Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q03174

- FRUA_STRMU

UniProt

Q03174 - FRUA_STRMU

Protein

Fructan beta-fructosidase

Gene

fruA

Organism
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 2 (28 Nov 2002)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    This protein is a fructanase enzyme which degrades levans and inulins to fructose and also cleaves sucrose into glucose and fructose and can therefore function as an extracellular invertase.

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei458 – 4581PROSITE-ProRule annotation
    Binding sitei474 – 4741SubstrateBy similarity
    Binding sitei783 – 7831SubstrateBy similarity

    GO - Molecular functioni

    1. fructan beta-fructosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Enzyme and pathway databases

    BioCyciSMUT210007:GC7Z-91-MONOMER.

    Protein family/group databases

    CAZyiGH32. Glycoside Hydrolase Family 32.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fructan beta-fructosidase (EC:3.2.1.80)
    Alternative name(s):
    Exo-beta-D-fructosidase
    Fructanase
    Gene namesi
    Name:fruA
    Ordered Locus Names:SMU_78
    OrganismiStreptococcus mutans serotype c (strain ATCC 700610 / UA159)
    Taxonomic identifieri210007 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
    ProteomesiUP000002512: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    1. cell wall Source: UniProtKB-SubCell
    2. extracellular region Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cell wall, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3939Sequence AnalysisAdd
    BLAST
    Chaini40 – 13911352Fructan beta-fructosidasePRO_0000033406Add
    BLAST
    Propeptidei1392 – 142332Removed by sortaseSequence AnalysisPRO_0000033407Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1391 – 13911Pentaglycyl murein peptidoglycan amidated threonineSequence Analysis

    Keywords - PTMi

    Peptidoglycan-anchor

    Expressioni

    Inductioni

    By sucrose, fructan substrates and fructose.

    Interactioni

    Protein-protein interaction databases

    STRINGi210007.SMU.78.

    Structurei

    3D structure databases

    ProteinModelPortaliQ03174.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni455 – 4584Substrate bindingBy similarity
    Regioni513 – 5142Substrate bindingBy similarity
    Regioni581 – 5822Substrate bindingBy similarity
    Regioni867 – 8715Involved in binding of sugars with beta-(2,6) linkages or binding of molecular weight fructansBy similarity

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1388 – 13925LPXTG sorting signalSequence Analysis

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 32 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG1621.
    KOiK03332.
    OMAiSYAAMTY.
    OrthoDBiEOG6DJXZ4.

    Family and domain databases

    Gene3Di2.120.10.10. 1 hit.
    2.60.120.200. 1 hit.
    2.60.120.560. 1 hit.
    InterProiIPR003343. Big_2.
    IPR025883. Cadherin-like_b_sandwich.
    IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR001362. Glyco_hydro_32.
    IPR018053. Glyco_hydro_32_AS.
    IPR013189. Glyco_hydro_32_C.
    IPR013148. Glyco_hydro_32_N.
    IPR023296. Glyco_hydro_beta-prop.
    IPR008964. Invasin/intimin_cell_adhesion.
    IPR022263. KxYKxGKxW.
    IPR001791. Laminin_G.
    IPR011040. Sialidases.
    [Graphical view]
    PfamiPF02368. Big_2. 1 hit.
    PF12733. Cadherin-like. 1 hit.
    PF08244. Glyco_hydro_32C. 1 hit.
    PF00251. Glyco_hydro_32N. 1 hit.
    PF02210. Laminin_G_2. 1 hit.
    [Graphical view]
    SMARTiSM00635. BID_2. 1 hit.
    SM00640. Glyco_32. 1 hit.
    [Graphical view]
    SUPFAMiSSF49373. SSF49373. 1 hit.
    SSF49899. SSF49899. 2 hits.
    SSF75005. SSF75005. 1 hit.
    TIGRFAMsiTIGR03715. KxYKxGKxW. 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.

    Q03174-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEEETVCKNW FMRKSGKSWI FGCAVFFVLG LATALPVAAE EISQTTAADT     50
    AVTEVRTEDS SQTSSQETAV TETTQSEGTA SKQLTTPAVA DQTTEPTDNE 100
    PISSSDGASS PYQVTDTTEP QQTLTPADSE PQAKADVQQA AAPKKEEINP 150
    VTNLEDMSHD TNGTWEVRED GIHSNAIGKG DSFLYSQSSG KNFVYATDVT 200
    FKQNSGAAAL VFRSNNDSNN KNMYAVNVDI GGHKAKFWRW VDNKDIQLID 250
    ERDVVPTADN RYTLKVVAVN NWISYYVNDI LMASTGDYVL QKADKGQNTV 300
    IPEGHFGLLN WNGDMVFQNT KFALLDDTTA PLIDNITVRS DRGNVEKQGQ 350
    FFSEEPLHIQ YVSNDASQVS LDIAKHNPAA TVTVEDKTGR VYTDPSHLPV 400
    NVGANYFTVK STVIDSFGRT VTLTYRINVH RRQNDEVYYN ELYRDQYHYS 450
    VKDGWANDPN GLVYYNGVYH LFHQFYDDTK WGPMHWAHAT STDLIHWKEE 500
    PIAFYPDSNG YMFSGCVVVD EHNSSGLFKT AKGGLVAIIT ANGNGQRMEL 550
    AYSEDEGKTW QKYDRIVADW SNDPLQNQDF RDPKVFHWNN QWFMVLAGGP 600
    LRIYSSNNLK DWKVESTYPD LHTECPDMYP IVANDGVLKW VLSRGGRFYK 650
    VGDFKQVDGK WTFIADDAYK DKDQVMNFGK DSYAAMTYYV HDFGTETRPT 700
    IPKLTEVNWM NTWEDYCNLV ADTVGQDFNG TFNLNLDLGL INENGQYILT 750
    QTPVKAYDSL RDVNTALHFK DVTVDANNTL LKDFKGDSYE IVSHFRPDEK 800
    TTKVGFNLRV GNGQATKVIY DLQTETLSID RSQSGTILSA AFAKVNSQHV 850
    TKNADGSIDL HIYVDRASVE VFSKNNTVAG ANQIFPNPEA VGASIIVEGG 900
    KAQADISVYQ MKTIWTDKKD TAKPVAMNTT TAKELALQVG QSQDLQVYLA 950
    PASVRQDVEW TISDPSLVRT SQKGNVLHLT AVKKGKLTIT AISKENPSLS 1000
    KTFTISITLN NFKTNLKGLQ SVTGKWYVDD ETLYDSNTSS NDYYMASQKP 1050
    GFKEYDYDID LKYQRGLINL FVASGNIDPS QAYSVQFGDS ETVRLYRFAG 1100
    DTIAEANMGK RINDDQYHHI KVTKTKNSII ISVDGQEVMS HNFDQVDSYF 1150
    NDAYVGLGLW DGAVEFQNFF VTDHATTPKP DSDPTPQPDA PEALAQEREL 1200
    IDPATGVRVI LQKGELASIV RVKVSHIETN DAHTPAVLNA KDYDLFNITP 1250
    IDKNEKVVAI TKPATVLLPI DAGKVVDKVV YLPNTDKEEN LPFTIVSLTD 1300
    SNGKKQSYVR FTAEHFSEYG LVYQAENQTN LKSKEKQDNV AISYPLNLEQ 1350
    EVKVSSISRK YAANKTADVN SVQQTEPSVM SSSPKATLPD TGDHKTDLSQ 1400
    LGVLAMIGSF LVEIAGYFKK RKD 1423
    Length:1,423
    Mass (Da):158,660
    Last modified:November 28, 2002 - v2
    Checksum:i03FF85E42535ABCA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti78 – 781G → E in AAA26889. (PubMed:1398976)Curated
    Sequence conflicti280 – 2801I → V in AAA26889. (PubMed:1398976)Curated
    Sequence conflicti942 – 9421S → T in AAA26889. (PubMed:1398976)Curated
    Sequence conflicti1002 – 10021T → I in AAA26889. (PubMed:1398976)Curated
    Sequence conflicti1290 – 12901N → S in AAA26889. (PubMed:1398976)Curated
    Sequence conflicti1384 – 13841P → S in AAA26889. (PubMed:1398976)Curated
    Sequence conflicti1416 – 14161G → S in AAA26889. (PubMed:1398976)Curated
    Sequence conflicti1421 – 14211R → S in AAA26889. (PubMed:1398976)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U78296 Genomic DNA. Translation: AAA26889.1.
    AE014133 Genomic DNA. Translation: AAN57863.1.
    PIRiA49206.
    RefSeqiNP_720557.1. NC_004350.2.

    Genome annotation databases

    EnsemblBacteriaiAAN57863; AAN57863; SMU_78.
    GeneIDi1029658.
    KEGGismu:SMU_78.
    PATRICi19662427. VBIStrMut61772_0067.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U78296 Genomic DNA. Translation: AAA26889.1 .
    AE014133 Genomic DNA. Translation: AAN57863.1 .
    PIRi A49206.
    RefSeqi NP_720557.1. NC_004350.2.

    3D structure databases

    ProteinModelPortali Q03174.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 210007.SMU.78.

    Protein family/group databases

    CAZyi GH32. Glycoside Hydrolase Family 32.

    Protocols and materials databases

    DNASUi 1029658.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAN57863 ; AAN57863 ; SMU_78 .
    GeneIDi 1029658.
    KEGGi smu:SMU_78.
    PATRICi 19662427. VBIStrMut61772_0067.

    Phylogenomic databases

    eggNOGi COG1621.
    KOi K03332.
    OMAi SYAAMTY.
    OrthoDBi EOG6DJXZ4.

    Enzyme and pathway databases

    BioCyci SMUT210007:GC7Z-91-MONOMER.

    Family and domain databases

    Gene3Di 2.120.10.10. 1 hit.
    2.60.120.200. 1 hit.
    2.60.120.560. 1 hit.
    InterProi IPR003343. Big_2.
    IPR025883. Cadherin-like_b_sandwich.
    IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR001362. Glyco_hydro_32.
    IPR018053. Glyco_hydro_32_AS.
    IPR013189. Glyco_hydro_32_C.
    IPR013148. Glyco_hydro_32_N.
    IPR023296. Glyco_hydro_beta-prop.
    IPR008964. Invasin/intimin_cell_adhesion.
    IPR022263. KxYKxGKxW.
    IPR001791. Laminin_G.
    IPR011040. Sialidases.
    [Graphical view ]
    Pfami PF02368. Big_2. 1 hit.
    PF12733. Cadherin-like. 1 hit.
    PF08244. Glyco_hydro_32C. 1 hit.
    PF00251. Glyco_hydro_32N. 1 hit.
    PF02210. Laminin_G_2. 1 hit.
    [Graphical view ]
    SMARTi SM00635. BID_2. 1 hit.
    SM00640. Glyco_32. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49373. SSF49373. 1 hit.
    SSF49899. SSF49899. 2 hits.
    SSF75005. SSF75005. 1 hit.
    TIGRFAMsi TIGR03715. KxYKxGKxW. 1 hit.
    PROSITEi PS00609. GLYCOSYL_HYDROL_F32. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of the Streptococcus mutans GS-5 fruA gene encoding exo-beta-D-fructosidase."
      Burne R.A., Penders J.E.C.
      Infect. Immun. 60:4621-4632(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: GS-5.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700610 / UA159.

    Entry informationi

    Entry nameiFRUA_STRMU
    AccessioniPrimary (citable) accession number: Q03174
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 28, 2002
    Last modified: October 1, 2014
    This is version 122 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3