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Protein

Pullulanase

Gene

pulA

Organism
Klebsiella pneumoniae
Status
Reviewed-Annotation score: Annotation score: 3 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 sitei684 – 6841NucleophileBy similarity
Active sitei713 – 7131Proton donorBy similarity
Sitei841 – 8411Transition 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
OrganismiKlebsiella pneumoniae
Taxonomic identifieri573 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeKlebsiella

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919PROSITE-ProRule annotationAdd
BLAST
Chaini20 – 10901071PullulanasePRO_0000001427Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi20 – 201N-palmitoyl cysteinePROSITE-ProRule annotation
Lipidationi20 – 201S-diacylglycerol cysteinePROSITE-ProRule annotation

Keywords - PTMi

Lipoprotein, Palmitate

Interactioni

Subunit structurei

Homotrimer.

Structurei

Secondary structure

1
1090
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi60 – 667Combined sources
Helixi68 – 714Combined sources
Beta strandi80 – 878Combined sources
Beta strandi95 – 973Combined sources
Beta strandi118 – 1247Combined sources
Beta strandi126 – 14419Combined sources
Beta strandi146 – 1494Combined sources
Turni150 – 1523Combined sources
Beta strandi157 – 1615Combined sources
Beta strandi168 – 1703Combined sources
Helixi171 – 1788Combined sources
Beta strandi186 – 1883Combined sources
Beta strandi190 – 1956Combined sources
Helixi197 – 1993Combined sources
Beta strandi203 – 21311Combined sources
Beta strandi221 – 2233Combined sources
Beta strandi231 – 2333Combined sources
Helixi237 – 2426Combined sources
Helixi244 – 2463Combined sources
Beta strandi251 – 2533Combined sources
Helixi260 – 2634Combined sources
Beta strandi266 – 2738Combined sources
Beta strandi278 – 2869Combined sources
Helixi288 – 29912Combined sources
Beta strandi305 – 3095Combined sources
Beta strandi312 – 3187Combined sources
Beta strandi323 – 3308Combined sources
Beta strandi336 – 3416Combined sources
Beta strandi343 – 3453Combined sources
Turni346 – 3494Combined sources
Beta strandi350 – 3556Combined sources
Helixi357 – 3593Combined sources
Beta strandi363 – 3719Combined sources
Turni373 – 3753Combined sources
Beta strandi377 – 3837Combined sources
Beta strandi389 – 3913Combined sources
Helixi393 – 3953Combined sources
Beta strandi397 – 3993Combined sources
Helixi406 – 4083Combined sources
Helixi425 – 4295Combined sources
Beta strandi432 – 4365Combined sources
Helixi438 – 4425Combined sources
Helixi450 – 4523Combined sources
Helixi456 – 4605Combined sources
Helixi465 – 47612Combined sources
Beta strandi480 – 4845Combined sources
Beta strandi487 – 4926Combined sources
Helixi496 – 4983Combined sources
Helixi506 – 5127Combined sources
Helixi514 – 5174Combined sources
Helixi522 – 5254Combined sources
Beta strandi526 – 5283Combined sources
Helixi531 – 5399Combined sources
Helixi548 – 5569Combined sources
Beta strandi559 – 5613Combined sources
Beta strandi568 – 5747Combined sources
Helixi586 – 60015Combined sources
Beta strandi605 – 6106Combined sources
Beta strandi613 – 6164Combined sources
Turni619 – 6213Combined sources
Helixi627 – 6304Combined sources
Turni632 – 6343Combined sources
Turni640 – 6423Combined sources
Beta strandi650 – 6545Combined sources
Helixi659 – 67416Combined sources
Beta strandi680 – 6834Combined sources
Helixi686 – 6883Combined sources
Helixi691 – 70212Combined sources
Beta strandi709 – 7124Combined sources
Turni720 – 7223Combined sources
Turni728 – 7347Combined sources
Beta strandi737 – 7393Combined sources
Helixi741 – 7488Combined sources
Helixi758 – 7614Combined sources
Turni765 – 7717Combined sources
Helixi781 – 79515Combined sources
Beta strandi799 – 8013Combined sources
Beta strandi803 – 8053Combined sources
Beta strandi811 – 8133Combined sources
Helixi814 – 8163Combined sources
Beta strandi817 – 8193Combined sources
Beta strandi822 – 8243Combined sources
Beta strandi827 – 8293Combined sources
Helixi830 – 8323Combined sources
Beta strandi833 – 8353Combined sources
Beta strandi840 – 8423Combined sources
Helixi845 – 8528Combined sources
Helixi859 – 87416Combined sources
Beta strandi876 – 8838Combined sources
Helixi886 – 8883Combined sources
Helixi898 – 9003Combined sources
Helixi902 – 9054Combined sources
Beta strandi918 – 9203Combined sources
Helixi924 – 9274Combined sources
Helixi928 – 9303Combined sources
Helixi931 – 9388Combined sources
Helixi946 – 96419Combined sources
Helixi967 – 9693Combined sources
Helixi974 – 9807Combined sources
Beta strandi981 – 9855Combined sources
Beta strandi994 – 10007Combined sources
Turni1003 – 10053Combined sources
Beta strandi1011 – 102111Combined sources
Beta strandi1023 – 10253Combined sources
Beta strandi1027 – 10293Combined sources
Turni1031 – 10344Combined sources
Helixi1041 – 10466Combined sources
Helixi1047 – 10493Combined sources
Turni1051 – 10544Combined sources
Beta strandi1063 – 10653Combined sources
Beta strandi1067 – 107610Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YOCX-ray2.88A/B21-1089[»]
ProteinModelPortaliP07206.
SMRiP07206. Positions 173-1090.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07206.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.20.20.80. 4 hits.
InterProiIPR013784. Carb-bd-like_fold.
IPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR004193. Glyco_hydro_13_N.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR005323. PUD.
IPR011839. Pullul_strch.
IPR024561. Pullul_strch_C.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 5 hits.
PfamiPF02922. CBM_48. 1 hit.
PF11852. DUF3372. 1 hit.
PF03714. PUD. 1 hit.
[Graphical view]
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF49452. SSF49452. 1 hit.
SSF51445. SSF51445. 1 hit.
SSF81296. SSF81296. 2 hits.
TIGRFAMsiTIGR02103. pullul_strch. 1 hit.
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P07206-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRYTRNALV LGSLVLLSGC DNGSSSSSSG NPDTPDNQDV VVRLPDVAVP
60 70 80 90 100
GEAVTAVENQ AVIHLVDIAG ITSSSAADYS SKNLYLWNNE TCDALSAPVA
110 120 130 140 150
DWNDVSTTPS GSDKYGPYWV IPLNKESGCI NVIVRDGTDK LIDSDLRVAF
160 170 180 190 200
GDFTDRTVSV IAGNSAVYDS RADAFRAAFG VALAEAHWVD KNTLLWPGGQ
210 220 230 240 250
DKPIVRLYYS HSSKVAADGE GKFTDRYLKL TPTTVSQQVS MRFPHLSSYA
260 270 280 290 300
AFKLPDNANV DELLQGETVA IAAAEDGILI SATQVQTAGV LDDAYAEAAE
310 320 330 340 350
ALSYGAQLAD GGVTFRVWAP TAQQVDVVVY SADKKVIGSH PMTRDSASGA
360 370 380 390 400
WSWQGGSDLK GAFYRYAMTV YHPQSRKVEQ YEVTDPYAHS LSTNSEYSQV
410 420 430 440 450
VDLNDSALKP DGWDNLTMPH AQKTKADLAK MTIHESHIRD LSAWDQTVPA
460 470 480 490 500
ELRGKYLALT AGDSNMVQHL KTLSASGVTH VELLPVFDLA TVNEFSDKVA
510 520 530 540 550
DIQQPFSRLC EVNSAVKSSE FAGYCDSGST VEEVLNQLKQ SDSQDNPQVQ
560 570 580 590 600
ALNTLVAQTD SYNWGYDPFH YTVPEGSYAT DPEGTTRIKE FRTMIQAIKQ
610 620 630 640 650
DLGMNVIMDV VYNHTNAAGP TDRTSVLDKI VPWYYQRLNE TTGSVESATC
660 670 680 690 700
CSDSAPEHRM FAKLIADSLA VWTTDYKIDG FRFDLMGYHP KAQILSAWER
710 720 730 740 750
IKALNPDIYF FGEGWDSNQS DRFEIASQIN LKGTGIGTFS DRLRDSVRGG
760 770 780 790 800
GPFDSGDALR QNQGIGSGAG VLPNELASLS DDQVRHLADL TRLGMAGNLA
810 820 830 840 850
DFVMIDKDGA AKKGSEIDYN GAPGGYAADP TEVVNYVSKH DNQTLWDMIS
860 870 880 890 900
YKASQEADLA TRVRMQAVSL ATVMLGQGIA FDQQGSELLR SKSFTRDSYD
910 920 930 940 950
SGDWFNRVDY SLQDNNYNVG MPRISDDGSN YEVITRVKEM VATPGEAELK
960 970 980 990 1000
QMTAFYQELT ELRKSSPLFT LGDGSAVMKR VDFRNTGSDQ QAGLLVMTVD
1010 1020 1030 1040 1050
DGMKAGASLD SRLDGLVVAI NAAPESRTLN EFAGETLQLS AIQQTAGENS
1060 1070 1080 1090
LANGVQIAAD GTVTLPAWSV AVLELPQGEA QGAGLPVSSK
Length:1,090
Mass (Da):118,098
Last modified:April 1, 1990 - v2
Checksum:i240AE7DFB3FF1BD6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61R → C in AAA25087 (PubMed:3902792).Curated
Sequence conflicti10 – 101V → F in AAA25087 (PubMed:3902792).Curated
Sequence conflicti15 – 151V → I in AAA25087 (PubMed:3902792).Curated
Sequence conflicti23 – 231G → S in AAA25087 (PubMed:3902792).Curated
Sequence conflicti31 – 311N → S in AAA25087 (PubMed:3902792).Curated
Sequence conflicti34 – 341T → N in AAA25087 (PubMed:3902792).Curated
Sequence conflicti36 – 361D → DGNP in AAA25087 (PubMed:3902792).Curated
Sequence conflicti55 – 584TAVE → MATA in AAA25087 (PubMed:3902792).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52181 Genomic DNA. Translation: CAA36431.1.
M12503 Genomic DNA. Translation: AAA25087.2.
M29097 Genomic DNA. Translation: AAA61976.1.
PIRiS11823.
S38801.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52181 Genomic DNA. Translation: CAA36431.1.
M12503 Genomic DNA. Translation: AAA25087.2.
M29097 Genomic DNA. Translation: AAA61976.1.
PIRiS11823.
S38801.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YOCX-ray2.88A/B21-1089[»]
ProteinModelPortaliP07206.
SMRiP07206. Positions 173-1090.
ModBaseiSearch...
MobiDBiSearch...

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...

Miscellaneous databases

EvolutionaryTraceiP07206.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.20.20.80. 4 hits.
InterProiIPR013784. Carb-bd-like_fold.
IPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR004193. Glyco_hydro_13_N.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR005323. PUD.
IPR011839. Pullul_strch.
IPR024561. Pullul_strch_C.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 5 hits.
PfamiPF02922. CBM_48. 1 hit.
PF11852. DUF3372. 1 hit.
PF03714. PUD. 1 hit.
[Graphical view]
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF49452. SSF49452. 1 hit.
SSF51445. SSF51445. 1 hit.
SSF81296. SSF81296. 2 hits.
TIGRFAMsiTIGR02103. pullul_strch. 1 hit.
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Molecular characterization of pulA and its product, pullulanase, a secreted enzyme of Klebsiella pneumoniae UNF5023."
    Kornacker M.G., Pugsley A.P.
    Mol. Microbiol. 4:73-85(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: UNF 5023.
  2. "Structure of two divergent promoters located in front of the gene encoding pullulanase in Klebsiella pneumoniae and positively regulated by the malT product."
    Chapon C., Raibaud O.
    J. Bacteriol. 164:639-645(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-62.
  3. "Klebsiella pneumoniae pulS gene encodes an outer membrane lipoprotein required for pullulanase secretion."
    D'Enfert C., Pugsley A.P.
    J. Bacteriol. 171:3673-3679(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 944-1090.

Entry informationi

Entry nameiPULA_KLEPN
AccessioniPrimary (citable) accession number: P07206
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1990
Last modified: July 6, 2016
This is version 126 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

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.