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Protein

Strictosidine-O-beta-D-glucosidase

Gene

SGR1

Organism
Rauvolfia serpentina (Serpentine wood) (Ophioxylon serpentinum)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Glucosidase specifically involved in alkaloid biosynthesis leading to the accumulation of several alkaloids, including ajmaline, an important plant-derived pharmaceutical used in the therapy of heart disorders.1 Publication

Catalytic activityi

Strictosidine + H2O = D-glucose + strictosidine aglycone.1 Publication

Kineticsi

Kcat is 9.8 sec(-1) with strictosidine as substrate (at pH 5.7 and 30 degrees Celsius, PubMed:17890378).

  1. KM=90 µM for strictosidine (at pH 5.7 and 30 degrees Celsius, PubMed:17890378)2 Publications
  2. KM=120 µM for strictosidine2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei57 – 571Substrate1 Publication
    Binding sitei161 – 1611Substrate1 Publication
    Active sitei207 – 2071Proton donor
    Binding sitei345 – 3451SubstrateBy similarity
    Binding sitei388 – 3881Substrate1 Publication
    Sitei388 – 3881Controls the gate shape and acceptance of substrates
    Active sitei416 – 4161Nucleophile
    Binding sitei465 – 4651Substrate1 Publication
    Binding sitei481 – 4811Substrate1 Publication

    GO - Molecular functioni

    • strictosidine beta-glucosidase activity Source: UniProtKB

    GO - Biological processi

    • alkaloid biosynthetic process Source: UniProtKB
    • carbohydrate metabolic process Source: InterPro
    • metabolic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Alkaloid metabolism

    Enzyme and pathway databases

    BRENDAi3.2.1.105. 5309.

    Protein family/group databases

    CAZyiGH1. Glycoside Hydrolase Family 1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Strictosidine-O-beta-D-glucosidase (EC:3.2.1.105)
    Gene namesi
    Name:SGR1
    OrganismiRauvolfia serpentina (Serpentine wood) (Ophioxylon serpentinum)
    Taxonomic identifieri4060 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsGentianalesApocynaceaeRauvolfioideaeVinceaeRauvolfiinaeRauvolfia

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi161 – 1611H → L or N: Loss of activity. 1 Publication
    Mutagenesisi207 – 2071E → D or Q: Loss of activity. 1 Publication
    Mutagenesisi373 – 3731F → T: Reduced affinity but increased activity. 1 Publication
    Mutagenesisi386 – 3861G → S: Reduced affinity and activity. 1 Publication
    Mutagenesisi388 – 3881W → A: Loss of activity and reduced affinity. 1 Publication
    Mutagenesisi416 – 4161E → D or Q: Loss of activity. 1 Publication
    Mutagenesisi481 – 4811Y → F: Reduced affinity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 532532Strictosidine-O-beta-D-glucosidasePRO_0000418401Add
    BLAST

    Structurei

    Secondary structure

    1
    532
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi40 – 423Combined sources
    Beta strandi48 – 525Combined sources
    Helixi55 – 584Combined sources
    Helixi71 – 788Combined sources
    Helixi80 – 823Combined sources
    Beta strandi89 – 913Combined sources
    Helixi95 – 10915Combined sources
    Beta strandi112 – 1176Combined sources
    Helixi120 – 1234Combined sources
    Beta strandi127 – 1293Combined sources
    Helixi135 – 15016Combined sources
    Beta strandi154 – 1629Combined sources
    Helixi166 – 1727Combined sources
    Helixi174 – 1763Combined sources
    Helixi180 – 19516Combined sources
    Helixi196 – 1983Combined sources
    Beta strandi200 – 2067Combined sources
    Helixi208 – 2169Combined sources
    Beta strandi230 – 2323Combined sources
    Turni234 – 2363Combined sources
    Helixi237 – 25923Combined sources
    Helixi261 – 2644Combined sources
    Beta strandi267 – 2737Combined sources
    Beta strandi276 – 2838Combined sources
    Helixi284 – 29714Combined sources
    Helixi299 – 3024Combined sources
    Helixi304 – 3074Combined sources
    Helixi312 – 3187Combined sources
    Helixi319 – 3213Combined sources
    Helixi327 – 3337Combined sources
    Beta strandi340 – 3434Combined sources
    Beta strandi347 – 3526Combined sources
    Helixi363 – 3664Combined sources
    Beta strandi369 – 3779Combined sources
    Beta strandi379 – 3835Combined sources
    Helixi393 – 40715Combined sources
    Beta strandi412 – 4176Combined sources
    Beta strandi425 – 4273Combined sources
    Helixi429 – 4324Combined sources
    Helixi436 – 45419Combined sources
    Beta strandi459 – 4657Combined sources
    Helixi473 – 4753Combined sources
    Beta strandi478 – 4803Combined sources
    Beta strandi483 – 4864Combined sources
    Turni488 – 4903Combined sources
    Beta strandi493 – 4953Combined sources
    Helixi497 – 50711Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2JF6X-ray2.82A/B1-532[»]
    2JF7X-ray2.48A/B1-532[»]
    3ZJ7X-ray2.50A/B1-532[»]
    3ZJ8X-ray3.01A/B1-532[»]
    ProteinModelPortaliQ8GU20.
    SMRiQ8GU20. Positions 37-507.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8GU20.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni206 – 2072Substrate binding
    Regioni472 – 4732Substrate binding

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 1 family.Curated

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001360. Glyco_hydro_1.
    IPR033132. Glyco_hydro_1_N_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PANTHERiPTHR10353. PTHR10353. 1 hit.
    PfamiPF00232. Glyco_hydro_1. 1 hit.
    [Graphical view]
    PRINTSiPR00131. GLHYDRLASE1.
    SUPFAMiSSF51445. SSF51445. 1 hit.
    PROSITEiPS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8GU20-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MDNTQAEPLV VAIVPKPNAS TEHTNSHLIP VTRSKIVVHR RDFPQDFIFG
    60 70 80 90 100
    AGGSAYQCEG AYNEGNRGPS IWDTFTQRSP AKISDGSNGN QAINCYHMYK
    110 120 130 140 150
    EDIKIMKQTG LESYRFSISW SRVLPGGRLA AGVNKDGVKF YHDFIDELLA
    160 170 180 190 200
    NGIKPSVTLF HWDLPQALED EYGGFLSHRI VDDFCEYAEF CFWEFGDKIK
    210 220 230 240 250
    YWTTFNEPHT FAVNGYALGE FAPGRGGKGD EGDPAIEPYV VTHNILLAHK
    260 270 280 290 300
    AAVEEYRNKF QKCQEGEIGI VLNSMWMEPL SDVQADIDAQ KRALDFMLGW
    310 320 330 340 350
    FLEPLTTGDY PKSMRELVKG RLPKFSADDS EKLKGCYDFI GMNYYTATYV
    360 370 380 390 400
    TNAVKSNSEK LSYETDDQVT KTFERNQKPI GHALYGGWQH VVPWGLYKLL
    410 420 430 440 450
    VYTKETYHVP VLYVTESGMV EENKTKILLS EARRDAERTD YHQKHLASVR
    460 470 480 490 500
    DAIDDGVNVK GYFVWSFFDN FEWNLGYICR YGIIHVDYKS FERYPKESAI
    510 520 530
    WYKNFIAGKS TTSPAKRRRE EAQVELVKRQ KT
    Length:532
    Mass (Da):60,881
    Last modified:March 1, 2003 - v1
    Checksum:iFC65D93E90212710
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AJ302044 mRNA. Translation: CAC83098.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AJ302044 mRNA. Translation: CAC83098.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2JF6X-ray2.82A/B1-532[»]
    2JF7X-ray2.48A/B1-532[»]
    3ZJ7X-ray2.50A/B1-532[»]
    3ZJ8X-ray3.01A/B1-532[»]
    ProteinModelPortaliQ8GU20.
    SMRiQ8GU20. Positions 37-507.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein family/group databases

    CAZyiGH1. Glycoside Hydrolase Family 1.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    BRENDAi3.2.1.105. 5309.

    Miscellaneous databases

    EvolutionaryTraceiQ8GU20.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001360. Glyco_hydro_1.
    IPR033132. Glyco_hydro_1_N_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PANTHERiPTHR10353. PTHR10353. 1 hit.
    PfamiPF00232. Glyco_hydro_1. 1 hit.
    [Graphical view]
    PRINTSiPR00131. GLHYDRLASE1.
    SUPFAMiSSF51445. SSF51445. 1 hit.
    PROSITEiPS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiSG1_RAUSE
    AccessioniPrimary (citable) accession number: Q8GU20
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 5, 2012
    Last sequence update: March 1, 2003
    Last modified: March 16, 2016
    This is version 59 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. 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.