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Reviewed, UniProtKB/Swiss-Prot O33833 (BFRA_THEMA)

Last modified January 19, 2010. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
    Beta-fructosidase
    EC=3.2.1.26
Alternative name(s):
    Sucrase
    Invertase
Gene names
Name: bfrA
Ordered Locus Names: TM_1414
OrganismThermotoga maritima [Complete proteome] [HAMAP]
Taxonomic identifier2336 [NCBI]
Taxonomic lineageBacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga

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Protein attributes

Sequence length432 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Hydrolysis of sucrose, raffinose, inulin and levan. Specific for the fructose moiety and the beta-anomeric configuration of the glycosidic linkages of its substrates. The enzyme released fructose from sucrose and raffinose, and the fructose polymer inulin is hydrolyzed quantitatively in an exo-type fashion.

Catalytic activity

Hydrolysis of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranosides.

Sequence similarities

Belongs to the glycosyl hydrolase 32 family.

Biophysicochemical properties

Temperature dependence:

Optimum temperature is 90-95 degrees Celsius. Highly thermostable.

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Ontologies

Keywords
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionbeta-fructofuranosidase 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

Chain1 – 432432Beta-fructosidase
PRO_0000169881

Regions

Region14 – 174Substrate binding
Region74 – 752Substrate binding
Region137 – 1382Substrate binding
Region188 – 1903Substrate binding

Sites

Active site171
Binding site331Substrate
Binding site411Substrate
Binding site921Substrate
Binding site2081Substrate
Binding site2601Substrate

Experimental info

Mutagenesis1901E → A: Loss of activity. Ref.4
Mutagenesis1901E → D: Reduced activity. Ref.4

Secondary structure

1 ....................................................................... 432
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
O33833-1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 39F61B2E1BC462B9

FASTA43249,841
        10         20         30         40         50         60 
MFKPNYHFFP ITGWMNDPNG LIFWKGKYHM FYQYNPRKPE WGNICWGHAV SDDLVHWRHL 

        70         80         90        100        110        120 
PVALYPDDET HGVFSGSAVE KDGKMFLVYT YYRDPTHNKG EKETQCVAMS ENGLDFVKYD 

       130        140        150        160        170        180 
GNPVISKPPE EGTHAFRDPK VNRSNGEWRM VLGSGKDEKI GRVLLYTSDD LFHWKYEGVI 

       190        200        210        220        230        240 
FEDETTKEIE CPDLVRIGEK DILIYSITST NSVLFSMGEL KEGKLNVEKR GLLDHGTDFY 

       250        260        270        280        290        300 
AAQTFFGTDR VVVIGWLQSW LRTGLYPTKR EGWNGVMSLP RELYVENNEL KVKPVDELLA 

       310        320        330        340        350        360 
LRKRKVFETA KSGTFLLDVK ENSYEIVCEF SGEIELRMGN ESEEVVITKS RDELIVDTTR 

       370        380        390        400        410        420 
SGVSGGEVRK STVEDEATNR IRAFLDSCSV EFFFNDSIAF SFRIHPENVY NILSVKSNQV 

       430 
KLEVFELENI WL

« Hide

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References

« Hide 'large scale' references
[1]"Analysis of the gene for beta-fructosidase (invertase, inulinase) of the hyperthermophilic bacterium Thermotoga maritima, and characterisation of the enzyme expressed in Escherichia coli."
Liebl W., Brem D., Gotschlich A.
Appl. Microbiol. Biotechnol. 50:55-64(1998) [PubMed: 9720201] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[2]"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima."
Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. expand/collapse author list , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.
Nature 399:323-329(1999) [PubMed: 10360571] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[3]"The three-dimensional structure of invertase (beta-fructosidase) from Thermotoga maritima reveals a bimodular arrangement and an evolutionary relationship between retaining and inverting glycosidases."
Alberto F., Bignon C., Sulzenbacher G., Henrissat B., Czjzek M.
J. Biol. Chem. 279:18903-18910(2004) [PubMed: 14973124] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2-432.
[4]"Crystal structure of inactivated Thermotoga maritima invertase in complex with the trisaccharide substrate raffinose."
Alberto F., Jordi E., Henrissat B., Czjzek M.
Biochem. J. 395:457-462(2006) [PubMed: 16411890] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) OF 2-432 IN COMPLEX WITH SUBSTRATES, MUTAGENESIS OF GLU-190.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ001073 Genomic DNA. Translation: CAA04518.1.
AE000512 Genomic DNA. Translation: AAD36485.1.
PIRD72255.
RefSeqNP_229215.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1UYPX-ray1.90A/B/C/D/E/F2-432[»]
1W2TX-ray1.87A/B/C/D/E/F2-432[»]
ModBaseSearch...

Protein family/group databases

CAZyGH32. Glycoside Hydrolase Family 32.

Genome annotation databases

GeneID898062.
GenomeReviewsGene locus TM_1414 in contig AE000512_GR.
KEGGtma:TM1414.
NMPDRfig|243274.1.peg.1399.
TIGRTM_1414.

Phylogenomic databases

HOGENOMHBG693902.
OMAQCLAISE.

Enzyme and pathway databases

BioCycTMAR243274:TM_1414-MONOMER.
BRENDA3.2.1.26. 16699.

Family and domain databases

InterProIPR008985. ConA-like_lec_gl.
IPR001362. Glyco_hydro_32.
IPR018053. Glyco_hydro_32_AS.
IPR013189. Glyco_hydro_32_C.
IPR013148. Glyco_hydro_32_N.
[Graphical view]
PfamPF08244. Glyco_hydro_32C. 1 hit.
PF00251. Glyco_hydro_32N. 1 hit.
[Graphical view]
SMARTSM00640. Glyco_32. 1 hit.
[Graphical view]
PROSITEPS00609. GLYCOSYL_HYDROL_F32. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameBFRA_THEMA
AccessionPrimary (citable) accession number: O33833
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: January 19, 2010
This is version 71 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)

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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

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