GUMK_XANCP
ID GUMK_XANCP Reviewed; 400 AA.
AC Q7CLR5;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 2.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=UDP-glucuronate:glycolipid 2-beta-glucuronosyltransferase;
DE Short=UDP-GlcA:glycolipid glucuronosyltransferase;
DE EC=2.4.1.264 {ECO:0000250|UniProtKB:Q8GCH2};
DE AltName: Full=D-man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphoundecaprenol 2-beta-glucuronyltransferase;
GN Name=gumK; OrderedLocusNames=XCC2445;
OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS 528 / LMG 568 / P 25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190485;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(2002).
CC -!- FUNCTION: Catalyzes the transfer of a glucuronic acid (GlcA) residue
CC from UDP-glucuronate to mannose-alpha-1,3-glucose-beta-1,4-glucose-P-P-
CC polyisoprenyl to form the lipid-linked tetrasaccharide GlcA-Man-Glc(2)-
CC PP-Pol, with a glucuronic acid-beta-mannose linkage. Is involved in the
CC biosynthesis of the exopolysaccharide xanthan, since it catalyzes the
CC fourth glycosylation step in the assembly of the pentasaccharide-P-P-
CC polyisoprenyl repeating unit of xanthan.
CC {ECO:0000250|UniProtKB:Q8GCH2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-Man-(1->3)-beta-D-Glc-(1->4)-alpha-D-Glc-1-di-
CC trans,octa-cis-undecaprenyl diphosphate + UDP-alpha-D-glucuronate =
CC beta-D-GlcA-(1->2)-alpha-D-Man-(1->3)-beta-D-Glc-(1->4)-alpha-D-Glc-
CC di-trans,octa-cis-undecaprenyl diphosphate + H(+) + UDP;
CC Xref=Rhea:RHEA:30631, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:61227, ChEBI:CHEBI:61252;
CC EC=2.4.1.264; Evidence={ECO:0000250|UniProtKB:Q8GCH2};
CC -!- PATHWAY: Glycan biosynthesis; xanthan biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 70 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM41722.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE008922; AAM41722.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_637798.2; NC_003902.1.
DR RefSeq; WP_011037586.1; NC_003902.1.
DR AlphaFoldDB; Q7CLR5; -.
DR SMR; Q7CLR5; -.
DR STRING; 340.xcc-b100_1721; -.
DR CAZy; GT70; Glycosyltransferase Family 70.
DR EnsemblBacteria; AAM41722; AAM41722; XCC2445.
DR GeneID; 58012962; -.
DR KEGG; xcc:XCC2445; -.
DR PATRIC; fig|190485.4.peg.2609; -.
DR eggNOG; COG0438; Bacteria.
DR HOGENOM; CLU_062817_0_0_6; -.
DR UniPathway; UPA01017; -.
DR Proteomes; UP000001010; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cell inner membrane; Cell membrane;
KW Glycosyltransferase; Membrane; Reference proteome; Transferase.
FT CHAIN 1..400
FT /note="UDP-glucuronate:glycolipid 2-beta-
FT glucuronosyltransferase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000414020"
FT REGION 377..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 157
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 230..231
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250"
FT BINDING 272..273
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250"
FT BINDING 292
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250"
FT BINDING 306..310
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250"
SQ SEQUENCE 400 AA; 44438 MW; 250231946AB7EB61 CRC64;
MSVSPAAPAS GIRRPCYLVL SAHDFRTPRR ANIHFITDQL ALRGTTRFFS LRYSRLSRMK
GDMRLPLDDT ANTVVSHNGV DCYLWRTTVH PFNTRRSWLR PVEDAMFRWY AAHPPKQLLD
WMRESDVIVF ESGIAVAFIE LAKRVNPAAK LVYRASDGLS TINVASYIER EFDRVAPTLD
VIALVSPAMA AEVASRDNVF HVGHGVDHNL DQLGDPSPYA EGIHAVAVGS MLFDPEFFVV
ASKAFPQVTF HVIGSGMGRH PGYGDNVIVY GEMKHAQTIG YIKHARFGIA PYASEQVPVY
LADSSMKLLQ YDFFGLPAVC PNAVVGPYKS RFGYTPGNAD SVIAAITQAL EAPRVRYRQC
LNWSDTTDRV LDPRAYPETR LYPHPPTAAP QLSSEAALSH
