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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)DescriptionActionsGraphical viewLength
Active sitei157Proton acceptor1 Publication1
Binding sitei292UDP-glucuronate1 Publication1

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)DescriptionActionsGraphical viewLength
Mutagenesisi157D → A, E or N: Loss of catalytic activity. Loss of xanthan production. 1 Publication1
Mutagenesisi192E → A: No effect on both substrate affinity and catalytic activity. 1 Publication1
Mutagenesisi207D → A: No effect on both substrate affinity and catalytic activity. 1 Publication1
Mutagenesisi231M → A: No effect on both substrate affinity and catalytic activity. 1 Publication1
Mutagenesisi234D → A: No effect on both substrate affinity and catalytic activity. 1 Publication1
Mutagenesisi272E → A: 2-fold decrease in both affinity for UDP-GlcA and catalytic activity. 1 Publication1
Mutagenesisi292Y → A: 14-fold decrease in catalytic efficiency. 25% of wild-type xanthan production. 1 Publication1
Mutagenesisi307K → A: 54-fold decrease in catalytic efficiency. 30% of wild-type xanthan production. 1 Publication1
Mutagenesisi310Q → A: 19-fold decrease in affinity for UDP-GlcA but no effect on catalytic activity. 60% of wild-type xanthan production. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004140191 – 400UDP-glucuronate:glycolipid 2-beta-glucuronosyltransferaseAdd BLAST400

Interactioni

Protein-protein interaction databases

STRINGi190485.XCC2445.

Structurei

Secondary structure

1400
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi17 – 23Combined sources7
Beta strandi27 – 29Combined sources3
Helixi32 – 43Combined sources12
Beta strandi46 – 50Combined sources5
Helixi57 – 60Combined sources4
Helixi65 – 70Combined sources6
Beta strandi73 – 77Combined sources5
Beta strandi80 – 84Combined sources5
Beta strandi87 – 89Combined sources3
Helixi97 – 99Combined sources3
Helixi100 – 112Combined sources13
Helixi116 – 124Combined sources9
Beta strandi126 – 133Combined sources8
Helixi134 – 138Combined sources5
Helixi139 – 145Combined sources7
Beta strandi149 – 157Combined sources9
Helixi159 – 162Combined sources4
Helixi166 – 175Combined sources10
Helixi176 – 178Combined sources3
Beta strandi180 – 185Combined sources6
Helixi187 – 192Combined sources6
Beta strandi199 – 201Combined sources3
Helixi210 – 214Combined sources5
Beta strandi221 – 228Combined sources8
Helixi235 – 244Combined sources10
Beta strandi248 – 254Combined sources7
Beta strandi267 – 270Combined sources4
Helixi275 – 283Combined sources9
Beta strandi286 – 289Combined sources4
Helixi301 – 304Combined sources4
Helixi306 – 313Combined sources8
Beta strandi318 – 321Combined sources4
Helixi322 – 324Combined sources3
Beta strandi329 – 334Combined sources6
Helixi339 – 351Combined sources13
Helixi363 – 371Combined sources9
Helixi373 – 375Combined sources3
Helixi377 – 379Combined sources3
Beta strandi380 – 382Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ8GCH2.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni230 – 231UDP-glucuronate binding2
Regioni272 – 273UDP-glucuronate binding2
Regioni306 – 310UDP-glucuronate binding5

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)DescriptionActionsGraphical viewLength
Sequence conflicti2S → G in AAN86640 (PubMed:14736729).Curated1
Sequence conflicti2S → G in AAA86379 (PubMed:14736729).Curated1
Sequence conflicti22A → S in AAN86640 (PubMed:14736729).Curated1
Sequence conflicti22A → S in AAA86379 (PubMed:14736729).Curated1
Sequence conflicti194A → V in AAN86640 (PubMed:14736729).Curated1
Sequence conflicti194A → V in AAA86379 (PubMed:14736729).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2HY7X-ray1.90A1-400[»]
2Q6VX-ray2.28A1-400[»]
3CUYX-ray2.30A1-400[»]
3CV3X-ray2.25A1-400[»]
ProteinModelPortaliQ8GCH2.
SMRiQ8GCH2.
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: November 2, 2016
This is version 41 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.