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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)DescriptionActionsGraphical viewLength
Binding sitei271Substrate1 Publication1
Active sitei272Nucleophile1 Publication1
Metal bindingi317Calcium 1Combined sources1 Publication1
Binding sitei340Substrate1 Publication1
Metal bindingi419Calcium 2Combined sources1 Publication1
Sitei425Transition state stabilizer1 Publication1
Metal bindingi450Calcium 2Combined sources1 Publication1
Metal bindingi487Calcium 2; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi489Calcium 2Combined sources1 Publication1
Metal bindingi521Calcium 2Combined sources1 Publication1
Active sitei524Proton donor/acceptor1 Publication1
Binding sitei542Substrate1 Publication1
Metal bindingi660Calcium 1Combined sources1 Publication1
Metal bindingi662Calcium 1; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi667Calcium 1Combined sources1 Publication1

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

BRENDAi2.4.1.9. 2873.
SABIO-RKQ74K42.

Protein family/group databases

CAZyiGH68. Glycoside Hydrolase Family 68.

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)DescriptionActionsGraphical viewLength
Mutagenesisi272D → N: Loss of catalytic activity. 1 Publication1
Mutagenesisi301 – 303Missing : 1.5% of wild-type activity. 1 Publication3
Mutagenesisi301N → A: 25% of wild-type activity. 1 Publication1
Mutagenesisi301N → S: 40% of wild-type activity. 1 Publication1
Mutagenesisi305N → A: 29% of wild-type activity. 1 Publication1
Mutagenesisi305N → S: 50% of wild-type activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 36Sequence analysisAdd BLAST36
ChainiPRO_000043124837 – 797InulosucraseAdd BLAST761
PropeptideiPRO_0000431249765 – 797Removed by sortasePROSITE-ProRule annotationAdd BLAST33

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei764Pentaglycyl murein peptidoglycan amidated alaninePROSITE-ProRule annotation1

Keywords - PTMi

Peptidoglycan-anchor

Interactioni

Protein-protein interaction databases

STRINGi257314.LJ0913.

Structurei

Secondary structure

1797
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi181 – 189Combined sources9
Helixi194 – 196Combined sources3
Helixi199 – 205Combined sources7
Beta strandi215 – 219Combined sources5
Helixi222 – 234Combined sources13
Turni237 – 239Combined sources3
Helixi246 – 248Combined sources3
Helixi253 – 255Combined sources3
Beta strandi256 – 258Combined sources3
Turni260 – 262Combined sources3
Beta strandi263 – 267Combined sources5
Beta strandi269 – 277Combined sources9
Turni279 – 281Combined sources3
Beta strandi290 – 298Combined sources9
Beta strandi306 – 313Combined sources8
Helixi319 – 321Combined sources3
Beta strandi323 – 327Combined sources5
Beta strandi336 – 345Combined sources10
Beta strandi351 – 359Combined sources9
Turni361 – 364Combined sources4
Beta strandi367 – 380Combined sources14
Helixi381 – 383Combined sources3
Beta strandi385 – 398Combined sources14
Beta strandi402 – 405Combined sources4
Helixi408 – 414Combined sources7
Beta strandi424 – 430Combined sources7
Beta strandi436 – 444Combined sources9
Helixi452 – 456Combined sources5
Helixi458 – 460Combined sources3
Helixi465 – 477Combined sources13
Helixi479 – 487Combined sources9
Beta strandi490 – 497Combined sources8
Beta strandi501 – 503Combined sources3
Beta strandi506 – 509Combined sources4
Beta strandi513 – 515Combined sources3
Turni517 – 519Combined sources3
Beta strandi524 – 531Combined sources8
Beta strandi534 – 542Combined sources9
Helixi543 – 545Combined sources3
Helixi549 – 559Combined sources11
Beta strandi563 – 575Combined sources13
Turni580 – 583Combined sources4
Beta strandi584 – 588Combined sources5
Beta strandi599 – 607Combined sources9
Beta strandi610 – 621Combined sources12
Turni624 – 627Combined sources4
Beta strandi637 – 644Combined sources8
Turni645 – 647Combined sources3
Beta strandi648 – 658Combined sources11
Helixi665 – 667Combined sources3
Helixi670 – 672Combined sources3
Beta strandi678 – 680Combined sources3
Beta strandi683 – 685Combined sources3
Turni687 – 691Combined sources5
Turni695 – 697Combined sources3
Turni700 – 703Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2YFRX-ray1.75A145-708[»]
2YFSX-ray2.60A145-708[»]
2YFTX-ray1.85A145-708[»]
ProteinModelPortaliQ74K42.
SMRiQ74K42.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni424 – 425Substrate binding1 Publication2
Regioni522 – 524Substrate binding1 Publication3

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi761 – 765LPXTG sorting signalPROSITE-ProRule annotation5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi706 – 752Pro-richPROSITE-ProRule annotationAdd BLAST47

Sequence similaritiesi

Belongs to the glycosyl hydrolase 68 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105EDQ. Bacteria.
ENOG410XR0E. LUCA.
KOiK20811.
OMAiWIWDESS.

Family and domain databases

Gene3Di2.115.10.20. 1 hit.
InterProiIPR003469. Glyco_hydro_68.
IPR023296. Glyco_hydro_beta-prop.
[Graphical view]
PfamiPF02435. Glyco_hydro_68. 1 hit.
[Graphical view]
SUPFAMiSSF75005. SSF75005. 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:LJ_0913.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2YFRX-ray1.75A145-708[»]
2YFSX-ray2.60A145-708[»]
2YFTX-ray1.85A145-708[»]
ProteinModelPortaliQ74K42.
SMRiQ74K42.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi257314.LJ0913.

Protein family/group databases

CAZyiGH68. Glycoside Hydrolase Family 68.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiENOG4105EDQ. Bacteria.
ENOG410XR0E. LUCA.
KOiK20811.
OMAiWIWDESS.

Enzyme and pathway databases

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.
[Graphical view]
PfamiPF02435. Glyco_hydro_68. 1 hit.
[Graphical view]
SUPFAMiSSF75005. SSF75005. 1 hit.
PROSITEiPS50847. GRAM_POS_ANCHORING. 1 hit.
[Graphical view]
ProtoNetiSearch...

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 30, 2016
This is version 79 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.