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Q9SPP9

- RG1_RAUSE

UniProt

Q9SPP9 - RG1_RAUSE

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Protein

Raucaffricine-O-beta-D-glucosidase

Gene

RG

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, PubMed:22004291, PubMed:10975500)2 Publications
  2. KM=1.8 mM for strictosidine (at pH 5 and 28 degrees Celsius, PubMed:22004291, PubMed:10975500)2 Publications

Vmax=0.5 nmol/sec/µg enzyme with raucaffricine as substrate (at pH 5 and 28 degrees Celsius, PubMed:22004291, PubMed:10975500)2 Publications

Vmax=2.6 pmol/sec/µg enzyme with strictosidine as substrate (at pH 5 and 28 degrees Celsius, PubMed:22004291, PubMed:10975500)2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei36 – 361Substrate1 Publication
Binding sitei140 – 1401SubstrateBy similarity
Active sitei186 – 1861Proton donor
Binding sitei193 – 1931Substrate1 Publication
Binding sitei347 – 3471SubstrateBy similarity
Sitei390 – 3901Directs the conformation of W-392
Binding sitei392 – 3921Substrate1 Publication
Sitei392 – 3921Control the gate shape and acceptance of substrates
Active sitei420 – 4201Nucleophile
Binding sitei420 – 4201Substrate1 Publication
Binding sitei469 – 4691Substrate1 Publication

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-glucosidasePRO_0000418400Add
BLAST

Structurei

Secondary structure

1
540
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi14 – 163Combined sources
Helixi19 – 213Combined sources
Beta strandi27 – 315Combined sources
Helixi34 – 374Combined sources
Helixi50 – 578Combined sources
Helixi59 – 613Combined sources
Helixi63 – 653Combined sources
Turni68 – 725Combined sources
Helixi74 – 8815Combined sources
Beta strandi91 – 966Combined sources
Helixi99 – 1024Combined sources
Helixi108 – 1103Combined sources
Helixi114 – 12916Combined sources
Beta strandi133 – 1419Combined sources
Helixi145 – 1517Combined sources
Helixi153 – 1553Combined sources
Helixi159 – 17416Combined sources
Turni175 – 1773Combined sources
Beta strandi180 – 1856Combined sources
Helixi187 – 1959Combined sources
Turni235 – 2373Combined sources
Helixi238 – 26023Combined sources
Helixi262 – 2654Combined sources
Beta strandi268 – 28215Combined sources
Helixi286 – 29914Combined sources
Helixi301 – 3044Combined sources
Helixi306 – 3094Combined sources
Helixi314 – 3207Combined sources
Helixi321 – 3233Combined sources
Helixi329 – 3357Combined sources
Beta strandi340 – 35415Combined sources
Helixi367 – 3704Combined sources
Beta strandi373 – 3764Combined sources
Beta strandi378 – 3814Combined sources
Beta strandi382 – 3854Combined sources
Helixi398 – 41114Combined sources
Beta strandi414 – 4218Combined sources
Helixi433 – 4364Combined sources
Helixi440 – 45819Combined sources
Beta strandi463 – 4697Combined sources
Helixi477 – 4793Combined sources
Beta strandi482 – 4843Combined sources
Beta strandi487 – 4904Combined sources
Turni492 – 4965Combined sources
Beta strandi498 – 5003Combined sources
Helixi502 – 51110Combined sources

3D structure databases

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

Family & Domainsi

Region

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

« Hide

        10         20         30         40         50
MATQSSAVID SNDATRISRS DFPADFIMGT GSSAYQIEGG ARDGGRGPSI
60 70 80 90 100
WDTFTHRRPD MIRGGTNGDV AVDSYHLYKE DVNILKNLGL DAYRFSISWS
110 120 130 140 150
RVLPGGRLSG GVNKEGINYY NNLIDGLLAN GIKPFVTLFH WDVPQALEDE
160 170 180 190 200
YGGFLSPRIV DDFCEYAELC FWEFGDRVKH WMTLNEPWTF SVHGYATGLY
210 220 230 240 250
APGRGRTSPE HVNHPTVQHR CSTVAPQCIC STGNPGTEPY WVTHHLLLAH
260 270 280 290 300
AAAVELYKNK FQRGQEGQIG ISHATQWMEP WDENSASDVE AAARALDFML
310 320 330 340 350
GWFMEPITSG DYPKSMKKFV GSRLPKFSPE QSKMLKGSYD FVGLNYYTAS
360 370 380 390 400
YVTNASTNSS GSNNFSYNTD IHVTYETDRN GVPIGPQSGS DWLLIYPEGI
410 420 430 440 450
RKILVYTKKT YNVPLIYVTE NGVDDVKNTN LTLSEARKDS MRLKYLQDHI
460 470 480 490 500
FNVRQAMNDG VNVKGYFAWS LLDNFEWGEG YGVRFGIIHI DYNDNFARYP
510 520 530 540
KDSAVWLMNS FHKNISKLPA VKRSIREDDE EQVSSKRLRK
Length:540
Mass (Da):60,934
Last modified:May 1, 2000 - v1
Checksum:i543A24654A4D5E7D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF149311 mRNA. Translation: AAF03675.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF149311 mRNA. Translation: AAF03675.1 .

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: October 29, 2014
This is version 72 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