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Protein

UDP-glucuronate:glycolipid 2-beta-glucuronosyltransferase

Gene

gumK

Organism
Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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 (By similarity).By similarity

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.

Pathwayi: xanthan biosynthesis

This protein is involved in the pathway xanthan biosynthesis, which is part of Glycan biosynthesis.
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 acceptorBy similarity
Binding sitei292 – 2921UDP-glucuronateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Carbohydrate metabolism

Enzyme and pathway databases

BioCyciXCAM190485:GIXZ-2443-MONOMER.
UniPathwayiUPA01017.

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
Ordered Locus Names:XCC2445
OrganismiXanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
Taxonomic identifieri190485 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas
Proteomesi
  • UP000001010 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 400400UDP-glucuronate:glycolipid 2-beta-glucuronosyltransferaseBy similarityPRO_0000414020Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi190485.XCC2445.

Structurei

3D structure databases

ProteinModelPortaliQ7CLR5.
SMRiQ7CLR5. Positions 13-385.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the glycosyltransferase 70 family.Curated

Phylogenomic databases

eggNOGiENOG4108NQK. Bacteria.
ENOG410XTG8. LUCA.
HOGENOMiHOG000219965.
KOiK13659.
OrthoDBiEOG60GRRV.

Sequencei

Sequence statusi: Complete.

Q7CLR5-1 [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 AAM41722.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE008922 Genomic DNA. Translation: AAM41722.1. Different initiation.
RefSeqiNP_637798.2. NC_003902.1.
WP_011037586.1. NC_003902.1.

Genome annotation databases

EnsemblBacteriaiAAM41722; AAM41722; XCC2445.
GeneIDi998848.
KEGGixcc:XCC2445.
PATRICi24075827. VBIXanCam115730_2609.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE008922 Genomic DNA. Translation: AAM41722.1. Different initiation.
RefSeqiNP_637798.2. NC_003902.1.
WP_011037586.1. NC_003902.1.

3D structure databases

ProteinModelPortaliQ7CLR5.
SMRiQ7CLR5. Positions 13-385.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi190485.XCC2445.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAM41722; AAM41722; XCC2445.
GeneIDi998848.
KEGGixcc:XCC2445.
PATRICi24075827. VBIXanCam115730_2609.

Phylogenomic databases

eggNOGiENOG4108NQK. Bacteria.
ENOG410XTG8. LUCA.
HOGENOMiHOG000219965.
KOiK13659.
OrthoDBiEOG60GRRV.

Enzyme and pathway databases

UniPathwayiUPA01017.
BioCyciXCAM190485:GIXZ-2443-MONOMER.

Family and domain databases

ProtoNetiSearch...

Publicationsi

  1. "Comparison of the genomes of two Xanthomonas pathogens with differing host specificities."
    da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., Ciapina L.P.
    , Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.
    Nature 417:459-463(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25.

Entry informationi

Entry nameiGUMK_XANCP
AccessioniPrimary (citable) accession number: Q7CLR5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2011
Last sequence update: November 16, 2011
Last modified: December 9, 2015
This is version 53 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

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.