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P07206 (PULA_KLEPN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pullulanase
EC=3.2.1.41
Alternative name(s):
Alpha-dextrin endo-1,6-alpha-glucosidase
Pullulan 6-glucanohydrolase
Gene names
Name:pulA
OrganismKlebsiella pneumoniae
Taxonomic identifier573 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Klebsiella

Protein attributes

Sequence length1090 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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.

Subunit structure

Homotrimer.

Subcellular location

Cell membrane; Lipid-anchor Probable.

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMLipoprotein
Palmitate
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentplasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncarbohydrate binding

Inferred from electronic annotation. Source: InterPro

cation binding

Inferred from electronic annotation. Source: InterPro

pullulanase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 By similarity
Chain20 – 10901071Pullulanase
PRO_0000001427

Sites

Active site6841Nucleophile By similarity
Active site7131Proton donor By similarity
Site8411Transition state stabilizer By similarity

Amino acid modifications

Lipidation201N-palmitoyl cysteine By similarity
Lipidation201S-diacylglycerol cysteine By similarity

Experimental info

Sequence conflict61R → C in AAA25087. Ref.2
Sequence conflict101V → F in AAA25087. Ref.2
Sequence conflict151V → I in AAA25087. Ref.2
Sequence conflict231G → S in AAA25087. Ref.2
Sequence conflict311N → S in AAA25087. Ref.2
Sequence conflict341T → N in AAA25087. Ref.2
Sequence conflict361D → DGNP in AAA25087. Ref.2
Sequence conflict55 – 584TAVE → MATA in AAA25087. Ref.2

Secondary structure

1 ............................................................................................................................................................................................................................ 1090
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07206 [UniParc].

Last modified April 1, 1990. Version 2.
Checksum: 240AE7DFB3FF1BD6

FASTA1,090118,098
        10         20         30         40         50         60 
MLRYTRNALV LGSLVLLSGC DNGSSSSSSG NPDTPDNQDV VVRLPDVAVP GEAVTAVENQ 

        70         80         90        100        110        120 
AVIHLVDIAG ITSSSAADYS SKNLYLWNNE TCDALSAPVA DWNDVSTTPS GSDKYGPYWV 

       130        140        150        160        170        180 
IPLNKESGCI NVIVRDGTDK LIDSDLRVAF GDFTDRTVSV IAGNSAVYDS RADAFRAAFG 

       190        200        210        220        230        240 
VALAEAHWVD KNTLLWPGGQ DKPIVRLYYS HSSKVAADGE GKFTDRYLKL TPTTVSQQVS 

       250        260        270        280        290        300 
MRFPHLSSYA AFKLPDNANV DELLQGETVA IAAAEDGILI SATQVQTAGV LDDAYAEAAE 

       310        320        330        340        350        360 
ALSYGAQLAD GGVTFRVWAP TAQQVDVVVY SADKKVIGSH PMTRDSASGA WSWQGGSDLK 

       370        380        390        400        410        420 
GAFYRYAMTV YHPQSRKVEQ YEVTDPYAHS LSTNSEYSQV VDLNDSALKP DGWDNLTMPH 

       430        440        450        460        470        480 
AQKTKADLAK MTIHESHIRD LSAWDQTVPA ELRGKYLALT AGDSNMVQHL KTLSASGVTH 

       490        500        510        520        530        540 
VELLPVFDLA TVNEFSDKVA DIQQPFSRLC EVNSAVKSSE FAGYCDSGST VEEVLNQLKQ 

       550        560        570        580        590        600 
SDSQDNPQVQ ALNTLVAQTD SYNWGYDPFH YTVPEGSYAT DPEGTTRIKE FRTMIQAIKQ 

       610        620        630        640        650        660 
DLGMNVIMDV VYNHTNAAGP TDRTSVLDKI VPWYYQRLNE TTGSVESATC CSDSAPEHRM 

       670        680        690        700        710        720 
FAKLIADSLA VWTTDYKIDG FRFDLMGYHP KAQILSAWER IKALNPDIYF FGEGWDSNQS 

       730        740        750        760        770        780 
DRFEIASQIN LKGTGIGTFS DRLRDSVRGG GPFDSGDALR QNQGIGSGAG VLPNELASLS 

       790        800        810        820        830        840 
DDQVRHLADL TRLGMAGNLA DFVMIDKDGA AKKGSEIDYN GAPGGYAADP TEVVNYVSKH 

       850        860        870        880        890        900 
DNQTLWDMIS YKASQEADLA TRVRMQAVSL ATVMLGQGIA FDQQGSELLR SKSFTRDSYD 

       910        920        930        940        950        960 
SGDWFNRVDY SLQDNNYNVG MPRISDDGSN YEVITRVKEM VATPGEAELK QMTAFYQELT 

       970        980        990       1000       1010       1020 
ELRKSSPLFT LGDGSAVMKR VDFRNTGSDQ QAGLLVMTVD DGMKAGASLD SRLDGLVVAI 

      1030       1040       1050       1060       1070       1080 
NAAPESRTLN EFAGETLQLS AIQQTAGENS LANGVQIAAD GTVTLPAWSV AVLELPQGEA 

      1090 
QGAGLPVSSK

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References

[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X52181 Genomic DNA. Translation: CAA36431.1.
M12503 Genomic DNA. Translation: AAA25087.2.
M29097 Genomic DNA. Translation: AAA61976.1.
PIRS11823.
S38801.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2FGZX-ray1.75A20-1090[»]
2FH6X-ray1.80A20-1090[»]
2FH8X-ray1.90A30-1090[»]
2FHBX-ray1.80A20-1090[»]
2FHCX-ray1.85A20-1090[»]
2FHFX-ray1.65A20-1090[»]
ProteinModelPortalP07206.
SMRP07206. Positions 173-1090.
ModBaseSearch...

Protein family/group databases

CAZyCBM41. Carbohydrate-Binding Module Family 41.
CBM48. Carbohydrate-Binding Module Family 48.
GH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.60.40.10. 1 hit.
3.20.20.80. 4 hits.
InterProIPR015902. 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]
PANTHERPTHR10357. PTHR10357. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
PF02922. CBM_48. 1 hit.
PF11852. DUF3372. 1 hit.
PF03714. PUD. 1 hit.
[Graphical view]
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
SSF81296. Ig_E-set. 1 hit.
TIGRFAMsTIGR02103. pullul_strch. 1 hit.
PROSITEPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP07206.

Entry information

Entry namePULA_KLEPN
AccessionPrimary (citable) accession number: P07206
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1990
Last modified: April 3, 2013
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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