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Protein

Fructan beta-fructosidase

Gene

fruA

Organism
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Active sitei458PROSITE-ProRule annotation1
Binding sitei474SubstrateBy similarity1
Binding sitei783SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosidase, Hydrolase

Enzyme and pathway databases

BioCyciSMUT210007:G1FZX-91-MONOMER

Protein family/group databases

CAZyiCBM66 Carbohydrate-Binding Module Family 66
GH32 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
Proteomesi
  • UP000002512 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cell wall, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 39Sequence analysisAdd BLAST39
ChainiPRO_000003340640 – 1391Fructan beta-fructosidaseAdd BLAST1352
PropeptideiPRO_00000334071392 – 1423Removed by sortaseSequence analysisAdd BLAST32

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1391Pentaglycyl murein peptidoglycan amidated threonineSequence analysis1

Keywords - PTMi

Peptidoglycan-anchor

Proteomic databases

PRIDEiQ03174

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)DescriptionActionsGraphical viewLength
Regioni455 – 458Substrate bindingBy similarity4
Regioni513 – 514Substrate bindingBy similarity2
Regioni581 – 582Substrate bindingBy similarity2
Regioni867 – 871Involved in binding of sugars with beta-(2,6) linkages or binding of molecular weight fructansBy similarity5

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1388 – 1392LPXTG sorting signalSequence analysis5

Sequence similaritiesi

Belongs to the glycosyl hydrolase 32 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105D7K Bacteria
COG1621 LUCA
KOiK03332
OMAiFYDDTKW

Family and domain databases

Gene3Di2.115.10.20, 1 hit
InterProiView protein in InterPro
IPR003343 Big_2
IPR025883 Cadherin-like_b_sandwich
IPR013320 ConA-like_dom_sf
IPR001362 Glyco_hydro_32
IPR018053 Glyco_hydro_32_AS
IPR013189 Glyco_hydro_32_C
IPR013148 Glyco_hydro_32_N
IPR023296 Glyco_hydro_beta-prop_sf
IPR008964 Invasin/intimin_cell_adhesion
IPR022263 KxYKxGKxW
IPR001791 Laminin_G
PfamiView protein in Pfam
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
SMARTiView protein in SMART
SM00635 BID_2, 1 hit
SM00640 Glyco_32, 1 hit
SUPFAMiSSF49373 SSF49373, 1 hit
SSF49899 SSF49899, 2 hits
SSF75005 SSF75005, 1 hit
TIGRFAMsiTIGR03715 KxYKxGKxW, 1 hit
PROSITEiView protein in PROSITE
PS00609 GLYCOSYL_HYDROL_F32, 1 hit

Sequencei

Sequence statusi: Complete.

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

Q03174-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEEETVCKNW FMRKSGKSWI FGCAVFFVLG LATALPVAAE EISQTTAADT
60 70 80 90 100
AVTEVRTEDS SQTSSQETAV TETTQSEGTA SKQLTTPAVA DQTTEPTDNE
110 120 130 140 150
PISSSDGASS PYQVTDTTEP QQTLTPADSE PQAKADVQQA AAPKKEEINP
160 170 180 190 200
VTNLEDMSHD TNGTWEVRED GIHSNAIGKG DSFLYSQSSG KNFVYATDVT
210 220 230 240 250
FKQNSGAAAL VFRSNNDSNN KNMYAVNVDI GGHKAKFWRW VDNKDIQLID
260 270 280 290 300
ERDVVPTADN RYTLKVVAVN NWISYYVNDI LMASTGDYVL QKADKGQNTV
310 320 330 340 350
IPEGHFGLLN WNGDMVFQNT KFALLDDTTA PLIDNITVRS DRGNVEKQGQ
360 370 380 390 400
FFSEEPLHIQ YVSNDASQVS LDIAKHNPAA TVTVEDKTGR VYTDPSHLPV
410 420 430 440 450
NVGANYFTVK STVIDSFGRT VTLTYRINVH RRQNDEVYYN ELYRDQYHYS
460 470 480 490 500
VKDGWANDPN GLVYYNGVYH LFHQFYDDTK WGPMHWAHAT STDLIHWKEE
510 520 530 540 550
PIAFYPDSNG YMFSGCVVVD EHNSSGLFKT AKGGLVAIIT ANGNGQRMEL
560 570 580 590 600
AYSEDEGKTW QKYDRIVADW SNDPLQNQDF RDPKVFHWNN QWFMVLAGGP
610 620 630 640 650
LRIYSSNNLK DWKVESTYPD LHTECPDMYP IVANDGVLKW VLSRGGRFYK
660 670 680 690 700
VGDFKQVDGK WTFIADDAYK DKDQVMNFGK DSYAAMTYYV HDFGTETRPT
710 720 730 740 750
IPKLTEVNWM NTWEDYCNLV ADTVGQDFNG TFNLNLDLGL INENGQYILT
760 770 780 790 800
QTPVKAYDSL RDVNTALHFK DVTVDANNTL LKDFKGDSYE IVSHFRPDEK
810 820 830 840 850
TTKVGFNLRV GNGQATKVIY DLQTETLSID RSQSGTILSA AFAKVNSQHV
860 870 880 890 900
TKNADGSIDL HIYVDRASVE VFSKNNTVAG ANQIFPNPEA VGASIIVEGG
910 920 930 940 950
KAQADISVYQ MKTIWTDKKD TAKPVAMNTT TAKELALQVG QSQDLQVYLA
960 970 980 990 1000
PASVRQDVEW TISDPSLVRT SQKGNVLHLT AVKKGKLTIT AISKENPSLS
1010 1020 1030 1040 1050
KTFTISITLN NFKTNLKGLQ SVTGKWYVDD ETLYDSNTSS NDYYMASQKP
1060 1070 1080 1090 1100
GFKEYDYDID LKYQRGLINL FVASGNIDPS QAYSVQFGDS ETVRLYRFAG
1110 1120 1130 1140 1150
DTIAEANMGK RINDDQYHHI KVTKTKNSII ISVDGQEVMS HNFDQVDSYF
1160 1170 1180 1190 1200
NDAYVGLGLW DGAVEFQNFF VTDHATTPKP DSDPTPQPDA PEALAQEREL
1210 1220 1230 1240 1250
IDPATGVRVI LQKGELASIV RVKVSHIETN DAHTPAVLNA KDYDLFNITP
1260 1270 1280 1290 1300
IDKNEKVVAI TKPATVLLPI DAGKVVDKVV YLPNTDKEEN LPFTIVSLTD
1310 1320 1330 1340 1350
SNGKKQSYVR FTAEHFSEYG LVYQAENQTN LKSKEKQDNV AISYPLNLEQ
1360 1370 1380 1390 1400
EVKVSSISRK YAANKTADVN SVQQTEPSVM SSSPKATLPD TGDHKTDLSQ
1410 1420
LGVLAMIGSF LVEIAGYFKK RKD
Length:1,423
Mass (Da):158,660
Last modified:November 28, 2002 - v2
Checksum:i03FF85E42535ABCA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti78G → E in AAA26889 (PubMed:1398976).Curated1
Sequence conflicti280I → V in AAA26889 (PubMed:1398976).Curated1
Sequence conflicti942S → T in AAA26889 (PubMed:1398976).Curated1
Sequence conflicti1002T → I in AAA26889 (PubMed:1398976).Curated1
Sequence conflicti1290N → S in AAA26889 (PubMed:1398976).Curated1
Sequence conflicti1384P → S in AAA26889 (PubMed:1398976).Curated1
Sequence conflicti1416G → S in AAA26889 (PubMed:1398976).Curated1
Sequence conflicti1421R → S in AAA26889 (PubMed:1398976).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U78296 Genomic DNA Translation: AAA26889.1
AE014133 Genomic DNA Translation: AAN57863.1
PIRiA49206
RefSeqiNP_720557.1, NC_004350.2
WP_002263413.1, NC_004350.2

Genome annotation databases

EnsemblBacteriaiAAN57863; AAN57863; SMU_78
GeneIDi1029658
KEGGismu:SMU_78
PATRICifig|210007.7.peg.67

Similar proteinsi

Entry informationi

Entry nameiFRUA_STRMU
AccessioniPrimary (citable) accession number: Q03174
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 28, 2002
Last modified: May 23, 2018
This is version 139 of the entry and version 2 of the sequence. See 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

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