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Protein

UDP-glucuronate:glycolipid 2-beta-glucuronosyltransferase

Gene

gumK

Organism
Xanthomonas campestris pv. campestris
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the transfer of a glucuronic acid (GlcA) residue from UDP-glucuronate to mannose-alpha-1,3-glucose-beta-1,4-glucose-P-P-polyisoprenyl to form the lipid-linked tetrasaccharide GlcA-Man-Glc(2)-PP-Pol, with a glucuronic acid-beta-mannose linkage. Is involved in the biosynthesis of the exopolysaccharide xanthan, since it catalyzes the fourth glycosylation step in the assembly of the pentasaccharide-P-P-polyisoprenyl repeating unit of xanthan. Is unable to use the trisaccharide acceptor freed from the pyrophosphate lipid moiety. Does not show specificity for the lipidic portion of the acceptor. Shows diminished activity when tested with 6-O-acetyl-mannose-alpha-1,3-glucose-beta-1,4-glucose-P-P-polyisoprenyl, a putative intermediate in the synthesis of xanthan; this could indicate that acetylation of the internal mannose takes place after the formation of the GumK product.1 Publication

Catalytic activityi

UDP-glucuronate + D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphospho-ditrans,octacis-undecaprenol = UDP + D-GlcA-beta-(1->2)-D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphospho-ditrans,octacis-undecaprenol.2 Publications

Kineticsi

  1. KM=62 µM for UDP-glucuronate1 Publication
  2. KM=198 µM for Man-Glc(2)-PP-Pol1 Publication
  1. Vmax=116 pmol/min/µg enzyme1 Publication

Pathwayi: xanthan biosynthesis

This protein is involved in the pathway xanthan biosynthesis, which is part of Glycan biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway xanthan biosynthesis and in Glycan biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei157 – 1571Proton acceptor1 Publication
Binding sitei292 – 2921UDP-glucuronate1 Publication

GO - Molecular functioni

  • glucuronosyltransferase activity Source: UniProtKB

GO - Biological processi

  • polysaccharide biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Carbohydrate metabolism

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15982.
BRENDAi2.4.1.264. 6708.
UniPathwayiUPA01017.

Protein family/group databases

CAZyiGT70. Glycosyltransferase Family 70.

Names & Taxonomyi

Protein namesi
Recommended name:
UDP-glucuronate:glycolipid 2-beta-glucuronosyltransferase (EC:2.4.1.264)
Short name:
UDP-GlcA:glycolipid glucuronosyltransferase
Alternative name(s):
D-man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphoundecaprenol 2-beta-glucuronyltransferase
Gene namesi
Name:gumK
OrganismiXanthomonas campestris pv. campestris
Taxonomic identifieri340 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

Subcellular locationi

  • Cell inner membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication

GO - Cellular componenti

  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene accumulate Man-alpha-1,3-Glc-beta-1,4-Glc-PP-polyisoprenyl, are unable to produce GlcA-Man-Glc(2)-PP-Pol, and show a decrease in xanthan production of more than 95%.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi157 – 1571D → A, E or N: Loss of catalytic activity. Loss of xanthan production. 1 Publication
Mutagenesisi192 – 1921E → A: No effect on both substrate affinity and catalytic activity. 1 Publication
Mutagenesisi207 – 2071D → A: No effect on both substrate affinity and catalytic activity. 1 Publication
Mutagenesisi231 – 2311M → A: No effect on both substrate affinity and catalytic activity. 1 Publication
Mutagenesisi234 – 2341D → A: No effect on both substrate affinity and catalytic activity. 1 Publication
Mutagenesisi272 – 2721E → A: 2-fold decrease in both affinity for UDP-GlcA and catalytic activity. 1 Publication
Mutagenesisi292 – 2921Y → A: 14-fold decrease in catalytic efficiency. 25% of wild-type xanthan production. 1 Publication
Mutagenesisi307 – 3071K → A: 54-fold decrease in catalytic efficiency. 30% of wild-type xanthan production. 1 Publication
Mutagenesisi310 – 3101Q → A: 19-fold decrease in affinity for UDP-GlcA but no effect on catalytic activity. 60% of wild-type xanthan production. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 400400UDP-glucuronate:glycolipid 2-beta-glucuronosyltransferasePRO_0000414019Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi190485.XCC2445.

Structurei

Secondary structure

1
400
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi17 – 237Combined sources
Beta strandi27 – 293Combined sources
Helixi32 – 4312Combined sources
Beta strandi46 – 505Combined sources
Helixi57 – 604Combined sources
Helixi65 – 706Combined sources
Beta strandi73 – 775Combined sources
Beta strandi80 – 845Combined sources
Beta strandi87 – 893Combined sources
Helixi97 – 993Combined sources
Helixi100 – 11213Combined sources
Helixi116 – 1249Combined sources
Beta strandi126 – 1338Combined sources
Helixi134 – 1385Combined sources
Helixi139 – 1457Combined sources
Beta strandi149 – 1579Combined sources
Helixi159 – 1624Combined sources
Helixi166 – 17510Combined sources
Helixi176 – 1783Combined sources
Beta strandi180 – 1856Combined sources
Helixi187 – 1926Combined sources
Beta strandi199 – 2013Combined sources
Helixi210 – 2145Combined sources
Beta strandi221 – 2288Combined sources
Helixi235 – 24410Combined sources
Beta strandi248 – 2547Combined sources
Beta strandi267 – 2704Combined sources
Helixi275 – 2839Combined sources
Beta strandi286 – 2894Combined sources
Helixi301 – 3044Combined sources
Helixi306 – 3138Combined sources
Beta strandi318 – 3214Combined sources
Helixi322 – 3243Combined sources
Beta strandi329 – 3346Combined sources
Helixi339 – 35113Combined sources
Helixi363 – 3719Combined sources
Helixi373 – 3753Combined sources
Helixi377 – 3793Combined sources
Beta strandi380 – 3823Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HY7X-ray1.90A1-400[»]
2Q6VX-ray2.28A1-400[»]
3CUYX-ray2.30A1-400[»]
3CV3X-ray2.25A1-400[»]
ProteinModelPortaliQ8GCH2.
SMRiQ8GCH2. Positions 13-385.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8GCH2.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni230 – 2312UDP-glucuronate binding
Regioni272 – 2732UDP-glucuronate binding
Regioni306 – 3105UDP-glucuronate binding

Sequence similaritiesi

Belongs to the glycosyltransferase 70 family.Curated

Phylogenomic databases

eggNOGiENOG4108NQK. Bacteria.
ENOG410XTG8. LUCA.
KOiK13659.

Sequencei

Sequence statusi: Complete.

Q8GCH2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVSPAAPAS GIRRPCYLVL SAHDFRTPRR ANIHFITDQL ALRGTTRFFS
60 70 80 90 100
LRYSRLSRMK GDMRLPLDDT ANTVVSHNGV DCYLWRTTVH PFNTRRSWLR
110 120 130 140 150
PVEDAMFRWY AAHPPKQLLD WMRESDVIVF ESGIAVAFIE LAKRVNPAAK
160 170 180 190 200
LVYRASDGLS TINVASYIER EFDRVAPTLD VIALVSPAMA AEVASRDNVF
210 220 230 240 250
HVGHGVDHNL DQLGDPSPYA EGIHAVAVGS MLFDPEFFVV ASKAFPQVTF
260 270 280 290 300
HVIGSGMGRH PGYGDNVIVY GEMKHAQTIG YIKHARFGIA PYASEQVPVY
310 320 330 340 350
LADSSMKLLQ YDFFGLPAVC PNAVVGPYKS RFGYTPGNAD SVIAAITQAL
360 370 380 390 400
EAPRVRYRQC LNWSDTTDRV LDPRAYPETR LYPHPPTAAP QLSSEAALSH
Length:400
Mass (Da):44,438
Last modified:November 16, 2011 - v2
Checksum:i250231946AB7EB61
GO

Sequence cautioni

The sequence AAA86379 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21S → G in AAN86640 (PubMed:14736729).Curated
Sequence conflicti2 – 21S → G in AAA86379 (PubMed:14736729).Curated
Sequence conflicti22 – 221A → S in AAN86640 (PubMed:14736729).Curated
Sequence conflicti22 – 221A → S in AAA86379 (PubMed:14736729).Curated
Sequence conflicti194 – 1941A → V in AAN86640 (PubMed:14736729).Curated
Sequence conflicti194 – 1941A → V in AAA86379 (PubMed:14736729).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U22511 Genomic DNA. Translation: AAA86379.1. Different initiation.
AY170889 Genomic DNA. Translation: AAN86640.1.
PIRiS67860.
RefSeqiWP_011037586.1. NZ_CP012146.1.

Genome annotation databases

KEGGiag:AAN86640.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U22511 Genomic DNA. Translation: AAA86379.1. Different initiation.
AY170889 Genomic DNA. Translation: AAN86640.1.
PIRiS67860.
RefSeqiWP_011037586.1. NZ_CP012146.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HY7X-ray1.90A1-400[»]
2Q6VX-ray2.28A1-400[»]
3CUYX-ray2.30A1-400[»]
3CV3X-ray2.25A1-400[»]
ProteinModelPortaliQ8GCH2.
SMRiQ8GCH2. Positions 13-385.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi190485.XCC2445.

Protein family/group databases

CAZyiGT70. Glycosyltransferase Family 70.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAN86640.

Phylogenomic databases

eggNOGiENOG4108NQK. Bacteria.
ENOG410XTG8. LUCA.
KOiK13659.

Enzyme and pathway databases

UniPathwayiUPA01017.
BioCyciMetaCyc:MONOMER-15982.
BRENDAi2.4.1.264. 6708.

Miscellaneous databases

EvolutionaryTraceiQ8GCH2.

Family and domain databases

ProtoNetiSearch...

Entry informationi

Entry nameiGUMK_XANCE
AccessioniPrimary (citable) accession number: Q8GCH2
Secondary accession number(s): Q56777
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2011
Last sequence update: November 16, 2011
Last modified: April 13, 2016
This is version 39 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.