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Protein

Levanase

Gene

sacC

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Exo-fructosidase that can hydrolyze both levan and inulin, leading to the production of free fructose. Is also able to hydrolyze sucrose and to a small extent raffinose, but not melezitose, stachylose, cellobiose, maltose, and lactose.1 Publication

Catalytic activityi

Hydrolysis of terminal, non-reducing (2->1)- and (2->6)-linked beta-D-fructofuranose residues in fructans.

Enzyme regulationi

Is completely inhibited by Ag+ and Hg2+ ions.1 Publication

Kineticsi

  1. KM=1.2 µM for levan (at pH 5.5 and 55 degrees Celsius)1 Publication
  2. KM=6.7 mM for inulin (at pH 5.5 and 55 degrees Celsius)1 Publication
  3. KM=64 mM for sucrose (at pH 5.5 and 55 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is 5.5 for inulin hydrolysis.1 Publication

    Temperature dependencei

    Optimum temperature is 55 degrees Celsius for inulin hydrolysis. Is rapidly inactivated at 60 degrees Celsius. High stable at 50 and 55 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei49PROSITE-ProRule annotation1
    Binding sitei65SubstrateBy similarity1
    Binding sitei73SubstrateBy similarity1
    Binding sitei223SubstrateBy similarity1
    Binding sitei313SubstrateBy similarity1

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism

    Enzyme and pathway databases

    BioCyciBSUB:BSU27030-MONOMER.
    BRENDAi3.2.1.80. 658.

    Protein family/group databases

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Levanase (EC:3.2.1.80)
    Alternative name(s):
    Beta-D-fructofuranosidase
    Exo-beta-D-fructosidase
    Exo-levanase
    Gene namesi
    Name:sacC
    Ordered Locus Names:BSU27030
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    Proteomesi
    • UP000001570 Componenti: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 24Sequence analysisAdd BLAST24
    ChainiPRO_000003340525 – 677LevanaseAdd BLAST653

    Proteomic databases

    PaxDbiP05656.

    Expressioni

    Inductioni

    Induced by low concentrations of fructose, but not by sucrose. Repressed by glucose or high concentrations of fructose.1 Publication

    Interactioni

    Protein-protein interaction databases

    STRINGi224308.Bsubs1_010100014776.

    Structurei

    Secondary structure

    1677
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi529 – 535Combined sources7
    Beta strandi538 – 581Combined sources44
    Beta strandi585 – 594Combined sources10
    Turni595 – 598Combined sources4
    Beta strandi599 – 606Combined sources8
    Beta strandi609 – 617Combined sources9
    Beta strandi626 – 633Combined sources8
    Beta strandi636 – 641Combined sources6
    Beta strandi644 – 650Combined sources7
    Beta strandi657 – 676Combined sources20

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4AZZX-ray1.70A/B515-677[»]
    4B1LX-ray1.65A515-677[»]
    4B1MX-ray1.10A/B/C515-677[»]
    ProteinModelPortaliP05656.
    SMRiP05656.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni46 – 49Substrate bindingBy similarity4
    Regioni105 – 106Substrate bindingBy similarity2
    Regioni171 – 172Substrate bindingBy similarity2

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 32 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiENOG4108HKT. Bacteria.
    COG1621. LUCA.
    HOGENOMiHOG000181424.
    InParanoidiP05656.
    KOiK03332.
    OMAiIQCMAYS.
    PhylomeDBiP05656.

    Family and domain databases

    Gene3Di2.120.10.10. 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.
    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.
    PROSITEiPS00609. GLYCOSYL_HYDROL_F32. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P05656-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKKRLIQVMI MFTLLLTMAF SADAADSSYY DEDYRPQYHF TPEANWMNDP
    60 70 80 90 100
    NGMVYYAGEY HLFYQYHPYG LQWGPMHWGH AVSKDLVTWE HLPVALYPDE
    110 120 130 140 150
    KGTIFSGSAV VDKNNTSGFQ TGKEKPLVAI YTQDREGHQV QSIAYSNDKG
    160 170 180 190 200
    RTWTKYAGNP VIPNPGKKDF RDPKVFWYEK EKKWVMVLAA GDRILIYTSK
    210 220 230 240 250
    NLKQWTYASE FGQDQGSHGG VWECPDLFEL PVDGNPNQKK WVMQVSVGNG
    260 270 280 290 300
    AVSGGSGMQY FVGDFDGTHF KNENPPNKVL WTDYGRDFYA AVSWSDIPST
    310 320 330 340 350
    DSRRLWLGWM SNWQYANDVP TSPWRSATSI PRELKLKAFT EGVRVVQTPV
    360 370 380 390 400
    KELETIRGTS KKWKNLTISP ASHNVLAGQS GDAYEINAEF KVSPGSAAEF
    410 420 430 440 450
    GFKVRTGENQ FTKVGYDRRN AKLFVDRSES GNDTFNPAFN TGKETAPLKP
    460 470 480 490 500
    VNGKVKLRIF VDRSSVEVFG NDGKQVITDI ILPDRSSKGL ELYAANGGVK
    510 520 530 540 550
    VKSLTIHPLK KVWGTTPFMS NMTGWTTVNG TWADTIEGKQ GRSDGDSFIL
    560 570 580 590 600
    SSASGSDFTY ESDITIKDGN GRGAGALMFR SDKDAKNGYL ANVDAKHDLV
    610 620 630 640 650
    KFFKFENGAA SVIAEYKTPI DVNKKYHLKT EAEGDRFKIY LDDRLVIDAH
    660 670
    DSVFSEGQFG LNVWDATAVF QNVTKES
    Length:677
    Mass (Da):75,951
    Last modified:November 1, 1988 - v1
    Checksum:i80FD6B0A5EE7F525
    GO

    Sequence cautioni

    The sequence CAA29137 differs from that shown. Reason: Erroneous initiation.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti658Q → L in CAA68542 (PubMed:3120151).Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X05649 Genomic DNA. Translation: CAA29137.1. Different initiation.
    Y00485 Genomic DNA. Translation: CAA68542.1.
    X92868 Genomic DNA. Translation: CAA63465.1.
    AL009126 Genomic DNA. Translation: CAB14645.1.
    X56098 Genomic DNA. Translation: CAA39581.1.
    PIRiA27286.
    RefSeqiNP_390581.1. NC_000964.3.
    WP_004398804.1. NZ_JNCM01000036.1.

    Genome annotation databases

    EnsemblBacteriaiCAB14645; CAB14645; BSU27030.
    GeneIDi938092.
    KEGGibsu:BSU27030.
    PATRICi18977260. VBIBacSub10457_2819.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X05649 Genomic DNA. Translation: CAA29137.1. Different initiation.
    Y00485 Genomic DNA. Translation: CAA68542.1.
    X92868 Genomic DNA. Translation: CAA63465.1.
    AL009126 Genomic DNA. Translation: CAB14645.1.
    X56098 Genomic DNA. Translation: CAA39581.1.
    PIRiA27286.
    RefSeqiNP_390581.1. NC_000964.3.
    WP_004398804.1. NZ_JNCM01000036.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4AZZX-ray1.70A/B515-677[»]
    4B1LX-ray1.65A515-677[»]
    4B1MX-ray1.10A/B/C515-677[»]
    ProteinModelPortaliP05656.
    SMRiP05656.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi224308.Bsubs1_010100014776.

    Protein family/group databases

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

    Proteomic databases

    PaxDbiP05656.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiCAB14645; CAB14645; BSU27030.
    GeneIDi938092.
    KEGGibsu:BSU27030.
    PATRICi18977260. VBIBacSub10457_2819.

    Phylogenomic databases

    eggNOGiENOG4108HKT. Bacteria.
    COG1621. LUCA.
    HOGENOMiHOG000181424.
    InParanoidiP05656.
    KOiK03332.
    OMAiIQCMAYS.
    PhylomeDBiP05656.

    Enzyme and pathway databases

    BioCyciBSUB:BSU27030-MONOMER.
    BRENDAi3.2.1.80. 658.

    Family and domain databases

    Gene3Di2.120.10.10. 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.
    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.
    PROSITEiPS00609. GLYCOSYL_HYDROL_F32. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiSACC_BACSU
    AccessioniPrimary (citable) accession number: P05656
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: November 1, 1988
    Last modified: November 30, 2016
    This is version 129 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Levanase cannot be detected in the wild-type B.subtilis but is mostly secreted into the culture medium by SacL mutants, especially at the end of the exponential growth phase.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. 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.