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Protein

Neopullulanase

Gene

nplT

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
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.

Catalytic activityi

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

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi147 – 1471CalciumCombined sources1 Publication
Metal bindingi149 – 1491Calcium; via carbonyl oxygenCombined sources1 Publication
Metal bindingi153 – 1531CalciumCombined sources1 Publication
Metal bindingi172 – 1721Calcium; via carbonyl oxygenCombined sources1 Publication
Metal bindingi174 – 1741CalciumCombined sources1 Publication
Binding sitei247 – 2471Substrate1 Publication
Binding sitei326 – 3261Substrate1 Publication
Active sitei328 – 3281Nucleophile1 Publication
Active sitei357 – 3571Proton donor1 Publication
Sitei424 – 4241Transition state stabilizerBy similarity
Binding sitei468 – 4681Substrate1 Publication
Binding sitei472 – 4721Substrate1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.2.1.135. 623.

Protein family/group databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Neopullulanase (EC:3.2.1.135)
Gene namesi
Name:nplT
OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifieri1422 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 588588NeopullulanasePRO_0000054310Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1
588
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 53Combined sources
Turni12 – 143Combined sources
Beta strandi15 – 217Combined sources
Beta strandi23 – 308Combined sources
Turni31 – 333Combined sources
Beta strandi35 – 428Combined sources
Beta strandi47 – 504Combined sources
Beta strandi55 – 584Combined sources
Beta strandi60 – 645Combined sources
Beta strandi66 – 7510Combined sources
Beta strandi82 – 909Combined sources
Beta strandi93 – 986Combined sources
Beta strandi101 – 1055Combined sources
Beta strandi114 – 1174Combined sources
Helixi122 – 1243Combined sources
Helixi130 – 1345Combined sources
Beta strandi137 – 1404Combined sources
Helixi142 – 1443Combined sources
Helixi150 – 1523Combined sources
Helixi175 – 1806Combined sources
Helixi182 – 1887Combined sources
Beta strandi192 – 1954Combined sources
Beta strandi202 – 2054Combined sources
Beta strandi210 – 2156Combined sources
Turni217 – 2193Combined sources
Helixi222 – 23413Combined sources
Beta strandi238 – 2436Combined sources
Helixi253 – 2619Combined sources
Helixi262 – 2643Combined sources
Helixi268 – 2703Combined sources
Beta strandi273 – 2775Combined sources
Beta strandi281 – 2833Combined sources
Beta strandi295 – 2984Combined sources
Helixi303 – 32018Combined sources
Beta strandi324 – 3274Combined sources
Helixi330 – 3323Combined sources
Helixi335 – 34814Combined sources
Beta strandi353 – 3564Combined sources
Helixi363 – 3653Combined sources
Beta strandi367 – 3704Combined sources
Beta strandi372 – 3754Combined sources
Helixi377 – 38711Combined sources
Helixi394 – 40613Combined sources
Helixi410 – 4145Combined sources
Beta strandi417 – 4204Combined sources
Beta strandi423 – 4253Combined sources
Helixi428 – 4314Combined sources
Turni432 – 4343Combined sources
Helixi436 – 44813Combined sources
Beta strandi449 – 4513Combined sources
Beta strandi454 – 4563Combined sources
Helixi459 – 4613Combined sources
Helixi470 – 4723Combined sources
Turni479 – 4813Combined sources
Helixi484 – 49916Combined sources
Helixi501 – 5055Combined sources
Beta strandi507 – 5115Combined sources
Turni516 – 5183Combined sources
Beta strandi519 – 5257Combined sources
Beta strandi530 – 5367Combined sources
Beta strandi538 – 5403Combined sources
Beta strandi542 – 5454Combined sources
Beta strandi551 – 5577Combined sources
Turni558 – 5603Combined sources
Beta strandi563 – 5653Combined sources
Beta strandi568 – 5703Combined sources
Beta strandi572 – 5754Combined sources
Beta strandi580 – 5878Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1J0HX-ray1.90A/B1-588[»]
1J0IX-ray2.40A/B1-588[»]
1J0JX-ray2.80A/B1-588[»]
1J0KX-ray3.20A/B1-588[»]
ProteinModelPortaliP38940.
SMRiP38940. Positions 1-588.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP38940.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni423 – 4242Substrate binding1 Publication

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.
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.
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.

Sequencei

Sequence statusi: Complete.

P38940-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRKEAIYHRP ADNFAYAYDS ETLHLRLRTK KDDIDRVELL HGDPYDWQNG
60 70 80 90 100
AWQFQMMPMR KTGSDELFDY WFAEVKPPYR RLRYGFVLYS GEEKLVYTEK
110 120 130 140 150
GFYFEVPTDD TAYYFCFPFL HRVDLFEAPD WVKDTVWYQI FPERFANGNP
160 170 180 190 200
SISPEGSRPW GSEDPTPTSF FGGDLQGIID HLDYLVDLGI TGIYLTPIFR
210 220 230 240 250
SPSNHKYDTA DYFEVDPHFG DKETLKTLID RCHEKGIRVM LDAVFNHCGY
260 270 280 290 300
EFAPFQDVWK NGESSKYKDW FHIHEFPLQT EPRPNYDTFR FVPQMPKLNT
310 320 330 340 350
ANPEVKRYLL DVATYWIREF DIDGWRLDVA NEIDHEFWRE FRQEVKALKP
360 370 380 390 400
DVYILGEIWH DAMPWLRGDQ FDAVMNYPFT DGVLRFFAKE EISARQFANQ
410 420 430 440 450
MMHVLHSYPN NVNEAAFNLL GSHDTSRILT VCGGDIRKVK LLFLFQLTFT
460 470 480 490 500
GSPCIYYGDE IGMTGGNDPE CRKCMVWDPM QQNKELHQHV KQLIALRKQY
510 520 530 540 550
RSLRRGEISF LHADDEMNYL IYKKTDGDET VLVIINRSDQ KADIPIPLDA
560 570 580
RGTWLVNLLT GERFAAEAET LCTSLPPYGF VLYAIEHW
Length:588
Mass (Da):69,145
Last modified:February 1, 1995 - v1
Checksum:iB2C7195D1CE34A33
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M28138 Genomic DNA. Translation: AAA22622.1.
PIRiA37008.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M28138 Genomic DNA. Translation: AAA22622.1.
PIRiA37008.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1J0HX-ray1.90A/B1-588[»]
1J0IX-ray2.40A/B1-588[»]
1J0JX-ray2.80A/B1-588[»]
1J0KX-ray3.20A/B1-588[»]
ProteinModelPortaliP38940.
SMRiP38940. Positions 1-588.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.2.1.135. 623.

Miscellaneous databases

EvolutionaryTraceiP38940.

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.
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.
ProtoNetiSearch...

Publicationsi

  1. "Nucleotide sequence of the neopullulanase gene from Bacillus stearothermophilus."
    Kuriki T., Imanaka T.
    J. Gen. Microbiol. 135:1521-1528(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-5.
    Strain: TRS40.
  2. "Three-dimensional structure and substrate binding of Bacillus stearothermophilus neopullulanase."
    Hondoh H., Kuriki T., Matsuura Y.
    J. Mol. Biol. 326:177-188(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH CALCIUM AND GLUCOSE, COFACTOR, SUBUNIT, ACTIVE SITE.

Entry informationi

Entry nameiNEPU_GEOSE
AccessioniPrimary (citable) accession number: P38940
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: May 11, 2016
This is version 92 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, Direct protein sequencing

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.