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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)DescriptionActionsGraphical viewLength
    Binding sitei57Substrate1 Publication1
    Binding sitei161Substrate1 Publication1
    Active sitei207Proton donor1
    Binding sitei345SubstrateBy similarity1
    Binding sitei388Substrate1 Publication1
    Sitei388Controls the gate shape and acceptance of substrates1
    Active sitei416Nucleophile1
    Binding sitei465Substrate1 Publication1
    Binding sitei481Substrate1 Publication1

    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

    BioCyciMetaCyc:MONOMER-12391.
    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)DescriptionActionsGraphical viewLength
    Mutagenesisi161H → L or N: Loss of activity. 1 Publication1
    Mutagenesisi207E → D or Q: Loss of activity. 1 Publication1
    Mutagenesisi373F → T: Reduced affinity but increased activity. 1 Publication1
    Mutagenesisi386G → S: Reduced affinity and activity. 1 Publication1
    Mutagenesisi388W → A: Loss of activity and reduced affinity. 1 Publication1
    Mutagenesisi416E → D or Q: Loss of activity. 1 Publication1
    Mutagenesisi481Y → F: Reduced affinity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004184011 – 532Strictosidine-O-beta-D-glucosidaseAdd BLAST532

    Structurei

    Secondary structure

    1532
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi40 – 42Combined sources3
    Beta strandi48 – 52Combined sources5
    Helixi55 – 58Combined sources4
    Helixi71 – 78Combined sources8
    Helixi80 – 82Combined sources3
    Beta strandi89 – 91Combined sources3
    Helixi95 – 109Combined sources15
    Beta strandi112 – 117Combined sources6
    Helixi120 – 123Combined sources4
    Beta strandi127 – 129Combined sources3
    Helixi135 – 150Combined sources16
    Beta strandi154 – 162Combined sources9
    Helixi166 – 172Combined sources7
    Helixi174 – 176Combined sources3
    Helixi180 – 195Combined sources16
    Helixi196 – 198Combined sources3
    Beta strandi200 – 206Combined sources7
    Helixi208 – 216Combined sources9
    Beta strandi230 – 232Combined sources3
    Turni234 – 236Combined sources3
    Helixi237 – 259Combined sources23
    Helixi261 – 264Combined sources4
    Beta strandi267 – 273Combined sources7
    Beta strandi276 – 283Combined sources8
    Helixi284 – 297Combined sources14
    Helixi299 – 302Combined sources4
    Helixi304 – 307Combined sources4
    Helixi312 – 318Combined sources7
    Helixi319 – 321Combined sources3
    Helixi327 – 333Combined sources7
    Beta strandi340 – 343Combined sources4
    Beta strandi347 – 352Combined sources6
    Helixi363 – 366Combined sources4
    Beta strandi369 – 377Combined sources9
    Beta strandi379 – 383Combined sources5
    Helixi393 – 407Combined sources15
    Beta strandi412 – 417Combined sources6
    Beta strandi425 – 427Combined sources3
    Helixi429 – 432Combined sources4
    Helixi436 – 454Combined sources19
    Beta strandi459 – 465Combined sources7
    Helixi473 – 475Combined sources3
    Beta strandi478 – 480Combined sources3
    Beta strandi483 – 486Combined sources4
    Turni488 – 490Combined sources3
    Beta strandi493 – 495Combined sources3
    Helixi497 – 507Combined sources11

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8GU20.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni206 – 207Substrate binding2
    Regioni472 – 473Substrate binding2

    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
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein family/group databases

    CAZyiGH1. Glycoside Hydrolase Family 1.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-12391.
    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: November 2, 2016
    This is version 61 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.