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Protein

Pullulanase

Gene

pulA

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Hydrolysis of (1->6)-alpha-D-glucosidic linkages in pullulan, amylopectin and glycogen, and in the alpha- and beta-limit dextrins of amylopectin and glycogen.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei535 – 5351NucleophileBy similarity
Active sitei564 – 5641Proton donorBy similarity
Sitei652 – 6521Transition state stabilizerBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Protein family/group databases

CAZyiCBM41. Carbohydrate-Binding Module Family 41.
CBM48. Carbohydrate-Binding Module Family 48.
GH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
Pullulanase (EC:3.2.1.41)
Alternative name(s):
Alpha-dextrin endo-1,6-alpha-glucosidase
Pullulan 6-glucanohydrolase
Gene namesi
Name:pulA
Ordered Locus Names:TM_1845
OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Taxonomic identifieri243274 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
Proteomesi
  • UP000008183 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence analysisAdd
BLAST
Chaini20 – 843824PullulanasePRO_0000001428Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi243274.TM1845.

Structurei

Secondary structure

1
843
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi21 – 288Combined sources
Beta strandi37 – 4711Combined sources
Beta strandi52 – 543Combined sources
Beta strandi58 – 603Combined sources
Beta strandi63 – 7210Combined sources
Beta strandi75 – 839Combined sources
Turni84 – 874Combined sources
Beta strandi88 – 9811Combined sources
Beta strandi103 – 1097Combined sources
Beta strandi116 – 1183Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2J71X-ray1.69A18-120[»]
2J72X-ray1.49A/B18-120[»]
2J73X-ray1.40A/B18-120[»]
ProteinModelPortaliO33840.
SMRiO33840. Positions 18-120.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO33840.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4108IUM. Bacteria.
COG1523. LUCA.
InParanoidiO33840.
KOiK01200.
OMAiWHASNSI.
OrthoDBiEOG66TG1T.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR013784. Carb-bd-like_fold.
IPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR004193. Glyco_hydro_13_N.
IPR013780. Glyco_hydro_b.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR005323. PUD.
IPR011840. PulA_typeI.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
PF02922. CBM_48. 1 hit.
PF03714. PUD. 1 hit.
[Graphical view]
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF49452. SSF49452. 1 hit.
SSF51445. SSF51445. 1 hit.
SSF81296. SSF81296. 1 hit.
TIGRFAMsiTIGR02104. pulA_typeI. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O33840-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTKLWLLLV LLLSALIFSE TTIVVHYHRY DGKYDGWNLW IWPVEPVSQE
60 70 80 90 100
GKAYQFTGED DFGKVAVVKL PMDLTKVGII VRLNEWQAKD VAKDRFIEIK
110 120 130 140 150
DGKAEVWILQ GVEEIFYEKP DTSPRIFFAQ ARSNKVIEAF LTNPVDTKKK
160 170 180 190 200
ELFKVTVDGK EIPVSRVEKA DPTDIDVTNY VRIVLSESLK EEDLRKDVEL
210 220 230 240 250
IIEGYKPARV IMMEILDDYY YDGELGAVYS PEKTIFRVWS PVSKWVKVLL
260 270 280 290 300
FKNGEDTEPY QVVNMEYKGN GVWEAVVEGD LDGVFYLYQL ENYGKIRTTV
310 320 330 340 350
DPYSKAVYAN SKKSAVVNLA RTNPEGWEND RGPKIEGYED AIIYEIHIAD
360 370 380 390 400
ITGLENSGVK NKGLYLGLTE ENTKGPGGVT TGLSHLVELG VTHVHILPFF
410 420 430 440 450
DFYTGDELDK DFEKYYNWGY DPYLFMVPEG RYSTDPKNPH TRIREVKEMV
460 470 480 490 500
KALHKHGIGV IMDMVFPHTY GIGELSAFDQ TVPYYFYRID KTGAYLNESG
510 520 530 540 550
CGNVIASERP MMRKFIVDTV TYWVKEYHID GFRFDQMGLI DKKTMLEVER
560 570 580 590 600
ALHKIDPTII LYGEPWGGWG APIRFGKSDV AGTHVAAFND EFRDAIRGSV
610 620 630 640 650
FNPSVKGFVM GGYGKETKIK RGVVGSINYD GKLIKSFALD PEETINYAAC
660 670 680 690 700
HDNHTLWDKN YLAAKADKKK EWTEEELKNA QKLAGAILLT SQGVPFLHGG
710 720 730 740 750
QDFCRTKNFN DNSYNAPISI NGFDYERKLQ FIDVFNYHKG LIKLRKEHPA
760 770 780 790 800
FRLKNAEEIK KHLEFLPGGR RIVAFMLKDH AGGDPWKDIV VIYNGNLEKT
810 820 830 840
TYKLPEGKWN VVVNSQKAGT EVIETVEGTI ELDPLSAYVL YRE
Length:843
Mass (Da):96,262
Last modified:June 1, 1998 - v2
Checksum:iC42DDE233D54FE77
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ001087 Genomic DNA. Translation: CAA04522.1.
AE000512 Genomic DNA. Translation: AAD36907.1.
PIRiH72204.
RefSeqiNP_229641.1. NC_000853.1.
WP_004082389.1. NZ_CP011107.1.

Genome annotation databases

EnsemblBacteriaiAAD36907; AAD36907; TM_1845.
GeneIDi897812.
KEGGitma:TM1845.
PATRICi23938679. VBITheMar51294_1866.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ001087 Genomic DNA. Translation: CAA04522.1.
AE000512 Genomic DNA. Translation: AAD36907.1.
PIRiH72204.
RefSeqiNP_229641.1. NC_000853.1.
WP_004082389.1. NZ_CP011107.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2J71X-ray1.69A18-120[»]
2J72X-ray1.49A/B18-120[»]
2J73X-ray1.40A/B18-120[»]
ProteinModelPortaliO33840.
SMRiO33840. Positions 18-120.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243274.TM1845.

Protein family/group databases

CAZyiCBM41. Carbohydrate-Binding Module Family 41.
CBM48. Carbohydrate-Binding Module Family 48.
GH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD36907; AAD36907; TM_1845.
GeneIDi897812.
KEGGitma:TM1845.
PATRICi23938679. VBITheMar51294_1866.

Phylogenomic databases

eggNOGiENOG4108IUM. Bacteria.
COG1523. LUCA.
InParanoidiO33840.
KOiK01200.
OMAiWHASNSI.
OrthoDBiEOG66TG1T.

Miscellaneous databases

EvolutionaryTraceiO33840.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR013784. Carb-bd-like_fold.
IPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR004193. Glyco_hydro_13_N.
IPR013780. Glyco_hydro_b.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR005323. PUD.
IPR011840. PulA_typeI.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
PF02922. CBM_48. 1 hit.
PF03714. PUD. 1 hit.
[Graphical view]
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF49452. SSF49452. 1 hit.
SSF51445. SSF51445. 1 hit.
SSF81296. SSF81296. 1 hit.
TIGRFAMsiTIGR02104. pulA_typeI. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and analysis of genes for amylolytic enzymes of the hyperthermophilic bacterium Thermotoga maritima."
    Bibel M., Brettl C., Gosslar U., Kriegshaeuser G., Liebl W.
    FEMS Microbiol. Lett. 158:9-15(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.

Entry informationi

Entry nameiPULA_THEMA
AccessioniPrimary (citable) accession number: O33840
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 1, 1998
Last modified: July 6, 2016
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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.