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Reviewed, UniProtKB/Swiss-Prot P07811 (PULA_KLEAE)

Last modified June 16, 2009. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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 aerogenes
Taxonomic identifier28451 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeKlebsiella

Protein attributes

Sequence length1096 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. Ref.2

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
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
Chain20 – 10961077Pullulanase
PRO_0000001426

Sites

Active site6941Nucleophile By similarity
Active site7231Proton donor By similarity
Active site8511 By similarity

Amino acid modifications

Lipidation201N-palmitoyl cysteine
Lipidation201S-diacylglycerol cysteine

Sequences

Sequence LengthMass (Da)Tools
P07811-1 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: FE7D9167CDACFD79

FASTA1,096119,336
        10         20         30         40         50         60 
MLRYTCHALF LGSLVLLSGC DNSSSSSTSG SPGSPGNPGN PGTPGTPDPQ DVVVRLPDVA 

        70         80         90        100        110        120 
VPGEAVQASA RQAVIHLVDI AGITSSTPAD YATKNLYLWN NETCDALSAP VADWNDVSTT 

       130        140        150        160        170        180 
PTGSDKYGPY WVIPLTKESG SINVIVRDGT NKLIDSGRVS FSDFTDRTVS VIAGNSAVYD 

       190        200        210        220        230        240 
SRADAFRAAF GVALADAHWV DKTTLLWPGG ENKPIVRLYY SHSSKVAADS NGEFSDKYVK 

       250        260        270        280        290        300 
LTPTTVNQQV SMRFPHLASY PAFKLPDDVN VDELLQGDDG GIAESDGILS LSHPGADRRR 

       310        320        330        340        350        360 
AGRYLCRRAE ALSYGAQLTD SGVTFRVWAP TAQQVELVIY SADKKVIASH PMTRDSASGA 

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

       430        440        450        460        470        480 
EGWDGLTMPH AQKTKADLAK MTIHESHIRD LSAWDQTVPA ELRGKYLALT AQESNMVQHL 

       490        500        510        520        530        540 
KQLSASGVTH IELLPVFDLA TVNEFSDKVA DIQQPFSRLC EVNSAVKSSE FAGYCDSGST 

       550        560        570        580        590        600 
VEEVLTQLKQ NDSKDNPQVQ ALNTLVAQTD SYNWGYDPFH YTVPEGSYAT DPEGTARIKE 

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

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

       730        740        750        760        770        780 
FGEGWDSNQS DRFEIASQIN LKGTGIGTFS DRLRDAVRGG GPFDSGDALR QNQGVGSGAG 

       790        800        810        820        830        840 
VLPNELTTLS DDQARHLADL TRLGMAGNLA DFVLIDKDGA VKRGSEIDYN GAPGGYAADP 

       850        860        870        880        890        900 
TEVVNYVSKH DNQTLWDMIS YKAAQEADLD TRVRMQAVSL ATVMLGQGIA FDQQGSELLR 

       910        920        930        940        950        960 
SKSFTRDSYD SGDWFNRVDY SLQDNNYNVG MPRSSDDGSN YDIIARVKDA VATPGETELK 

       970        980        990       1000       1010       1020 
QMTAFYQELT ALRKSSPLFT LGDGATVMKR VDFRNTGADQ QTGLLVMTID DGMQAGRQSG 

      1030       1040       1050       1060       1070       1080 
QPCRRHRGGD QRRAGKPDAA GLRRHIAPAE RYSAGGGRPV AGERVQVAAD GSVTLPAWSV 

      1090 
AVLELPQASR RALACR 

« Hide

References

[1]"Entire nucleotide sequence of the pullulanase gene of Klebsiella aerogenes W70."
Katsuragi N., Takizawa N., Murooka Y.
J. Bacteriol. 169:2301-2306(1987) [PubMed: 3155373] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: W70.
[2]"Collagen-like sequences stabilize homotrimers of a bacterial hydrolase."
Charalambous B.M., Keen J.N., McPherson M.J.
EMBO J. 7:2903-2909(1988) [PubMed: 2846288] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-74, SUBUNIT.
Strain: FG9.

Cross-references

Sequence databases

M16187 Genomic DNA. Translation: AAA25124.1. Sequence problems.
PIRA26879.

3D structure databases

HSSPHSSP built from PDB template 1M7X based on UniProtKB P07762.
SMRP07811. Positions 51-1092.
ModBaseSearch...

Protein family/group databases

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

Enzyme and pathway databases

BRENDA3.2.1.41. 366.

Family and domain databases

InterProIPR006047. Glyco_hydro_13_cat.
IPR004193. Glyco_hydro_13_N.
IPR013781. Glyco_hydro_sg_catalytic.
IPR013783. Ig-like_fold.
IPR005323. PUD.
IPR011839. Pullul_strch.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
G3DSA:2.60.40.10. Ig-like_fold. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
PF02922. CBM_48. 1 hit.
PF03714. PUD. 1 hit.
[Graphical view]
TIGRFAMsTIGR02103. pullul_strch. 1 hit.
PROSITEPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePULA_KLEAE
AccessionPrimary (citable) accession number: P07811
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: June 16, 2009
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents