSLNPDAL
360 370 380 390 400
IVGEIWHDAS GWLMGDQFDS VMNYLFRESV IRFFATGEIH AERFDAELTR
410 420 430 440 450
ARMLYPEQAA QGLWNLLDSH DTERFLTSCG GNEAKFRLAV LFQMTYLGTP
460 470 480 490 500
LIYYGDEIGM AGATDPDCRR PMIWEEKEQN RGLFEFYKEL IRLRHRLASL
510 520 530 540 550
TRGNVRSWHA DKQANLYAFV RTVQDQHVGV VLNNRGEKQT VLLQVPESGG
560 570 580
KTWLDCLTGE EVHGKQGQLK LTLRPYQGMI LWNGR
Length:585
Mass (Da):67,467
Last modified:November 1, 1995 - v1
Checksum:iE311813A05A7791A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13178 Genomic DNA. Translation: BAA02473.1.
PIRiJC1486.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13178 Genomic DNA. Translation: BAA02473.1.
PIRiJC1486.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliQ08751.
SMRiQ08751.
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

EvolutionaryTraceiQ08751.

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.
IPR032091. Malt_amylase_C.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 2 hits.
PfamiPF00128. Alpha-amylase. 1 hit.
PF02903. Alpha-amylase_N. 1 hit.
PF16657. Malt_amylase_C. 1 hit.
[Graphical view]
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF81296. SSF81296. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiNEPU2_THEVU
AccessioniPrimary (citable) accession number: Q08751
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 2, 2016
This is version 95 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.