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Protein

Galactinol--sucrose galactosyltransferase

Gene

RFS

Organism
Pisum sativum (Garden pea)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Transglycosidase operating by a ping-pong reaction mechanism. Involved in the synthesis of raffinose, a major soluble carbohydrate in seeds, roots and tubers. Able to utilize D-ononitol and D-pinitol as acceptors. May also act as a glycoside hydrolase.1 Publication

Catalytic activityi

Alpha-D-galactosyl-(1->3)-1D-myo-inositol + sucrose = myo-inositol + raffinose.1 Publication

Enzyme regulationi

Inhibited by 1-deoxygalactonojirimycin. Not inhibited by stachyose. Strong inhibition of the hydrolytic activity by sucrose.1 Publication

Kineticsi

partially purified enzyme.

  1. KM=7.3 mM for galactinol for the raffinose synthesis activity1 Publication
  2. KM=22.9 mM for sucrose for the raffinose synthesis activity1 Publication
  3. KM=1.0 mM for galactinol for the galactinol hydrolysis activity1 Publication

Vmax=199.2 pmol/sec/mg enzyme for the raffinose synthesis activity1 Publication

Vmax=27.3 pmol/sec/mg enzyme for the galactinol hydrolysis activity1 Publication

pH dependencei

Optimum pH is 7.0.1 Publication

GO - Molecular functioni

  1. galactinol-sucrose galactosyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. carbohydrate metabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Carbohydrate metabolism

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-12496.
BRENDAi2.4.1.82. 4872.

Protein family/group databases

CAZyiGH36. Glycoside Hydrolase Family 36.

Names & Taxonomyi

Protein namesi
Recommended name:
Galactinol--sucrose galactosyltransferase (EC:2.4.1.82)
Alternative name(s):
Raffinose synthase
Gene namesi
Name:RFS
OrganismiPisum sativum (Garden pea)
Taxonomic identifieri3888 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 798798Galactinol--sucrose galactosyltransferasePRO_0000389254Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ8VWN6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi53 – 597Poly-Thr
Compositional biasi75 – 784Poly-Asn
Compositional biasi281 – 2844Poly-Asp

Sequence similaritiesi

Belongs to the glycosyl hydrolases 36 family.Curated

Family and domain databases

Gene3Di3.20.20.70. 2 hits.
InterProiIPR013785. Aldolase_TIM.
IPR017853. Glycoside_hydrolase_SF.
IPR008811. Glycosyl_hydrolases_36.
[Graphical view]
PfamiPF05691. Raffinose_syn. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 3 hits.

Sequencei

Sequence statusi: Complete.

Q8VWN6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAPPSITKTA TQQDVISTVD IGNSPLLSIS LDQSRNFLVN GHPFLTQVPP
60 70 80 90 100
NITTTTTSTP SPFLDFKSNK DTIANNNNTL QQQGCFVGFN TTEAKSHHVV
110 120 130 140 150
PLGKLKGIKF TSIFRFKVWW TTHWVGTNGH ELQHETQILI LDKNISLGRP
160 170 180 190 200
YVLLLPILEN SFRTSLQPGL NDYVDMSVES GSTHVTGSTF KACLYLHLSN
210 220 230 240 250
DPYRLVKEAV KVIQTKLGTF KTLEEKTPPS IIEKFGWCTW DAFYLKVHPK
260 270 280 290 300
GVWEGVKALT DGGCPPGFVI IDDGWQSISH DDDDPVTERD GMNRTSAGEQ
310 320 330 340 350
MPCRLIKYEE NYKFREYENG DNGGKKGLVG FVRDLKEEFR SVESVYVWHA
360 370 380 390 400
LCGYWGGVRP KVCGMPEAKV VVPKLSPGVK MTMEDLAVDK IVENGVGLVP
410 420 430 440 450
PNLAQEMFDG IHSHLESAGI DGVKVDVIHL LELLSEEYGG RVELAKAYYK
460 470 480 490 500
ALTSSVNKHF KGNGVIASME HCNDFFLLGT EAISLGRVGD DFWCCDPSGD
510 520 530 540 550
PNGTYWLQGC HMVHCAYNSL WMGNFIHPDW DMFQSTHPCA EFHAASRAIS
560 570 580 590 600
GGPVYVSDCV GNHNFKLLKS FVLPDGSILR CQHYALPTRD CLFEDPLHNG
610 620 630 640 650
KTMLKIWNLN KYAGVLGLFN CQGGGWCPET RRNKSASEFS HAVTCYASPE
660 670 680 690 700
DIEWCNGKTP MDIKGVDVFA VYFFKEKKLS LMKCSDRLEV SLEPFSFELM
710 720 730 740 750
TVSPLKVFSK RLIQFAPIGL VNMLNSGGAV QSLEFDDSAS LVKIGVRGCG
760 770 780 790
ELSVFASEKP VCCKIDGVSV EFDYEDKMVR VQILWPGSST LSLVEFLF
Length:798
Mass (Da):88,717
Last modified:March 1, 2002 - v1
Checksum:i8D3F3ED5BF8617B7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ426475 mRNA. Translation: CAD20127.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ426475 mRNA. Translation: CAD20127.2.

3D structure databases

ProteinModelPortaliQ8VWN6.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH36. Glycoside Hydrolase Family 36.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-12496.
BRENDAi2.4.1.82. 4872.

Family and domain databases

Gene3Di3.20.20.70. 2 hits.
InterProiIPR013785. Aldolase_TIM.
IPR017853. Glycoside_hydrolase_SF.
IPR008811. Glycosyl_hydrolases_36.
[Graphical view]
PfamiPF05691. Raffinose_syn. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 3 hits.
ProtoNetiSearch...

Publicationsi

  1. "Functional expression of a cDNA encoding pea (Pisum sativum L.) raffinose synthase, partial purification of the enzyme from maturing seeds, and steady-state kinetic analysis of raffinose synthesis."
    Peterbauer T., Mach L., Mucha J., Richter A.
    Planta 215:839-846(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
    Strain: cv. Kelvedon Wonder.
    Tissue: Seed.

Entry informationi

Entry nameiRFS_PEA
AccessioniPrimary (citable) accession number: Q8VWN6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 24, 2009
Last sequence update: March 1, 2002
Last modified: October 1, 2014
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.