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P38536 (APU_THETU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Amylopullulanase
Alternative name(s):
Alpha-amylase/pullulanase
Pullulanase type II

Including the following 2 domains:

  1. Alpha-amylase
    EC=3.2.1.1
    Alternative name(s):
    1,4-alpha-D-glucan glucanohydrolase
  2. Pullulanase
    EC=3.2.1.41
    Alternative name(s):
    1,4-alpha-D-glucan glucanohydrolase
    Alpha-dextrin endo-1,6-alpha-glucosidase
Gene names
Name:amyB
OrganismThermoanaerobacter thermosulfurogenes (Clostridium thermosulfurogenes)
Taxonomic identifier33950 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Thermoanaerobacterales › Thermoanaerobacterales Family III. Incertae Sedis › Thermoanaerobacterium

Protein attributes

Sequence length1861 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.

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.

Cofactor

Binds 1 calcium ion per subunit By similarity.

Subcellular location

Secreted › cell wall. Note: It C-terminus may serve as an S-layer anchor.

Post-translational modification

Glycosylated.

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

Contains 1 CBM20 (carbohydrate binding type-20) domain.

Contains 2 fibronectin type-III domains.

Contains 3 SLH (S-layer homology) domains.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   Cellular componentCell wall
Secreted
   DomainRepeat
Signal
   LigandCalcium
Metal-binding
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcell wall

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular region

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionalpha-amylase activity

Inferred from electronic annotation. Source: EC

carbohydrate binding

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

pullulanase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3535 Potential
Chain36 – 18611826Amylopullulanase
PRO_0000001325

Regions

Domain930 – 101586Fibronectin type-III 1
Domain1159 – 124587Fibronectin type-III 2
Domain1246 – 1354109CBM20
Domain1677 – 174064SLH 1
Domain1741 – 179959SLH 2
Domain1802 – 186160SLH 3

Sites

Active site6281Nucleophile By similarity
Active site6571Proton donor By similarity
Metal binding4011Calcium By similarity
Metal binding4031Calcium; via carbonyl oxygen By similarity
Metal binding4061Calcium By similarity
Metal binding4071Calcium By similarity
Metal binding4521Calcium; via carbonyl oxygen By similarity
Metal binding4531Calcium By similarity
Binding site5261Substrate By similarity
Binding site6261Substrate By similarity
Binding site7971Substrate By similarity
Site7341Transition state stabilizer By similarity

Experimental info

Sequence conflict17341D → E in AAB00841. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P38536 [UniParc].

Last modified November 1, 1995. Version 2.
Checksum: 06C23070E453B574

FASTA1,861206,104
        10         20         30         40         50         60 
MNKKLFTNRF ISFNMSLLLV LTAVFSSIPL HSVHAADNAS VVANIVGEFQ DQLGDSNWNI 

        70         80         90        100        110        120 
DSNITIMQYM GNGLYEFTTP TQLKAGSYQY KVALNHSWDG GGVPSQGNLT LNLANDSYVT 

       130        140        150        160        170        180 
FWFDYNTQSV TDSTKYTPIA NDKLPRLVGT IQSAIGAGND WKPETSTAIM TDDNFDNVYS 

       190        200        210        220        230        240 
YTAHVPKGDY QYKVTLGNTW DENYGANGVK DGSNIQINVT NDADITFYYD ANTHNIWTNY 

       250        260        270        280        290        300 
SPILTGLDNN IYYDDLKHDT HDSFFRNPFG AVKVDQTVTL RIQAKNHDLE SARISYWDDI 

       310        320        330        340        350        360 
NKIRIELPMT RIGESPDGNF EYWEIKLSFD HPTRIWYYFI LKDGTKTAYY GDNDDQLGGV 

       370        380        390        400        410        420 
GKATDTVNKD FELTVYDKNF DTPDWMKGAV MYQIFPDRFY NGDTSNDHAK TLSRGNDPIE 

       430        440        450        460        470        480 
FHNNWNDLPD NPNNAGTPGY TGDGIWSNDF FGDLKGIDDK LDYLKGLGVS VIYLNPIFES 

       490        500        510        520        530        540 
PSNHKYDTAD YTKIDEMFGT TQDFEKLMSD AHAKGIKIIL DGVFNHTSDD SIYFNRYGKY 

       550        560        570        580        590        600 
PGLGAYQAWK EGNQSLSPYG DWYTINSDGT YECWWGYDSL PVIKSLNGSE YNVTSWANFI 

       610        620        630        640        650        660 
INDENAISKY WLNPDGNLND GADGWRLDVE NEVAHDFWTH FRNAINTVKF EAPMIAENWG 

       670        680        690        700        710        720 
DASLDLLGDS FNSVMNYQFR NDIIDFLIGQ SFDDGNGQHN PIDAAKLDQR LMSIYERYPL 

       730        740        750        760        770        780 
PAFYSTMNLL GSHDTMRILT VFGYNSADPN ENSDAAKQLA EQKLKLATIL QMGYPGMADI 

       790        800        810        820        830        840 
YYGDEAGVSG GKDPDDRRTF PWGNEDTTLQ DFFKNISSIR NNNQVLKTGD LETLYAQNDV 

       850        860        870        880        890        900 
YAIGRRIING KDAFGTSYPD SAAIVAINRS KSDKQIAIDT TKFLRDGVTF KDLINNNVSY 

       910        920        930        940        950        960 
SISNGQIVID VPAMSGVMLI SDDGQDLTAP QAPSNVVVTS GNGKVDLSWL QSDGATGYNI 

       970        980        990       1000       1010       1020 
YRSSVEGGLY EKIASNVTET TFEDANVTNG LKYVYAISAI DELGNESGIS NDAVAYPAYP 

      1030       1040       1050       1060       1070       1080 
IGWVGNLTQV SDNHIIGVDK PTEDIYAEVW ADGLTNSTGQ GPNMIAQLGY KYVSGTVYDS 

      1090       1100       1110       1120       1130       1140 
VYGSVYNSVY GVDDSGFTWV NAQYVGDIGN NDQYKASFTP DKIGQWEYLM RFSDNQGQDW 

      1150       1160       1170       1180       1190       1200 
ITTSTLSFYV VPSDDLIKPT APYLNQPGTE SSRVSLTWNP STDNVGIYDY EIYRSDGGTF 

      1210       1220       1230       1240       1250       1260 
NKIATVSNEV YNYIDTSVIN GVTYNYKVVA VDLSFNRTES NVVTIKPDVV PIKVIFNVTV 

      1270       1280       1290       1300       1310       1320 
PDYTPDAVNL AGTFPNATWD PSAQQMTKID NNTYSITLTL DEGTQIEYKY ARGSWDKVEK 

      1330       1340       1350       1360       1370       1380 
DEYGNEFASN RKVTIVNQGN NEMTINDTVY RWRDIPIFIY SPSSNMTVDS NISTMEVKGN 

      1390       1400       1410       1420       1430       1440 
TYKGAKVTIN GDSFVQDKNG VFTKDVSLNY GVNKIKIHVE PNDGSVYGND QGRITELTKD 

      1450       1460       1470       1480       1490       1500 
IEIDVIRQEN NSGSGTGNNN TSTSGSNSSS TGSGSTGSTS ITSNISNTSN TSNTIGVITK 

      1510       1520       1530       1540       1550       1560 
NGNVITLTLD AGKAKDLIVN SKDKKVVFDI TTIGEGQQKV VQISKDILDT SAANGKDIVI 

      1570       1580       1590       1600       1610       1620 
KSDNASIALT KDALNQNQIQ NGVNVSIKDN GKPNVTNYVS LSNVVDITIS GISGNVTLAK 

      1630       1640       1650       1660       1670       1680 
PVEVTLNISK ANDPRKVAVY YYNPTTNQWE YVGGKVDASS GTITFNATHF SQYAAFEYDK 

      1690       1700       1710       1720       1730       1740 
TFNDIKDNWA KDVIEVLASR HIVEGMTDTQ YEPNKTVTRA EFTAMILRLL NIKDETYSGE 

      1750       1760       1770       1780       1790       1800 
FSDVKSGDWY ANAIEAAYKA GIIEGDGKNA RPNDSITREE MTAIAMRAYE MLTQYKEENI 

      1810       1820       1830       1840       1850       1860 
GATTFSDDKS ISDWARNVVA NAAKLGIVNG EPNNVFAPKG NATRAEAAAI IYGLLEKSGN 


I

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References

[1]"Pullulanase of Thermoanaerobacterium thermosulfurigenes EM1 (Clostridium thermosulfurogenes): molecular analysis of the gene, composite structure of the enzyme, and a common model for its attachment to the cell surface."
Matuschek M., Burchhardt G., Sahm K., Bahl H.
J. Bacteriol. 176:3295-3302(1994) [PubMed: 8195085] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: DSM 3896 / EM1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M57692 Genomic DNA. Translation: AAB00841.1.

3D structure databases

ProteinModelPortalP38536.
ModBaseSearch...

Protein family/group databases

CAZyCBM20. Carbohydrate-Binding Module Family 20.
CBM34. Carbohydrate-Binding Module Family 34.
GH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR006048. A-amylase_b_C.
IPR015902. Alpha_amylase.
IPR013784. Carb-bd-like_fold.
IPR002044. CBM_fam20.
IPR003961. Fibronectin_type3.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR004185. Glyco_hydro_13_lg-like_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR001119. S-layer_homology_dom.
[Graphical view]
Gene3DG3DSA:2.60.40.1180. Glyco_hydro_13_b. 1 hit.
G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
G3DSA:2.60.40.10. Ig-like_fold. 4 hits.
PANTHERPTHR10357. Alpha_amylase. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
PF02903. Alpha-amylase_N. 1 hit.
PF00395. SLH. 3 hits.
[Graphical view]
SMARTSM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
SM01065. CBM_2. 1 hit.
SM00060. FN3. 2 hits.
[Graphical view]
SUPFAMSSF49452. CBD_4. 1 hit.
SSF49265. FN_III-like. 2 hits.
SSF51445. Glyco_hydro_cat. 1 hit.
SSF81296. Ig_E-set. 1 hit.
PROSITEPS51166. CBM20. 1 hit.
PS50853. FN3. 2 hits.
PS51272. SLH. 3 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAPU_THETU
AccessionPrimary (citable) accession number: P38536
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: November 1, 1995
Last modified: January 25, 2012
This is version 91 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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents