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Q9SPP9

- RG1_RAUSE

UniProt

Q9SPP9 - RG1_RAUSE

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Protein
Raucaffricine-O-beta-D-glucosidase
Gene
RG, VGT
Organism
Rauvolfia serpentina (Serpentwood) (Devilpepper)
Status
Reviewed - 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 treatment of heart disorders.1 Publication

Catalytic activityi

Raucaffricine + H2O = D-glucose + vomilenine.1 Publication
UDP-glucose + vomilenine = UDP + raucaffricine.1 Publication

Kineticsi

  1. KM=1.3 mM for raucaffricine (at pH 5 and 28 degrees Celsius, 1 Publication and 1 Publication)2 Publications
  2. KM=1.8 mM for strictosidine (at pH 5 and 28 degrees Celsius, 1 Publication and 1 Publication)

Vmax=0.5 nmol/sec/µg enzyme with raucaffricine as substrate (at pH 5 and 28 degrees Celsius, 1 Publication

and 1 Publication)

Vmax=2.6 pmol/sec/µg enzyme with strictosidine as substrate (at pH 5 and 28 degrees Celsius, 1 Publication

and 1 Publication)

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei36 – 361Substrate
Binding sitei140 – 1401Substrate By similarity
Active sitei186 – 1861Proton donor
Binding sitei193 – 1931Substrate
Binding sitei347 – 3471Substrate By similarity
Sitei390 – 3901Directs the conformation of W-392
Binding sitei392 – 3921Substrate
Sitei392 – 3921Control the gate shape and acceptance of substrates
Active sitei420 – 4201Nucleophile
Binding sitei420 – 4201Substrate
Binding sitei469 – 4691Substrate

GO - Molecular functioni

  1. raucaffricine beta-glucosidase activity Source: UniProtKB
  2. vomilenine glucosyltransferase activity Source: UniProtKB

GO - Biological processi

  1. alkaloid biosynthetic process Source: UniProtKB
  2. carbohydrate metabolic process Source: InterPro
  3. metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase, Transferase

Keywords - Biological processi

Alkaloid metabolism

Enzyme and pathway databases

BRENDAi3.2.1.125. 257570.

Protein family/group databases

CAZyiGH1. Glycoside Hydrolase Family 1.

Names & Taxonomyi

Protein namesi
Recommended name:
Raucaffricine-O-beta-D-glucosidase (EC:3.2.1.125)
Short name:
Raucaffricine beta-glucosidase
Short name:
RsRG
Alternative name(s):
Vomilenine glucosyltransferase (EC:2.4.1.219)
Short name:
RsVGT
Gene namesi
Name:RG
Synonyms:VGT
OrganismiRauvolfia serpentina (Serpentwood) (Devilpepper)
Taxonomic identifieri4060 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsGentianalesApocynaceaeRauvolfioideaeVinceaeRauvolfiinaeRauvolfia

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi186 – 1861E → D or Q: Loss of activity. 1 Publication
Mutagenesisi189 – 1891T → A: Reduced activity. 1 Publication
Mutagenesisi193 – 1931H → A: Reduced activity. 1 Publication
Mutagenesisi200 – 2001Y → A: Loss of activity. 1 Publication
Mutagenesisi390 – 3901S → G: Reduced activity. 1 Publication
Mutagenesisi392 – 3921W → A: Loss of activity. 1 Publication
Mutagenesisi420 – 4201E → Q: Loss of activity. 1 Publication
Mutagenesisi476 – 4761E → A or L: Loss of activity. 1 Publication
Mutagenesisi485 – 4851F → Y: Reduced activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 540540Raucaffricine-O-beta-D-glucosidase
PRO_0000418400Add
BLAST

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi14 – 163
Helixi19 – 213
Beta strandi27 – 315
Helixi34 – 374
Helixi50 – 578
Helixi59 – 613
Helixi63 – 653
Turni68 – 725
Helixi74 – 8815
Beta strandi91 – 966
Helixi99 – 1024
Helixi108 – 1103
Helixi114 – 12916
Beta strandi133 – 1419
Helixi145 – 1517
Helixi153 – 1553
Helixi159 – 17416
Turni175 – 1773
Beta strandi180 – 1856
Helixi187 – 1959
Turni235 – 2373
Helixi238 – 26023
Helixi262 – 2654
Beta strandi268 – 28215
Helixi286 – 29914
Helixi301 – 3044
Helixi306 – 3094
Helixi314 – 3207
Helixi321 – 3233
Helixi329 – 3357
Beta strandi340 – 35415
Helixi367 – 3704
Beta strandi373 – 3764
Beta strandi378 – 3814
Beta strandi382 – 3854
Helixi398 – 41114
Beta strandi414 – 4218
Helixi433 – 4364
Helixi440 – 45819
Beta strandi463 – 4697
Helixi477 – 4793
Beta strandi482 – 4843
Beta strandi487 – 4904
Turni492 – 4965
Beta strandi498 – 5003
Helixi502 – 51110

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3U57X-ray2.43A/B1-513[»]
3U5UX-ray2.20A/B1-513[»]
3U5YX-ray2.30A/B1-513[»]
3ZJ6X-ray2.40A/B1-540[»]
4A3YX-ray2.15A/B1-540[»]
4ATDX-ray2.10A/B1-513[»]
4ATLX-ray2.52A/B1-513[»]
4EK7X-ray2.30A/B1-513[»]
ProteinModelPortaliQ9SPP9.
SMRiQ9SPP9. Positions 17-508.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni185 – 1862Substrate binding
Regioni476 – 4772Substrate binding

Sequence similaritiesi

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
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.

Q9SPP9-1 [UniParc]FASTAAdd to Basket

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MATQSSAVID SNDATRISRS DFPADFIMGT GSSAYQIEGG ARDGGRGPSI    50
WDTFTHRRPD MIRGGTNGDV AVDSYHLYKE DVNILKNLGL DAYRFSISWS 100
RVLPGGRLSG GVNKEGINYY NNLIDGLLAN GIKPFVTLFH WDVPQALEDE 150
YGGFLSPRIV DDFCEYAELC FWEFGDRVKH WMTLNEPWTF SVHGYATGLY 200
APGRGRTSPE HVNHPTVQHR CSTVAPQCIC STGNPGTEPY WVTHHLLLAH 250
AAAVELYKNK FQRGQEGQIG ISHATQWMEP WDENSASDVE AAARALDFML 300
GWFMEPITSG DYPKSMKKFV GSRLPKFSPE QSKMLKGSYD FVGLNYYTAS 350
YVTNASTNSS GSNNFSYNTD IHVTYETDRN GVPIGPQSGS DWLLIYPEGI 400
RKILVYTKKT YNVPLIYVTE NGVDDVKNTN LTLSEARKDS MRLKYLQDHI 450
FNVRQAMNDG VNVKGYFAWS LLDNFEWGEG YGVRFGIIHI DYNDNFARYP 500
KDSAVWLMNS FHKNISKLPA VKRSIREDDE EQVSSKRLRK 540
Length:540
Mass (Da):60,934
Last modified:May 1, 2000 - v1
Checksum:i543A24654A4D5E7D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF149311 mRNA. Translation: AAF03675.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF149311 mRNA. Translation: AAF03675.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3U57 X-ray 2.43 A/B 1-513 [» ]
3U5U X-ray 2.20 A/B 1-513 [» ]
3U5Y X-ray 2.30 A/B 1-513 [» ]
3ZJ6 X-ray 2.40 A/B 1-540 [» ]
4A3Y X-ray 2.15 A/B 1-540 [» ]
4ATD X-ray 2.10 A/B 1-513 [» ]
4ATL X-ray 2.52 A/B 1-513 [» ]
4EK7 X-ray 2.30 A/B 1-513 [» ]
ProteinModelPortali Q9SPP9.
SMRi Q9SPP9. Positions 17-508.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH1. Glycoside Hydrolase Family 1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BRENDAi 3.2.1.125. 257570.

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
InterProi IPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
PANTHERi PTHR10353. PTHR10353. 1 hit.
Pfami PF00232. Glyco_hydro_1. 1 hit.
[Graphical view ]
PRINTSi PR00131. GLHYDRLASE1.
SUPFAMi SSF51445. SSF51445. 1 hit.
PROSITEi PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Molecular cloning and functional bacterial expression of a plant glucosidase specifically involved in alkaloid biosynthesis."
    Warzecha H., Gerasimenko I., Kutchan T.M., Stoeckigt J.
    Phytochemistry 54:657-666(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 80-111; 319-326; 403-408; 410-425 AND 428-438, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    Strain: BENTH. ex KURZ.
    Tissue: Protoplast.
  2. "Structures of alkaloid biosynthetic glucosidases decode substrate specificity."
    Xia L., Ruppert M., Wang M., Panjikar S., Lin H., Rajendran C., Barleben L., Stoeckigt J.
    ACS Chem. Biol. 7:226-234(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 1-513 IN COMPLEX WITH SUBSTRATE, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLU-186; THR-189; HIS-193; TYR-200; SER-390; TRP-392; GLU-420; GLU-476 AND PHE-485.

Entry informationi

Entry nameiRG1_RAUSE
AccessioniPrimary (citable) accession number: Q9SPP9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 11, 2013
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 70 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, Direct protein sequencing

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

External Data

Dasty 3

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