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Q03174

- FRUA_STRMU

UniProt

Q03174 - FRUA_STRMU

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Protein

Fructan beta-fructosidase

Gene
fruA, SMU_78
Organism
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at transcript leveli

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 – 4581 By similarity
Binding sitei474 – 4741Substrate By similarity
Binding sitei783 – 7831Substrate By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

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

Secretedcell wall; Peptidoglycan-anchor Reviewed prediction

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell wall, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3939 Reviewed predictionAdd
BLAST
Chaini40 – 13911352Fructan beta-fructosidasePRO_0000033406Add
BLAST
Propeptidei1392 – 142332Removed by sortase Reviewed predictionPRO_0000033407Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1391 – 13911Pentaglycyl murein peptidoglycan amidated threonine Reviewed prediction

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.

Family & Domainsi

Region

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

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1388 – 13925LPXTG sorting signal Reviewed prediction

Sequence similaritiesi

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti78 – 781G → E in AAA26889. 1 Publication
Sequence conflicti280 – 2801I → V in AAA26889. 1 Publication
Sequence conflicti942 – 9421S → T in AAA26889. 1 Publication
Sequence conflicti1002 – 10021T → I in AAA26889. 1 Publication
Sequence conflicti1290 – 12901N → S in AAA26889. 1 Publication
Sequence conflicti1384 – 13841P → S in AAA26889. 1 Publication
Sequence conflicti1416 – 14161G → S in AAA26889. 1 Publication
Sequence conflicti1421 – 14211R → S in AAA26889. 1 Publication

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

« Hide 'large scale' publications
  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: May 14, 2014
This is version 121 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

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

Similar proteinsi