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Protein

Beta-fructosidase

Gene

bfrA

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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

Temperature dependencei

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei17 – 171
Binding sitei33 – 331Substrate
Binding sitei41 – 411Substrate
Binding sitei92 – 921Substrate
Binding sitei208 – 2081Substrate
Binding sitei260 – 2601Substrate

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BRENDAi3.2.1.26. 6331.

Protein family/group databases

CAZyiGH32. Glycoside Hydrolase Family 32.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-fructosidase (EC:3.2.1.26)
Alternative name(s):
Invertase
Sucrase
Gene namesi
Name:bfrA
Ordered Locus Names:TM_1414
OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Taxonomic identifieri243274 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
Proteomesi
  • UP000008183 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi190 – 1901E → A: Loss of activity. 1 Publication
Mutagenesisi190 – 1901E → D: Reduced activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 432432Beta-fructosidasePRO_0000169881Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi243274.TM1414.

Structurei

Secondary structure

1
432
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 73Combined sources
Beta strandi11 – 2414Combined sources
Beta strandi27 – 359Combined sources
Beta strandi38 – 403Combined sources
Beta strandi45 – 5612Combined sources
Beta strandi58 – 647Combined sources
Beta strandi71 – 8111Combined sources
Beta strandi84 – 9310Combined sources
Beta strandi102 – 11413Combined sources
Beta strandi133 – 14311Combined sources
Beta strandi145 – 15612Combined sources
Turni157 – 1593Combined sources
Beta strandi160 – 17314Combined sources
Beta strandi175 – 1839Combined sources
Beta strandi190 – 1978Combined sources
Beta strandi200 – 2078Combined sources
Turni208 – 2114Combined sources
Beta strandi212 – 22110Combined sources
Beta strandi224 – 23310Combined sources
Beta strandi236 – 2383Combined sources
Beta strandi240 – 2445Combined sources
Beta strandi249 – 25810Combined sources
Turni260 – 2623Combined sources
Helixi263 – 2653Combined sources
Helixi268 – 2714Combined sources
Beta strandi281 – 2866Combined sources
Beta strandi289 – 2946Combined sources
Helixi296 – 3016Combined sources
Beta strandi302 – 31110Combined sources
Beta strandi313 – 3164Combined sources
Beta strandi320 – 3223Combined sources
Beta strandi324 – 33916Combined sources
Beta strandi344 – 3507Combined sources
Beta strandi353 – 3575Combined sources
Beta strandi368 – 3725Combined sources
Beta strandi377 – 38610Combined sources
Beta strandi389 – 3946Combined sources
Turni395 – 3973Combined sources
Beta strandi398 – 4036Combined sources
Beta strandi412 – 42716Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UYPX-ray1.90A/B/C/D/E/F2-432[»]
1W2TX-ray1.87A/B/C/D/E/F2-432[»]
ProteinModelPortaliO33833.
SMRiO33833. Positions 1-432.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO33833.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni14 – 174Substrate binding
Regioni74 – 752Substrate binding
Regioni137 – 1382Substrate binding
Regioni188 – 1903Substrate binding

Sequence similaritiesi

Belongs to the glycosyl hydrolase 32 family.Curated

Phylogenomic databases

eggNOGiENOG4108HKT. Bacteria.
COG1621. LUCA.
InParanoidiO33833.
KOiK01193.
OMAiARQSKWR.
OrthoDBiEOG6KDKMP.

Family and domain databases

Gene3Di2.115.10.20. 1 hit.
2.60.120.560. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR001362. Glyco_hydro_32.
IPR018053. Glyco_hydro_32_AS.
IPR013189. Glyco_hydro_32_C.
IPR013148. Glyco_hydro_32_N.
IPR023296. Glyco_hydro_beta-prop.
[Graphical view]
PfamiPF00251. Glyco_hydro_32N. 1 hit.
[Graphical view]
SMARTiSM00640. Glyco_32. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF75005. SSF75005. 1 hit.
PROSITEiPS00609. GLYCOSYL_HYDROL_F32. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O33833-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFKPNYHFFP ITGWMNDPNG LIFWKGKYHM FYQYNPRKPE WGNICWGHAV
60 70 80 90 100
SDDLVHWRHL PVALYPDDET HGVFSGSAVE KDGKMFLVYT YYRDPTHNKG
110 120 130 140 150
EKETQCVAMS ENGLDFVKYD GNPVISKPPE EGTHAFRDPK VNRSNGEWRM
160 170 180 190 200
VLGSGKDEKI GRVLLYTSDD LFHWKYEGVI FEDETTKEIE CPDLVRIGEK
210 220 230 240 250
DILIYSITST NSVLFSMGEL KEGKLNVEKR GLLDHGTDFY AAQTFFGTDR
260 270 280 290 300
VVVIGWLQSW LRTGLYPTKR EGWNGVMSLP RELYVENNEL KVKPVDELLA
310 320 330 340 350
LRKRKVFETA KSGTFLLDVK ENSYEIVCEF SGEIELRMGN ESEEVVITKS
360 370 380 390 400
RDELIVDTTR SGVSGGEVRK STVEDEATNR IRAFLDSCSV EFFFNDSIAF
410 420 430
SFRIHPENVY NILSVKSNQV KLEVFELENI WL
Length:432
Mass (Da):49,841
Last modified:January 1, 1998 - v1
Checksum:i39F61B2E1BC462B9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ001073 Genomic DNA. Translation: CAA04518.1.
AE000512 Genomic DNA. Translation: AAD36485.1.
PIRiD72255.
RefSeqiNP_229215.1. NC_000853.1.
WP_004081649.1. NZ_CP011107.1.

Genome annotation databases

EnsemblBacteriaiAAD36485; AAD36485; TM_1414.
GeneIDi898062.
KEGGitma:TM1414.
PATRICi23937772. VBITheMar51294_1425.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ001073 Genomic DNA. Translation: CAA04518.1.
AE000512 Genomic DNA. Translation: AAD36485.1.
PIRiD72255.
RefSeqiNP_229215.1. NC_000853.1.
WP_004081649.1. NZ_CP011107.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UYPX-ray1.90A/B/C/D/E/F2-432[»]
1W2TX-ray1.87A/B/C/D/E/F2-432[»]
ProteinModelPortaliO33833.
SMRiO33833. Positions 1-432.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243274.TM1414.

Protein family/group databases

CAZyiGH32. Glycoside Hydrolase Family 32.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD36485; AAD36485; TM_1414.
GeneIDi898062.
KEGGitma:TM1414.
PATRICi23937772. VBITheMar51294_1425.

Phylogenomic databases

eggNOGiENOG4108HKT. Bacteria.
COG1621. LUCA.
InParanoidiO33833.
KOiK01193.
OMAiARQSKWR.
OrthoDBiEOG6KDKMP.

Enzyme and pathway databases

BRENDAi3.2.1.26. 6331.

Miscellaneous databases

EvolutionaryTraceiO33833.

Family and domain databases

Gene3Di2.115.10.20. 1 hit.
2.60.120.560. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR001362. Glyco_hydro_32.
IPR018053. Glyco_hydro_32_AS.
IPR013189. Glyco_hydro_32_C.
IPR013148. Glyco_hydro_32_N.
IPR023296. Glyco_hydro_beta-prop.
[Graphical view]
PfamiPF00251. Glyco_hydro_32N. 1 hit.
[Graphical view]
SMARTiSM00640. Glyco_32. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF75005. SSF75005. 1 hit.
PROSITEiPS00609. GLYCOSYL_HYDROL_F32. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
    Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
  2. 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) OF 2-432 IN COMPLEX WITH SUBSTRATES, MUTAGENESIS OF GLU-190.

Entry informationi

Entry nameiBFRA_THEMA
AccessioniPrimary (citable) accession number: O33833
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: May 11, 2016
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.