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Protein

Inulosucrase

Gene

inuJ

Organism
Lactobacillus johnsonii (strain CNCM I-12250 / La1 / NCC 533)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Fructosyltransferase that catalyzes the polymerization of the fructose moiety of sucrose to produce inulin polymer and inulin oligosaccharides such as 1-kestose and nystose.2 Publications

Catalytic activityi

Sucrose + ((2->1)-beta-D-fructosyl)(n) = glucose + ((2->1)-beta-D-fructosyl)(n+1).2 Publications

Cofactori

Ca2+1 Publication

pH dependencei

Optimum pH is 7. More than 85% of the activity is retained in the pH range 4.5-6.0. Activity decreases sharply at pH 7.5.1 Publication

Temperature dependencei

Optimum temperature is 55 degrees Celsius. Activity drastically decreases at 60 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei271 – 2711Substrate1 Publication
Active sitei272 – 2721Nucleophile1 Publication
Metal bindingi317 – 3171Calcium 1Combined sources1 Publication
Binding sitei340 – 3401Substrate1 Publication
Metal bindingi419 – 4191Calcium 2Combined sources1 Publication
Sitei425 – 4251Transition state stabilizer1 Publication
Metal bindingi450 – 4501Calcium 2Combined sources1 Publication
Metal bindingi487 – 4871Calcium 2; via carbonyl oxygenCombined sources1 Publication
Metal bindingi489 – 4891Calcium 2Combined sources1 Publication
Metal bindingi521 – 5211Calcium 2Combined sources1 Publication
Active sitei524 – 5241Proton donor/acceptor1 Publication
Binding sitei542 – 5421Substrate1 Publication
Metal bindingi660 – 6601Calcium 1Combined sources1 Publication
Metal bindingi662 – 6621Calcium 1; via carbonyl oxygenCombined sources1 Publication
Metal bindingi667 – 6671Calcium 1Combined sources1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BioCyciLJOH257314:GJN3-775-MONOMER.
BRENDAi2.4.1.9. 2873.
SABIO-RKQ74K42.

Names & Taxonomyi

Protein namesi
Recommended name:
Inulosucrase1 Publication (EC:2.4.1.92 Publications)
Short name:
ISBy similarity
Gene namesi
Name:inuJ1 Publication
Synonyms:ftf1 Publication
Ordered Locus Names:LJ_0913
OrganismiLactobacillus johnsonii (strain CNCM I-12250 / La1 / NCC 533)
Taxonomic identifieri257314 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus
Proteomesi
  • UP000000581 Componenti: Chromosome

Subcellular locationi

  • Secretedcell wall PROSITE-ProRule annotation; Peptidoglycan-anchor PROSITE-ProRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell wall, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi272 – 2721D → N: Loss of catalytic activity. 1 Publication
Mutagenesisi301 – 3033Missing : 1.5% of wild-type activity. 1 Publication
Mutagenesisi301 – 3011N → A: 25% of wild-type activity. 1 Publication
Mutagenesisi301 – 3011N → S: 40% of wild-type activity. 1 Publication
Mutagenesisi305 – 3051N → A: 29% of wild-type activity. 1 Publication
Mutagenesisi305 – 3051N → S: 50% of wild-type activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3636Sequence analysisAdd
BLAST
Chaini37 – 797761InulosucrasePRO_0000431248Add
BLAST
Propeptidei765 – 79733Removed by sortasePROSITE-ProRule annotationPRO_0000431249Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei764 – 7641Pentaglycyl murein peptidoglycan amidated alaninePROSITE-ProRule annotation

Keywords - PTMi

Peptidoglycan-anchor

Interactioni

Protein-protein interaction databases

STRINGi257314.LJ0913.

Structurei

Secondary structure

1
797
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi181 – 1899Combined sources
Helixi194 – 1963Combined sources
Helixi199 – 2057Combined sources
Beta strandi215 – 2195Combined sources
Helixi222 – 23413Combined sources
Turni237 – 2393Combined sources
Helixi246 – 2483Combined sources
Helixi253 – 2553Combined sources
Beta strandi256 – 2583Combined sources
Turni260 – 2623Combined sources
Beta strandi263 – 2675Combined sources
Beta strandi269 – 2779Combined sources
Turni279 – 2813Combined sources
Beta strandi290 – 2989Combined sources
Beta strandi306 – 3138Combined sources
Helixi319 – 3213Combined sources
Beta strandi323 – 3275Combined sources
Beta strandi336 – 34510Combined sources
Beta strandi351 – 3599Combined sources
Turni361 – 3644Combined sources
Beta strandi367 – 38014Combined sources
Helixi381 – 3833Combined sources
Beta strandi385 – 39814Combined sources
Beta strandi402 – 4054Combined sources
Helixi408 – 4147Combined sources
Beta strandi424 – 4307Combined sources
Beta strandi436 – 4449Combined sources
Helixi452 – 4565Combined sources
Helixi458 – 4603Combined sources
Helixi465 – 47713Combined sources
Helixi479 – 4879Combined sources
Beta strandi490 – 4978Combined sources
Beta strandi501 – 5033Combined sources
Beta strandi506 – 5094Combined sources
Beta strandi513 – 5153Combined sources
Turni517 – 5193Combined sources
Beta strandi524 – 5318Combined sources
Beta strandi534 – 5429Combined sources
Helixi543 – 5453Combined sources
Helixi549 – 55911Combined sources
Beta strandi563 – 57513Combined sources
Turni580 – 5834Combined sources
Beta strandi584 – 5885Combined sources
Beta strandi599 – 6079Combined sources
Beta strandi610 – 62112Combined sources
Turni624 – 6274Combined sources
Beta strandi637 – 6448Combined sources
Turni645 – 6473Combined sources
Beta strandi648 – 65811Combined sources
Helixi665 – 6673Combined sources
Helixi670 – 6723Combined sources
Beta strandi678 – 6803Combined sources
Beta strandi683 – 6853Combined sources
Turni687 – 6915Combined sources
Turni695 – 6973Combined sources
Turni700 – 7034Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YFRX-ray1.75A145-708[»]
2YFSX-ray2.60A145-708[»]
2YFTX-ray1.85A145-708[»]
ProteinModelPortaliQ74K42.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni424 – 4252Substrate binding1 Publication
Regioni522 – 5243Substrate binding1 Publication

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi761 – 7655LPXTG sorting signalPROSITE-ProRule annotation

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi706 – 75247Pro-richPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyl hydrolase 68 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105EDQ. Bacteria.
ENOG410XR0E. LUCA.
KOiK00692.
OMAiWRTATYS.
OrthoDBiEOG6038XR.

Family and domain databases

Gene3Di2.115.10.20. 1 hit.
InterProiIPR003469. Glyco_hydro_68.
IPR023296. Glyco_hydro_beta-prop.
IPR019931. LPXTG_anchor.
[Graphical view]
PfamiPF02435. Glyco_hydro_68. 1 hit.
[Graphical view]
SUPFAMiSSF75005. SSF75005. 1 hit.
TIGRFAMsiTIGR01167. LPXTG_anchor. 1 hit.
PROSITEiPS50847. GRAM_POS_ANCHORING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q74K42-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLENKNHKKI SLSGKSLLMG TLSTAAIVLS ASTANAATIN ADNVNENQTV
60 70 80 90 100
EVTASSVNNE NNKQVTEKDS ADKSTSDVAE DANTKKSNEN TETTEKNTQT
110 120 130 140 150
VVTNAPVSDV KNTNTVTAET PVDKVVNNSD QKTTNAATTD TKKDDVKQVE
160 170 180 190 200
KKDSVDKTNA EENKDSSVKP AENATKAELK GQVKDIVEES GVDTSKLTND
210 220 230 240 250
QINELNKINF SKEAKSGTQL TYNDFKKIAK TLIEQDARYA IPFFNASKIK
260 270 280 290 300
NMPAAKTLDA QSGKVEDLEI WDSWPVQDAK TGYVSNWNGY QLVIGMMGVP
310 320 330 340 350
NVNDNHIYLL YNKYGDNDFN HWKNAGPIFG LGTPVIQQWS GSATLNKDGS
360 370 380 390 400
IQLYYTKVDT SDNNTNHQKL ASATVYLNLE KDQDKISIAH VDNDHIVFEG
410 420 430 440 450
DGYHYQTYDQ WKETNKGADN IAMRDAHVID DDNGNRYLVF EASTGTENYQ
460 470 480 490 500
GDDQIYQWLN YGGTNKDNLG DFFQILSNSD IKDRAKWSNA AIGIIKLNDD
510 520 530 540 550
VKNPSVAKVY SPLISAPMVS DEIERPDVVK LGNKYYLFAA TRLNRGSNDD
560 570 580 590 600
AWMATNKAVG DNVAMIGYVS DNLTHGYVPL NESGVVLTAS VPANWRTATY
610 620 630 640 650
SYYAVPVEGR DDQLLITSYI TNRGEVAGKG MHATWAPSFL LQINPDNTTT
660 670 680 690 700
VLAKMTNQGD WIWDDSSENP DMMGVLEKDA PNSAALPGEW GKPVDWDLIG
710 720 730 740 750
GYNLKPHQPV TPIPNVPTTP ETPTTPDKPE VPTTPEVPTT PETPTPEAPK
760 770 780 790
NPVKKTSQSK LPKAGDKNSF AAVVLGAVSS ILGAVGLTGV SKRKRNN
Length:797
Mass (Da):87,186
Last modified:July 5, 2004 - v1
Checksum:i3E1F6460C93342C8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017198 Genomic DNA. Translation: AAS08734.1.
RefSeqiWP_011161805.1. NC_005362.1.

Genome annotation databases

EnsemblBacteriaiAAS08734; AAS08734; LJ_0913.
GeneIDi23681827.
KEGGiljo:LJ0913.
PATRICi22238180. VBILacJoh1832_0770.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017198 Genomic DNA. Translation: AAS08734.1.
RefSeqiWP_011161805.1. NC_005362.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YFRX-ray1.75A145-708[»]
2YFSX-ray2.60A145-708[»]
2YFTX-ray1.85A145-708[»]
ProteinModelPortaliQ74K42.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi257314.LJ0913.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAS08734; AAS08734; LJ_0913.
GeneIDi23681827.
KEGGiljo:LJ0913.
PATRICi22238180. VBILacJoh1832_0770.

Phylogenomic databases

eggNOGiENOG4105EDQ. Bacteria.
ENOG410XR0E. LUCA.
KOiK00692.
OMAiWRTATYS.
OrthoDBiEOG6038XR.

Enzyme and pathway databases

BioCyciLJOH257314:GJN3-775-MONOMER.
BRENDAi2.4.1.9. 2873.
SABIO-RKQ74K42.

Family and domain databases

Gene3Di2.115.10.20. 1 hit.
InterProiIPR003469. Glyco_hydro_68.
IPR023296. Glyco_hydro_beta-prop.
IPR019931. LPXTG_anchor.
[Graphical view]
PfamiPF02435. Glyco_hydro_68. 1 hit.
[Graphical view]
SUPFAMiSSF75005. SSF75005. 1 hit.
TIGRFAMsiTIGR01167. LPXTG_anchor. 1 hit.
PROSITEiPS50847. GRAM_POS_ANCHORING. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CNCM I-1225 / La1 / NCC 533.
  2. "The probiotic Lactobacillus johnsonii NCC 533 produces high-molecular-mass inulin from sucrose by using an inulosucrase enzyme."
    Anwar M.A., Kralj S., van der Maarel M.J., Dijkhuizen L.
    Appl. Environ. Microbiol. 74:3426-3433(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
    Strain: CNCM I-1225 / La1 / NCC 533.
  3. "Crystal structure of inulosucrase from Lactobacillus: insights into the substrate specificity and product specificity of GH68 fructansucrases."
    Pijning T., Anwar M.A., Boger M., Dobruchowska J.M., Leemhuis H., Kralj S., Dijkhuizen L., Dijkstra B.W.
    J. Mol. Biol. 412:80-93(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 145-708 OF APOENZYME AND COMPLEX WITH THE TRANSFRUCTOSYLATION PRODUCT 1-KESTOSE AND CALCIUM AND MUTANT ASN-272 IN COMPLEX WITH SUCROSE, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, MUTAGENESIS OF ASP-272; ASN-301 AND ASN-305.
    Strain: CNCM I-1225 / La1 / NCC 533.

Entry informationi

Entry nameiINUS_LACJO
AccessioniPrimary (citable) accession number: Q74K42
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 26, 2014
Last sequence update: July 5, 2004
Last modified: November 11, 2015
This is version 75 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.