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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)DescriptionActionsGraphical viewLength
Metal bindingi147CalciumCombined sources1 Publication1
Metal bindingi149Calcium; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi153CalciumCombined sources1 Publication1
Metal bindingi172Calcium; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi174CalciumCombined sources1 Publication1
Binding sitei247Substrate1 Publication1
Binding sitei326Substrate1 Publication1
Active sitei328Nucleophile1 Publication1
Active sitei357Proton donor1 Publication1
Sitei424Transition state stabilizerBy similarity1
Binding sitei468Substrate1 Publication1
Binding sitei472Substrate1 Publication1

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)DescriptionActionsGraphical viewLength
ChainiPRO_00000543101 – 588NeopullulanaseAdd BLAST588

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1588
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 5Combined sources3
Turni12 – 14Combined sources3
Beta strandi15 – 21Combined sources7
Beta strandi23 – 30Combined sources8
Turni31 – 33Combined sources3
Beta strandi35 – 42Combined sources8
Beta strandi47 – 50Combined sources4
Beta strandi55 – 58Combined sources4
Beta strandi60 – 64Combined sources5
Beta strandi66 – 75Combined sources10
Beta strandi82 – 90Combined sources9
Beta strandi93 – 98Combined sources6
Beta strandi101 – 105Combined sources5
Beta strandi114 – 117Combined sources4
Helixi122 – 124Combined sources3
Helixi130 – 134Combined sources5
Beta strandi137 – 140Combined sources4
Helixi142 – 144Combined sources3
Helixi150 – 152Combined sources3
Helixi175 – 180Combined sources6
Helixi182 – 188Combined sources7
Beta strandi192 – 195Combined sources4
Beta strandi202 – 205Combined sources4
Beta strandi210 – 215Combined sources6
Turni217 – 219Combined sources3
Helixi222 – 234Combined sources13
Beta strandi238 – 243Combined sources6
Helixi253 – 261Combined sources9
Helixi262 – 264Combined sources3
Helixi268 – 270Combined sources3
Beta strandi273 – 277Combined sources5
Beta strandi281 – 283Combined sources3
Beta strandi295 – 298Combined sources4
Helixi303 – 320Combined sources18
Beta strandi324 – 327Combined sources4
Helixi330 – 332Combined sources3
Helixi335 – 348Combined sources14
Beta strandi353 – 356Combined sources4
Helixi363 – 365Combined sources3
Beta strandi367 – 370Combined sources4
Beta strandi372 – 375Combined sources4
Helixi377 – 387Combined sources11
Helixi394 – 406Combined sources13
Helixi410 – 414Combined sources5
Beta strandi417 – 420Combined sources4
Beta strandi423 – 425Combined sources3
Helixi428 – 431Combined sources4
Turni432 – 434Combined sources3
Helixi436 – 448Combined sources13
Beta strandi449 – 451Combined sources3
Beta strandi454 – 456Combined sources3
Helixi459 – 461Combined sources3
Helixi470 – 472Combined sources3
Turni479 – 481Combined sources3
Helixi484 – 499Combined sources16
Helixi501 – 505Combined sources5
Beta strandi507 – 511Combined sources5
Turni516 – 518Combined sources3
Beta strandi519 – 525Combined sources7
Beta strandi530 – 536Combined sources7
Beta strandi538 – 540Combined sources3
Beta strandi542 – 545Combined sources4
Beta strandi551 – 557Combined sources7
Turni558 – 560Combined sources3
Beta strandi563 – 565Combined sources3
Beta strandi568 – 570Combined sources3
Beta strandi572 – 575Combined sources4
Beta strandi580 – 587Combined sources8

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP38940.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni423 – 424Substrate binding1 Publication2

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.
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
PDB 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.
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

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.
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...

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: 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, 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.