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Protein

Levanase

Gene
N/A
Organism
Bacillus sp. (strain L7)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the hydrolysis of levan with endo-type specificity. The products of levan hydrolysis are a mixture of fructose and a series of fructooligosaccharides up to 12-mer, with levantriose being the major oligosaccharide obtained. Is not active towards sucrose.1 Publication

Catalytic activityi

Random hydrolysis of (2->6)-beta-D-fructofuranosidic linkages in (2->6)-beta-D-fructans (levans) containing more than 3 fructose units.

Enzyme regulationi

Is completely inhibited by low concentrations of heavy metal ions, while Ca2+ and Mg2+ or chelating agents such as EDTA neither inhibit nor activate the enzyme to any signicant extent.1 Publication

pH dependencei

Optimum pH is about 5.5 at 50 degrees Celsius and shows an apparent shift towards higher pH values at higher temperatures.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei412 – 4121By similarity
Binding sitei428 – 4281SubstrateBy similarity
Binding sitei591 – 5911SubstrateBy similarity
Binding sitei679 – 6791SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Protein family/group databases

CAZyiCBM66. Carbohydrate-Binding Module Family 66.
GH32. Glycoside Hydrolase Family 32.

Names & Taxonomyi

Protein namesi
Recommended name:
Levanase (EC:3.2.1.65)
Alternative name(s):
2,6-beta-D-fructan fructanohydrolase
Endo-levanase
OrganismiBacillus sp. (strain L7)
Taxonomic identifieri62626 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Subcellular locationi

  • Secreted 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence analysisAdd
BLAST
Chaini24 – ›921›898LevanasePRO_0000344252Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliO31411.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni409 – 4124Substrate bindingBy similarity
Regioni460 – 4612Substrate bindingBy similarity
Regioni539 – 5402Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the glycosyl hydrolase 32 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.120.10.10. 1 hit.
2.60.120.560. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR001362. Glyco_hydro_32.
IPR013189. Glyco_hydro_32_C.
IPR013148. Glyco_hydro_32_N.
IPR023296. Glyco_hydro_beta-prop.
IPR011040. Sialidases.
[Graphical view]
PfamiPF08244. Glyco_hydro_32C. 1 hit.
PF00251. Glyco_hydro_32N. 1 hit.
[Graphical view]
SMARTiSM00640. Glyco_32. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF75005. SSF75005. 1 hit.

Sequencei

Sequence statusi: Fragment.

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

O31411-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMKWFAKLIL SLSLAVVMAA SSAAISFGAS NSSLDTHASL VTQLDSAASE
60 70 80 90 100
AAEGKSAMIN ESAINSNVTG WKLHGKGRME VTGEGLRLTS DPQENVMAIS
110 120 130 140 150
ETVADDFIYE ADVMVTDPQA DATLLFRSGE DGWSSYMLQL ALGAGVIRLK
160 170 180 190 200
DASGGEGVLN VERKVEAKPG DIYHLRVKAE GTRLQVYWGQ QYEPVIDTEA
210 220 230 240 250
AAHRTGRLGL HVWNGSALFQ NIRVSDMSGN TLEPISSQGL WQPDLKGLKG
260 270 280 290 300
TGEDGLEAKK VFRNHEADVV LEGDLILNGQ GSAGLLFRSN AQGTEGYAAV
310 320 330 340 350
LQGEGERVRV YLKKADGTIL HESRVTYPSQ RESRHHLEVK AIGERIQIFV
360 370 380 390 400
DGYEPAAIDM VDTAFPSGYH GVMASSGIAY FQDVYITPYA SYYTEKYRPQ
410 420 430 440 450
YHYSPIRGSA SDPNGLVYFE GEYHLFHQDG GQWAHAVSRD LIHWKRLPIA
460 470 480 490 500
LPWNDLGHVW SGSAVADTTN ASGLFGSSGG KGLIAYYTSY NPDRHNGNQK
510 520 530 540 550
IGLAYSTDRG RTWKYSEEHP VVIENPGKTG EDPGGWDFRD PKVVRDEANN
560 570 580 590 600
RWVMVVSGGD HIRLFTSTNL LNWTLTDQFG YGAYIRGGVW ECPDLFQLPV
610 620 630 640 650
EGSKKRKWVL MISTGANPNT QGSDAEYFIG DLTPEGKFIN DNPAGTVLKT
660 670 680 690 700
DWGKEYYASM SFSDMPDGRR IMLAWMTNWD YPFSFPTTGW KGQLSIPRQV
710 720 730 740 750
SLKETEEGIR MHQTPIEELA QLRSPVLTSP TARWGTSGEN LLKGITSGAY
760 770 780 790 800
EIEAELELPP TGAASEFGFR LREGDGQRTL VGYRAAGSKM FVDRSASGMT
810 820 830 840 850
DFSDLFSTLH EAPLKPEGNR IKLRILVDES SVEVFGNDGR VVFSDVIFPD
860 870 880 890 900
PASRGMSFYS EGGKVKVVSL QVHALQHIWR EDEAKEPRVV MDTETLELSL
910 920
GQTKPLFASI DNGQGKGADG I
Length:921
Mass (Da):101,206
Last modified:July 22, 2008 - v2
Checksum:i24B04DE96067DC44
GO

Sequence cautioni

The sequence CAA73180 differs from that shown. Reason: Frameshift at position 728. The exact location of the frameshift is not clear.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei921 – 9211

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y12619 Genomic DNA. Translation: CAA73180.1. Frameshift.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y12619 Genomic DNA. Translation: CAA73180.1. Frameshift.

3D structure databases

ProteinModelPortaliO31411.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM66. Carbohydrate-Binding Module Family 66.
GH32. Glycoside Hydrolase Family 32.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di2.120.10.10. 1 hit.
2.60.120.560. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR001362. Glyco_hydro_32.
IPR013189. Glyco_hydro_32_C.
IPR013148. Glyco_hydro_32_N.
IPR023296. Glyco_hydro_beta-prop.
IPR011040. Sialidases.
[Graphical view]
PfamiPF08244. Glyco_hydro_32C. 1 hit.
PF00251. Glyco_hydro_32N. 1 hit.
[Graphical view]
SMARTiSM00640. Glyco_32. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF75005. SSF75005. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiSACC_BACL7
AccessioniPrimary (citable) accession number: O31411
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: July 22, 2008
Last modified: September 7, 2016
This is version 63 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

Functional characterization has been done on a chimeric protein carrying at its C-terminus a fragment of the cloning vector instead of the levanase sequence.Curated

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. 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.