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Q08751

- NEPU2_THEVU

UniProt

Q08751 - NEPU2_THEVU

Protein

Neopullulanase 2

Gene

tvaII

Organism
Thermoactinomyces vulgaris
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    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

    Binds 1 calcium 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

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MLLEAIFHEA KGSYAYPISE TQLRVRLRAK KGDVVRCEVL YADRYASPEE    50
    ELAHALAGKA GSDERFDYFE ALLECSTKRV KYVFLLTGPQ GEAVYFGETG 100
    FSAERSKAGV FQYAYIHRSE VFTTPEWAKE AVIYQIFPER FANGDPSNDP 150
    PGTEQWAKDA RPRHDSFYGG DLKGVIDRLP YLEELGVTAL YFTPIFASPS 200
    HHKYDTADYL AIDPQFGDLP TFRRLVDEAH RRGIKIILDA VFNHAGDQFF 250
    AFRDVLQKGE QSRYKDWFFI EDFPVSKTSR TNYETFAVQV PAMPKLRTEN 300
    PEVKEYLFDV ARFWMEQGID GWRLDVANEV DHAFWREFRR LVKSLNPDAL 350
    IVGEIWHDAS GWLMGDQFDS VMNYLFRESV IRFFATGEIH AERFDAELTR 400
    ARMLYPEQAA QGLWNLLDSH DTERFLTSCG GNEAKFRLAV LFQMTYLGTP 450
    LIYYGDEIGM AGATDPDCRR PMIWEEKEQN RGLFEFYKEL IRLRHRLASL 500
    TRGNVRSWHA DKQANLYAFV RTVQDQHVGV VLNNRGEKQT VLLQVPESGG 550
    KTWLDCLTGE EVHGKQGQLK LTLRPYQGMI LWNGR 585
    Length:585
    Mass (Da):67,467
    Last modified:November 1, 1995 - v1
    Checksum:iE311813A05A7791A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D13178 Genomic DNA. Translation: BAA02473.1.
    PIRiJC1486.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D13178 Genomic DNA. Translation: BAA02473.1 .
    PIRi JC1486.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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: October 1, 2014
    This is version 87 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