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Protein

Sucrose synthase 1

Gene

SUS1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Sucrose-cleaving enzyme that provides UDP-glucose and fructose for various metabolic pathways.1 Publication

Catalytic activityi

NDP-glucose + D-fructose = NDP + sucrose.

Kineticsi

  1. KM=4.37 mM for D-fructose (synthetic reaction) at pH 9.42 Publications
  2. KM=0.04 mM for UDP-glucose (synthetic reaction) at pH 9.42 Publications
  3. KM=31.58 mM for sucrose (degradative reaction) at pH 62 Publications
  4. KM=53 mM for sucrose (degradative reaction) at pH 72 Publications
  5. KM=0.08 mM for UDP (degradative reaction) at pH 62 Publications
  6. KM=0.39 mM for UDP (degradative reaction) at pH 72 Publications
  7. KM=0.17 mM for ADP (degradative reaction) at pH 72 Publications
  1. Vmax=11.14 µmol/min/mg enzyme for synthetic reaction at pH 9.42 Publications
  2. Vmax=4.68 µmol/min/mg enzyme for degradative reaction at pH 62 Publications
  3. Vmax=585 µmol/min/mg enzyme for degradative reaction at pH 72 Publications

pH dependencei

Optimum pH is 6.0-7.0 for degradative reaction and 7.0 (PubMed:22184213) or 9.0-9.5 (PubMed:17257168) for synthetic reaction.2 Publications

GO - Molecular functioni

  • sucrose synthase activity Source: UniProtKB

GO - Biological processi

  • response to cadmium ion Source: TAIR
  • response to cold Source: UniProtKB
  • response to flooding Source: TAIR
  • response to glucose Source: UniProtKB
  • response to hypoxia Source: UniProtKB
  • response to mannitol Source: UniProtKB
  • response to osmotic stress Source: TAIR
  • response to sorbitol Source: UniProtKB
  • response to sucrose Source: UniProtKB
  • response to water deprivation Source: UniProtKB
  • sucrose metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Stress response

Enzyme and pathway databases

BioCyciARA:AT5G20830-MONOMER.
MetaCyc:AT5G20830-MONOMER.
BRENDAi2.4.1.13. 399.

Protein family/group databases

CAZyiGT4. Glycosyltransferase Family 4.

Names & Taxonomyi

Protein namesi
Recommended name:
Sucrose synthase 1 (EC:2.4.1.13)
Short name:
AtSUS1
Alternative name(s):
Sucrose-UDP glucosyltransferase 1
Gene namesi
Name:SUS1
Ordered Locus Names:At5g20830
ORF Names:T1M15.230
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G20830.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: TAIR
  • plasmodesma Source: TAIR
Complete GO annotation...

Pathology & Biotechi

Biotechnological usei

A one-pot system for efficient enzymatic production of a wide range of glucosides couples the activities of two recombinant enzymes, UDP-glucose: curcumin glucosyltransferase from Catharanthus roseus (CaUGT2) and sucrose synthase from Arabidopsis thaliana (AtSUS1). UDP, a product inhibitor of UDP-glucosyltransferase, was removed from the system and used for regeneration of UDP-glucose by the second enzyme, AtSUS1. The productivity was increased several-fold and UDP-glucose initially added to the reaction mixture could be reduced to one-tenth of the normal level.1 Publication

Disruption phenotypei

No visible phenotype.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002046441 – 808Sucrose synthase 1Add BLAST808

Proteomic databases

PaxDbiP49040.
PRIDEiP49040.

PTM databases

iPTMnetiP49040.
SwissPalmiP49040.

Expressioni

Tissue specificityi

Expressed in the phloem of leaves and in roots. Detected in the whole plant but more precisely confined to the vasculature in cotyledons, mature leaves and siliques.4 Publications

Inductioni

By cold, drought and anaerobic stress. By sugar or osmoticum. By anoxia in the roots (at protein level). Up-regulated by NUC/IDD8.5 Publications

Gene expression databases

GenevisibleiP49040. AT.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

BioGridi17481. 3 interactors.
STRINGi3702.AT5G20830.1.

Structurei

Secondary structure

1808
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi16 – 18Combined sources3
Turni19 – 23Combined sources5
Helixi30 – 40Combined sources11
Beta strandi43 – 47Combined sources5
Helixi48 – 53Combined sources6
Turni54 – 58Combined sources5
Helixi61 – 63Combined sources3
Turni64 – 68Combined sources5
Helixi69 – 74Combined sources6
Beta strandi76 – 81Combined sources6
Beta strandi83 – 93Combined sources11
Beta strandi96 – 103Combined sources8
Beta strandi109 – 112Combined sources4
Helixi114 – 126Combined sources13
Beta strandi136 – 138Combined sources3
Helixi140 – 143Combined sources4
Helixi152 – 154Combined sources3
Helixi158 – 169Combined sources12
Turni170 – 172Combined sources3
Helixi174 – 186Combined sources13
Beta strandi192 – 196Combined sources5
Helixi203 – 219Combined sources17
Helixi226 – 235Combined sources10
Helixi246 – 261Combined sources16
Helixi265 – 274Combined sources10
Beta strandi280 – 284Combined sources5
Beta strandi292 – 294Combined sources3
Helixi303 – 325Combined sources23
Beta strandi333 – 339Combined sources7
Beta strandi346 – 348Combined sources3
Beta strandi351 – 355Combined sources5
Beta strandi360 – 367Combined sources8
Beta strandi369 – 371Combined sources3
Beta strandi374 – 376Combined sources3
Turni382 – 384Combined sources3
Helixi386 – 388Combined sources3
Helixi389 – 403Combined sources15
Beta strandi409 – 414Combined sources6
Helixi415 – 429Combined sources15
Beta strandi433 – 436Combined sources4
Helixi441 – 444Combined sources4
Turni446 – 451Combined sources6
Helixi452 – 459Combined sources8
Helixi461 – 474Combined sources14
Beta strandi475 – 481Combined sources7
Helixi483 – 487Combined sources5
Beta strandi490 – 492Combined sources3
Helixi497 – 499Combined sources3
Beta strandi500 – 504Combined sources5
Turni505 – 507Combined sources3
Beta strandi508 – 513Combined sources6
Beta strandi521 – 523Combined sources3
Turni530 – 532Combined sources3
Turni539 – 541Combined sources3
Helixi544 – 546Combined sources3
Helixi547 – 555Combined sources9
Beta strandi563 – 565Combined sources3
Beta strandi570 – 572Combined sources3
Beta strandi574 – 578Combined sources5
Turni583 – 586Combined sources4
Helixi587 – 596Combined sources10
Helixi598 – 603Combined sources6
Beta strandi605 – 609Combined sources5
Helixi620 – 635Combined sources16
Beta strandi639 – 645Combined sources7
Helixi651 – 663Combined sources13
Beta strandi667 – 670Combined sources4
Beta strandi675 – 677Combined sources3
Helixi679 – 686Combined sources8
Beta strandi691 – 697Combined sources7
Helixi699 – 702Combined sources4
Turni705 – 707Combined sources3
Beta strandi710 – 712Combined sources3
Helixi717 – 733Combined sources17
Helixi736 – 751Combined sources16
Helixi755 – 776Combined sources22
Turni777 – 779Combined sources3
Helixi780 – 793Combined sources14
Helixi795 – 801Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3S27X-ray2.91A/B/C/D/E/F/G/H1-808[»]
3S28X-ray2.80A/B/C/D/E/F/G/H1-808[»]
3S29X-ray2.85A/B/C/D/E/F/G/H1-808[»]
ProteinModelPortaliP49040.
SMRiP49040.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP49040.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni277 – 754GT-B glycosyltransferaseAdd BLAST478

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0853. Eukaryota.
COG0438. LUCA.
HOGENOMiHOG000240125.
InParanoidiP49040.
KOiK00695.
OMAiMANAERM.
OrthoDBiEOG0936023J.
PhylomeDBiP49040.

Family and domain databases

InterProiIPR001296. Glyco_trans_1.
IPR000368. Sucrose_synth.
IPR012820. Sucrose_synthase_pln/cyn.
[Graphical view]
PfamiPF00534. Glycos_transf_1. 1 hit.
PF00862. Sucrose_synth. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02470. sucr_synth. 1 hit.

Sequencei

Sequence statusi: Complete.

P49040-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANAERMITR VHSQRERLNE TLVSERNEVL ALLSRVEAKG KGILQQNQII
60 70 80 90 100
AEFEALPEQT RKKLEGGPFF DLLKSTQEAI VLPPWVALAV RPRPGVWEYL
110 120 130 140 150
RVNLHALVVE ELQPAEFLHF KEELVDGVKN GNFTLELDFE PFNASIPRPT
160 170 180 190 200
LHKYIGNGVD FLNRHLSAKL FHDKESLLPL LKFLRLHSHQ GKNLMLSEKI
210 220 230 240 250
QNLNTLQHTL RKAEEYLAEL KSETLYEEFE AKFEEIGLER GWGDNAERVL
260 270 280 290 300
DMIRLLLDLL EAPDPCTLET FLGRVPMVFN VVILSPHGYF AQDNVLGYPD
310 320 330 340 350
TGGQVVYILD QVRALEIEML QRIKQQGLNI KPRILILTRL LPDAVGTTCG
360 370 380 390 400
ERLERVYDSE YCDILRVPFR TEKGIVRKWI SRFEVWPYLE TYTEDAAVEL
410 420 430 440 450
SKELNGKPDL IIGNYSDGNL VASLLAHKLG VTQCTIAHAL EKTKYPDSDI
460 470 480 490 500
YWKKLDDKYH FSCQFTADIF AMNHTDFIIT STFQEIAGSK ETVGQYESHT
510 520 530 540 550
AFTLPGLYRV VHGIDVFDPK FNIVSPGADM SIYFPYTEEK RRLTKFHSEI
560 570 580 590 600
EELLYSDVEN KEHLCVLKDK KKPILFTMAR LDRVKNLSGL VEWYGKNTRL
610 620 630 640 650
RELANLVVVG GDRRKESKDN EEKAEMKKMY DLIEEYKLNG QFRWISSQMD
660 670 680 690 700
RVRNGELYRY ICDTKGAFVQ PALYEAFGLT VVEAMTCGLP TFATCKGGPA
710 720 730 740 750
EIIVHGKSGF HIDPYHGDQA ADTLADFFTK CKEDPSHWDE ISKGGLQRIE
760 770 780 790 800
EKYTWQIYSQ RLLTLTGVYG FWKHVSNLDR LEARRYLEMF YALKYRPLAQ

AVPLAQDD
Length:808
Mass (Da):92,998
Last modified:April 14, 2009 - v3
Checksum:iCDB56C6A57BD852E
GO

Sequence cautioni

The sequence BAD94975 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti61R → Q in CAA50317 (PubMed:8220487).Curated1
Sequence conflicti108V → L in CAA50317 (PubMed:8220487).Curated1
Sequence conflicti222S → P in CAA50317 (PubMed:8220487).Curated1
Sequence conflicti405N → D in CAA50317 (PubMed:8220487).Curated1
Sequence conflicti434C → QC in CAA50317 (PubMed:8220487).Curated1
Sequence conflicti609V → I in CAA50317 (PubMed:8220487).Curated1
Sequence conflicti751 – 752EK → DE in CAA50317 (PubMed:8220487).Curated2
Sequence conflicti799 – 800Missing in CAA50317 (PubMed:8220487).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70990 Genomic DNA. Translation: CAA50317.1.
AF296832 Genomic DNA. No translation available.
CP002688 Genomic DNA. Translation: AED92894.1.
CP002688 Genomic DNA. Translation: AED92895.1.
AK316826 mRNA. Translation: BAH19538.1.
AK222090 mRNA. Translation: BAD94975.1. Different initiation.
RefSeqiNP_001031915.1. NM_001036838.2.
NP_197583.1. NM_122090.4.
UniGeneiAt.21918.

Genome annotation databases

EnsemblPlantsiAT5G20830.1; AT5G20830.1; AT5G20830.
AT5G20830.2; AT5G20830.2; AT5G20830.
GeneIDi832206.
GrameneiAT5G20830.1; AT5G20830.1; AT5G20830.
AT5G20830.2; AT5G20830.2; AT5G20830.
KEGGiath:AT5G20830.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70990 Genomic DNA. Translation: CAA50317.1.
AF296832 Genomic DNA. No translation available.
CP002688 Genomic DNA. Translation: AED92894.1.
CP002688 Genomic DNA. Translation: AED92895.1.
AK316826 mRNA. Translation: BAH19538.1.
AK222090 mRNA. Translation: BAD94975.1. Different initiation.
RefSeqiNP_001031915.1. NM_001036838.2.
NP_197583.1. NM_122090.4.
UniGeneiAt.21918.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3S27X-ray2.91A/B/C/D/E/F/G/H1-808[»]
3S28X-ray2.80A/B/C/D/E/F/G/H1-808[»]
3S29X-ray2.85A/B/C/D/E/F/G/H1-808[»]
ProteinModelPortaliP49040.
SMRiP49040.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi17481. 3 interactors.
STRINGi3702.AT5G20830.1.

Protein family/group databases

CAZyiGT4. Glycosyltransferase Family 4.

PTM databases

iPTMnetiP49040.
SwissPalmiP49040.

Proteomic databases

PaxDbiP49040.
PRIDEiP49040.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G20830.1; AT5G20830.1; AT5G20830.
AT5G20830.2; AT5G20830.2; AT5G20830.
GeneIDi832206.
GrameneiAT5G20830.1; AT5G20830.1; AT5G20830.
AT5G20830.2; AT5G20830.2; AT5G20830.
KEGGiath:AT5G20830.

Organism-specific databases

TAIRiAT5G20830.

Phylogenomic databases

eggNOGiKOG0853. Eukaryota.
COG0438. LUCA.
HOGENOMiHOG000240125.
InParanoidiP49040.
KOiK00695.
OMAiMANAERM.
OrthoDBiEOG0936023J.
PhylomeDBiP49040.

Enzyme and pathway databases

BioCyciARA:AT5G20830-MONOMER.
MetaCyc:AT5G20830-MONOMER.
BRENDAi2.4.1.13. 399.

Miscellaneous databases

EvolutionaryTraceiP49040.
PROiP49040.

Gene expression databases

GenevisibleiP49040. AT.

Family and domain databases

InterProiIPR001296. Glyco_trans_1.
IPR000368. Sucrose_synth.
IPR012820. Sucrose_synthase_pln/cyn.
[Graphical view]
PfamiPF00534. Glycos_transf_1. 1 hit.
PF00862. Sucrose_synth. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02470. sucr_synth. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiSUSY1_ARATH
AccessioniPrimary (citable) accession number: P49040
Secondary accession number(s): B9DFM1, Q56WF2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: April 14, 2009
Last modified: November 30, 2016
This is version 118 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  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.