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Q08751

- NEPU2_THEVU

UniProt

Q08751 - NEPU2_THEVU

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Protein

Neopullulanase 2

Gene

tvaII

Organism
Thermoactinomyces vulgaris
Status
Reviewed - 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.

Catalytic activityi

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

Cofactori

Ca2+Note: Binds 1 Ca(2+) ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi143 – 1431Calcium
Metal bindingi145 – 1451Calcium; via carbonyl oxygen
Metal bindingi148 – 1481Calcium
Metal bindingi149 – 1491Calcium
Metal bindingi169 – 1691Calcium; via carbonyl oxygen
Metal bindingi171 – 1711Calcium
Active sitei325 – 3251Nucleophile
Active sitei354 – 3541Proton donor
Sitei421 – 4211Transition state stabilizerBy similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. neopullulanase activity Source: UniProtKB-EC

GO - Biological processi

  1. carbohydrate metabolic process Source: UniProtKB-KW
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:3.2.1.135)
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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 585585Neopullulanase 2PRO_0000054311Add
BLAST

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1
585
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 53Combined sources
Turni12 – 143Combined sources
Beta strandi15 – 195Combined sources
Beta strandi22 – 309Combined sources
Turni31 – 333Combined sources
Beta strandi35 – 428Combined sources
Beta strandi48 – 503Combined sources
Beta strandi53 – 564Combined sources
Beta strandi58 – 625Combined sources
Beta strandi64 – 7411Combined sources
Beta strandi76 – 783Combined sources
Beta strandi80 – 878Combined sources
Beta strandi89 – 913Combined sources
Beta strandi93 – 975Combined sources
Beta strandi100 – 1045Combined sources
Helixi105 – 1084Combined sources
Beta strandi111 – 1133Combined sources
Helixi118 – 1203Combined sources
Helixi127 – 1304Combined sources
Beta strandi133 – 1364Combined sources
Helixi138 – 1403Combined sources
Helixi146 – 1483Combined sources
Helixi172 – 1776Combined sources
Helixi179 – 1857Combined sources
Beta strandi189 – 1924Combined sources
Beta strandi199 – 2024Combined sources
Beta strandi207 – 2126Combined sources
Turni214 – 2163Combined sources
Helixi219 – 23012Combined sources
Turni231 – 2333Combined sources
Beta strandi235 – 2406Combined sources
Helixi250 – 2589Combined sources
Helixi259 – 2613Combined sources
Helixi265 – 2673Combined sources
Beta strandi270 – 2745Combined sources
Beta strandi278 – 2803Combined sources
Beta strandi285 – 2895Combined sources
Beta strandi294 – 2963Combined sources
Helixi301 – 31616Combined sources
Beta strandi321 – 3244Combined sources
Helixi327 – 3293Combined sources
Helixi332 – 34514Combined sources
Beta strandi350 – 3534Combined sources
Helixi360 – 3623Combined sources
Beta strandi364 – 3674Combined sources
Beta strandi369 – 3724Combined sources
Helixi374 – 38411Combined sources
Helixi391 – 40212Combined sources
Helixi407 – 4104Combined sources
Beta strandi414 – 4174Combined sources
Helixi425 – 4284Combined sources
Turni429 – 4313Combined sources
Helixi433 – 44513Combined sources
Beta strandi446 – 4538Combined sources
Helixi456 – 4583Combined sources
Helixi467 – 4693Combined sources
Helixi476 – 4783Combined sources
Helixi481 – 49616Combined sources
Helixi498 – 5025Combined sources
Beta strandi504 – 5118Combined sources
Turni512 – 5154Combined sources
Beta strandi516 – 5238Combined sources
Beta strandi526 – 5338Combined sources
Beta strandi535 – 5373Combined sources
Beta strandi539 – 5446Combined sources
Helixi547 – 5493Combined sources
Beta strandi551 – 5555Combined sources
Turni556 – 5583Combined sources
Beta strandi561 – 5633Combined sources
Beta strandi568 – 5736Combined sources
Beta strandi578 – 5825Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 1-585.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ08751.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR006048. 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]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 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.

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 .
PIRi JC1486.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BVZ X-ray 2.60 A/B 1-585 [» ]
1G1Y X-ray 3.00 A/B 1-585 [» ]
1JF5 X-ray 3.20 A/B 1-585 [» ]
1JF6 X-ray 3.20 A/B 1-585 [» ]
1JI2 X-ray 2.30 A/B 1-585 [» ]
1JIB X-ray 3.30 A/B 1-585 [» ]
1JL8 X-ray 3.20 A/B 1-585 [» ]
1VB9 X-ray 2.20 A/B 1-585 [» ]
1VFM X-ray 2.90 A/B 1-585 [» ]
1VFO X-ray 2.81 A/B 1-585 [» ]
1VFU X-ray 3.10 A/B 1-585 [» ]
1WZK X-ray 2.30 A/B 1-585 [» ]
1WZL X-ray 2.00 A/B 1-585 [» ]
1WZM X-ray 3.20 A/B 1-585 [» ]
2D2O X-ray 2.10 A/B 1-585 [» ]
3A6O X-ray 2.80 A/B 1-585 [» ]
ProteinModelPortali Q08751.
SMRi Q08751. Positions 1-585.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi CBM34. Carbohydrate-Binding Module Family 34.
GH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei Q08751.

Family and domain databases

Gene3Di 2.60.40.10. 1 hit.
2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProi IPR006048. 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 ]
PANTHERi PTHR10357. PTHR10357. 1 hit.
Pfami PF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
PF02903. Alpha-amylase_N. 1 hit.
[Graphical view ]
SMARTi SM00642. Aamy. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
SSF81296. SSF81296. 1 hit.
ProtoNeti Search...

Publicationsi

  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).

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 26, 2014
This is version 88 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

External Data

Dasty 3