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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)DescriptionActionsGraphical viewLength
Active sitei171
Binding sitei33Substrate1
Binding sitei41Substrate1
Binding sitei92Substrate1
Binding sitei208Substrate1
Binding sitei260Substrate1

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)DescriptionActionsGraphical viewLength
Mutagenesisi190E → A: Loss of activity. 1 Publication1
Mutagenesisi190E → D: Reduced activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001698811 – 432Beta-fructosidaseAdd BLAST432

Proteomic databases

PRIDEiO33833.

Interactioni

Protein-protein interaction databases

STRINGi243274.TM1414.

Structurei

Secondary structure

1432
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 7Combined sources3
Beta strandi11 – 24Combined sources14
Beta strandi27 – 35Combined sources9
Beta strandi38 – 40Combined sources3
Beta strandi45 – 56Combined sources12
Beta strandi58 – 64Combined sources7
Beta strandi71 – 81Combined sources11
Beta strandi84 – 93Combined sources10
Beta strandi102 – 114Combined sources13
Beta strandi133 – 143Combined sources11
Beta strandi145 – 156Combined sources12
Turni157 – 159Combined sources3
Beta strandi160 – 173Combined sources14
Beta strandi175 – 183Combined sources9
Beta strandi190 – 197Combined sources8
Beta strandi200 – 207Combined sources8
Turni208 – 211Combined sources4
Beta strandi212 – 221Combined sources10
Beta strandi224 – 233Combined sources10
Beta strandi236 – 238Combined sources3
Beta strandi240 – 244Combined sources5
Beta strandi249 – 258Combined sources10
Turni260 – 262Combined sources3
Helixi263 – 265Combined sources3
Helixi268 – 271Combined sources4
Beta strandi281 – 286Combined sources6
Beta strandi289 – 294Combined sources6
Helixi296 – 301Combined sources6
Beta strandi302 – 311Combined sources10
Beta strandi313 – 316Combined sources4
Beta strandi320 – 322Combined sources3
Beta strandi324 – 339Combined sources16
Beta strandi344 – 350Combined sources7
Beta strandi353 – 357Combined sources5
Beta strandi368 – 372Combined sources5
Beta strandi377 – 386Combined sources10
Beta strandi389 – 394Combined sources6
Turni395 – 397Combined sources3
Beta strandi398 – 403Combined sources6
Beta strandi412 – 427Combined sources16

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiO33833.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni14 – 17Substrate binding4
Regioni74 – 75Substrate binding2
Regioni137 – 138Substrate binding2
Regioni188 – 190Substrate binding3

Sequence similaritiesi

Belongs to the glycosyl hydrolase 32 family.Curated

Phylogenomic databases

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

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UYPX-ray1.90A/B/C/D/E/F2-432[»]
1W2TX-ray1.87A/B/C/D/E/F2-432[»]
ProteinModelPortaliO33833.
SMRiO33833.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243274.TM1414.

Protein family/group databases

CAZyiGH32. Glycoside Hydrolase Family 32.

Proteomic databases

PRIDEiO33833.

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.

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...

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: November 2, 2016
This is version 120 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.