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UniProtKB/Swiss-Prot entry P21332

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name O16G_BACCE
Primary accession number P21332
Secondary accession numbers None
Integrated into Swiss-Prot on May 1, 1991
Sequence was last modified on May 1, 1991 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 62)
Name and origin of the protein
Protein name Oligo-1,6-glucosidase
Synonyms EC 3.2.1.10
Oligosaccharide alpha-1,6-glucosidase
Sucrase-isomaltase
Isomaltase
Dextrin 6-alpha-D-glucanohydrolase
Gene name
Name: malL
From
Bacillus cereus [TaxID: 1396] 
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus; Bacillus cereus group.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-10.
STRAIN=ATCC 7064 / NRS 201;
PubMed=2120057 [NCBI, ExPASy, EBI, Israel, Japan]
Watanabe K., Kitamura K., Iha H., Suzuki Y.;
"Primary structure of the oligo-1,6-glucosidase of Bacillus cereus ATCC7064 deduced from the nucleotide sequence of the cloned gene.";
Eur. J. Biochem. 192:609-620(1990).
[2]
 X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
STRAIN=ATCC 7064 / NRS 201;
PubMed=8370659 [NCBI, ExPASy, EBI, Israel, Japan]
Kizaki H., Hata Y., Watanabe K., Katsube Y., Suzuki Y.;
"Polypeptide folding of Bacillus cereus ATCC7064 oligo-1,6-glucosidase revealed by 3.0-A resolution X-ray analysis.";
J. Biochem. 113:646-649(1993).
[3]
 X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
STRAIN=ATCC 7064 / NRS 201;
DOI=10.1006/jmbi.1997.1018; PubMed=9193006 [NCBI, ExPASy, EBI, Israel, Japan]
Watanabe K., Hata Y., Kizaki H., Katsube Y., Suzuki Y.;
"The refined crystal structure of Bacillus cereus oligo-1,6-glucosidase at 2.0-A resolution: structural characterization of proline-substitution sites for protein thermostabilization.";
J. Mol. Biol. 269:142-153(1997).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X53507; CAA37583.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S13579; S13579.
3D structure databases
PDB
1UOK; X-ray; 2.00 A; A=1-558.[ExPASy / RCSB / EBI]
PDBsum 1UOK; -.
ModBase P21332.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0043169; Molecular function: cation binding (inferred from electronic annotation from InterPro).
GO:0004574; Molecular function: oligo-1,6-glucosidase activity (inferred from electronic annotation from EC).
GO:0005975; Biological process: carbohydrate metabolic process (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR013780; Glyco_hydro_13_b.
IPR006047; Glyco_hydro_13_cat.
IPR006589; Glyco_hydro_13_sub_cat.
IPR013781; Glyco_hydro_sub_cat.
Graphical view of domain structure.
Gene3D G3DSA:2.60.40.1180; Glyco_hydro_13_b; 1.
G3DSA:3.20.20.80; Glyco_hydro_cat; 1.
Pfam PF00128; Alpha-amylase; 1.
Pfam graphical view of domain structure.
SMART SM00642; Aamy; 1.
SMART graphical view of domain structure.
ProtoNet P21332.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cytoplasm; Direct protein sequencing; Glycosidase; Hydrolase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   558  558     Oligo-1,6-glucosidase. PRO_0000054313
ACT_SITE   199   199        Nucleophile. 
ACT_SITE   255   255        Proton donor. 
ACT_SITE   329   329         
HELIX   5     8  4      
STRAND   11    14  4      
HELIX   16    18  3      
STRAND   22    27  6      
HELIX   30    34  5      
HELIX   37    43  7      
STRAND   47    50  4      
TURN   59    62  4      
STRAND   66    71  6      
HELIX   73    75  3      
HELIX   78    90  13      
STRAND   94    99  6      
HELIX   109   114  6      
HELIX   123   125  3      
STRAND   132   135  4      
STRAND   145   152  8      
TURN   153   156  4      
STRAND   157   160  4      
HELIX   175   190  16      
STRAND   195   198  4      
HELIX   201   203  3      
HELIX   224   226  3      
TURN   227   229  3      
HELIX   233   243  11      
HELIX   245   247  3      
STRAND   251   255  5      
HELIX   261   268  8      
HELIX   270   272  3      
HELIX   282   284  3      
STRAND   292   296  5      
HELIX   301   314  14      
STRAND   316   319  4      
HELIX   333   336  4      
HELIX   344   356  13      
STRAND   358   365  8      
HELIX   368   370  3      
HELIX   380   382  3      
HELIX   386   397  12      
HELIX   403   413  11      
HELIX   415   418  4      
TURN   428   431  4      
HELIX   443   446  4      
HELIX   450   455  6      
HELIX   460   473  14      
HELIX   475   479  5      
STRAND   481   486  6      
STRAND   490   499  10      
STRAND   502   509  8      
STRAND   511   513  3      
STRAND   515   518  4      
STRAND   528   535  8      
STRAND   543   547  5      
STRAND   552   557  6      
Sequence information
Length: 558 AA [This is the length of the unprocessed precursor] Molecular weight: 66013 Da [This is the MW of the unprocessed precursor] CRC64: 502336D7A77C7182 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MEKQWWKESV VYQIYPRSFM DSNGDGIGDL RGIISKLDYL KELGIDVIWL SPVYESPNDD 

        70         80         90        100        110        120 
NGYDISDYCK IMNEFGTMED WDELLHEMHE RNMKLMMDLV VNHTSDEHNW FIESRKSKDN 

       130        140        150        160        170        180 
KYRDYYIWRP GKEGKEPNNW GAAFSGSAWQ YDEMTDEYYL HLFSKKQPDL NWDNEKVRQD 

       190        200        210        220        230        240 
VYEMMKFWLE KGIDGFRMDV INFISKEEGL PTVETEEEGY VSGHKHFMNG PNIHKYLHEM 

       250        260        270        280        290        300 
NEEVLSHYDI MTVGEMPGVT TEEAKLYTGE ERKELQMVFQ FEHMDLDSGE GGKWDVKPCS 

       310        320        330        340        350        360 
LLTLKENLTK WQKALEHTGW NSLYWNNHDQ PRVVSRFGND GMYRIESAKM LATVLHMMKG 

       370        380        390        400        410        420 
TPYIYQGEEI GMTNVRFESI DEYRDIETLN MYKEKVMERG EDIEKVMQSI YIKGRDNART 

       430        440        450        460        470        480 
PMQWDDQNHA GFTTGEPWIT VNPNYKEINV KQAIQNKDSI FYYYKKLIEL RKNNEIVVYG 

       490        500        510        520        530        540 
SYDLILENNP SIFAYVRTYG VEKLLVIANF TAEECIFELP EDISYSEVEL LIHNYDVENG 

       550 
PIENITLRPY EAMVFKLK
P21332 in FASTA format

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