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Reviewed, UniProtKB/Swiss-Prot P36905 (APU_THESA)

Last modified June 16, 2009. Version 71. 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

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Names and origin

Protein namesRecommended name:
    Amylopullulanase
Alternative name(s):
    Alpha-amylase/pullulanase
Including the following 2 domains:
    1- Recommended name:
            Alpha-amylase
              EC=3.2.1.1
        Alternative name(s):
            1,4-alpha-D-glucan glucanohydrolase
    2- Recommended name:
            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: apu
OrganismThermoanaerobacter saccharolyticum
Taxonomic identifier28896 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Thermoanaerobacterales › Thermoanaerobacterales Family III. Incertae Sedis › Thermoanaerobacterium

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Protein attributes

Sequence length1279 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology.

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General annotation (Comments)

Catalytic activity

Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in oligosaccharides and polysaccharides.

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.

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

Contains 2 fibronectin type-III domains.

Sequence caution

The sequence AAA19800.1 differs from that shown. Reason: Miscellaneous discrepancy. Contaminating sequence. Vector contamination at the C-terminus, a segment of 9 residues, which seems to originate from a puc-type vector.

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Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionalpha-amylase activity

Inferred from electronic annotation. Source: EC

calcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

pullulanase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3535 Potential
Chain36 – 12791244Amylopullulanase
PRO_0000001324

Regions

Domain931 – 101686Fibronectin type-III 1
Domain1155 – 124591Fibronectin type-III 2

Sites

Active site6291Nucleophile By similarity
Active site6581Proton donor By similarity
Active site7351 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 binding4541Calcium By similarity

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Sequences

Sequence LengthMass (Da)Tools
P36905-1 [UniParc].

Last modified February 1, 1995. Version 2.
Checksum: 095CCBCA391624DD

FASTA1,279142,431
        10         20         30         40         50         60 
MYKKLFTKKF ISFVMSLLLV LTAAFSSMPF HNVYAADNAS VVANIVGDFQ DQLGDSNWNI 

        70         80         90        100        110        120 
DSNITIMQYV GNGLYEFTTP TQLKAGSYQY KVALNHSWNG GGVPSQGNLT LNLTNDSYVT 

       130        140        150        160        170        180 
FWFDYNTQSV TDSTKYTPIS NDKLPRLVGT IQSAIGAGKD WDPGTSTAIM IDDNFDNVYS 

       190        200        210        220        230        240 
YTAHIPKGDY QYKVTLGNTW AENYGANGVQ DGSNIQLSVA NDADITFFYD ANTHNIWTNY 

       250        260        270        280        290        300 
SPTLTGLDNN IYYDDLKHDT HDPFFRNPFG AIKVGQTVTL RIQAKNHDLE SARISYWDDI 

       310        320        330        340        350        360 
NKTRTELPMT RIGESPDGNY EYWEIKLSFD HPTRIWYYFI LKDGTKTAYY GDNDDQLGGL 

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

       430        440        450        460        470        480 
FHNDWNDLPD NPNNAGTPGY TGDGIWSNDF FGGDLKGIDD KLDYLKGLGV SVIYLNPIFE 

       490        500        510        520        530        540 
SPSNHKYDTA DYTKIDEMFG TTQDFEKLMS DAHAKGINII LDGVFNHTSD DSIYFNRYGK 

       550        560        570        580        590        600 
YPDLGAYQDW KDGNQSLSPY GDWYTINSDG TYECWWGYDS LPVIKSLNGS EYNVTSWANF 

       610        620        630        640        650        660 
IINDKNAISK YWLNPDENLN DGADGWRLDV ENEVAHDFWT HFRDAINTVK PEAPMIAENW 

       670        680        690        700        710        720 
GDASLDLLGD SFNSVMNYQF RNDIIDFLIG QSFDDGNGQH NPIDAAKLDQ RLMSIYERYP 

       730        740        750        760        770        780 
LPAFYSTMNL LGSHDTMSIL TVFGYNSADP NENSDAAKRL AEQKLKLATI LQMGYPGMAD 

       790        800        810        820        830        840 
IYYGDEAGVS GGKDPDDRRT FPWGNEDTAL QDFFKNVSSI RNNNQVLKTG DLETLYAQND 

       850        860        870        880        890        900 
VYAIGRRIIN GKDAFGNSYP DSAAIVAINR SNSDQQITID TTKFLRDGVA FKDLINGDKS 

       910        920        930        940        950        960 
YTINGGQITI NIPAMSGVML ISDDGQDLTA PQVPSNVVAT SGNGKVDLSW SQSDGATGYN 

       970        980        990       1000       1010       1020 
IYRSSVEGGL YEKIASNVTG TTFEDTNVTN GLKYVYAISA VDELGNESEM SIDTVAYPAY 

      1030       1040       1050       1060       1070       1080 
PIGWVGNLTQ VVDNHVISVS NPTEDIYAEV WADGLTNSTG QGPNMIAQLG YKYVGGTVND 

      1090       1100       1110       1120       1130       1140 
SVYGSVYNSV YGVDDSDFTW VNAQYVGDIG NNDQYKASLH LINRSMGYLM RFSDNQGQSW 

      1150       1160       1170       1180       1190       1200 
TTTDTLSFYV VPSDDLIKPT APILNQPGVE SSRVSLTWSP STDNVGIYNY EIYRSDGGTF 

      1210       1220       1230       1240       1250       1260 
NKIATVSNEV YNYVDTSVIN GTTYSYKVVA ADPSFNRTES NVVTIKPDVV PIKVTFNVTV 

      1270 
PDYTPNSVNL AGTFPNATW

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References

[1]"Cloning and sequencing of the Thermoanaerobacterium saccharolyticum B6A-RI apu gene and purification and characterization of the amylopullulanase from Escherichia coli."
Ramesh M.V., Podkovyrov S.M., Lowe S.E., Zeikus J.G.
Appl. Environ. Microbiol. 60:94-101(1994) [PubMed: 8117096] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: B6A-RI.
[2]Robison K.
Unpublished observations (NOV-1994)
Cited for: IDENTIFICATION OF PROBABLE VECTOR CONTAMINATION.

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Cross-references

Sequence databases

L07762 Unassigned DNA. Translation: AAA19800.1. Sequence problems.

3D structure databases

HSSPHSSP built from PDB template 1JI1 based on UniProtKB Q60053.
ModBaseSearch...

Protein family/group databases

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

Family and domain databases

InterProIPR006048. A-amylase_b_C.
IPR008957. Fibronectin_typ-III-like_fold.
IPR003961. FN_III.
IPR006047. Glyco_hydro_13_cat.
IPR004185. Glyco_hydro_13_lg-like.
IPR006589. Glyco_hydro_13_sub_cat.
IPR013781. Glyco_hydro_sg_catalytic.
IPR013783. Ig-like_fold.
[Graphical view]
Gene3DG3DSA:2.60.40.30. FN_III-like. 2 hits.
G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
G3DSA:2.60.40.10. Ig-like_fold. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
PF02903. Alpha-amylase_N. 1 hit.
PF00041. fn3. 2 hits.
[Graphical view]
SMARTSM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
SM00060. FN3. 2 hits.
[Graphical view]
PROSITEPS50853. FN3. 2 hits.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameAPU_THESA
AccessionPrimary (citable) accession number: P36905
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: February 1, 1995
Last modified: June 16, 2009
This is version 71 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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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