ID   GUMH_XANCA              Reviewed;         380 AA.
AC   Q56774;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=GDP-mannose:cellobiosyl-diphosphopolyprenol alpha-mannosyltransferase;
DE            EC=2.4.1.252;
DE   AltName: Full=Exopolysaccharide xanthan biosynthesis glycosyltransferase GumH;
GN   Name=gumH;
OS   Xanthomonas campestris.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=339;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=B1459;
RA   Capage M.A., Doherty D.H., Betlach M.R., Vanderslice R.W.;
RT   "Recombinant-DNA mediated production of xanthan gum.";
RL   Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=9537354; DOI=10.1128/jb.180.7.1607-1617.1998;
RA   Katzen F., Ferreiro D.U., Oddo C.G., Ielmini M.V., Becker A., Puhler A.,
RA   Ielpi L.;
RT   "Xanthomonas campestris pv. campestris gum mutants: effects on xanthan
RT   biosynthesis and plant virulence.";
RL   J. Bacteriol. 180:1607-1617(1998).
RN   [3]
RP   FUNCTION.
RX   PubMed=11001941; DOI=10.1074/jbc.m007496200;
RA   Abdian P.L., Lellouch A.C., Gautier C., Ielpi L., Geremia R.A.;
RT   "Identification of essential amino acids in the bacterial alpha
RT   -mannosyltransferase aceA.";
RL   J. Biol. Chem. 275:40568-40575(2000).
CC   -!- FUNCTION: Involved in the biosynthesis of the exopolysaccharide
CC       xanthan, a polymer that is comprised of repeating pentasaccharide units
CC       with the structure of a beta-(1,4)-linked D-glucose backbone with
CC       trisaccharide side chains composed of mannose-beta-(1,4)-glucuronic
CC       acid-beta-(1,2)-mannose attached to alternate glucose residues in the
CC       backbone by alpha-(1,3) linkages. Xanthan is involved in pathogenicity
CC       but has also been used in a variety of applications as a specialty
CC       polymer for commercial applications, including food additives, where
CC       they act as viscosifying, stabilizing, emulsifying, or gelling agents.
CC       {ECO:0000269|PubMed:11001941, ECO:0000269|PubMed:9537354}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-Glc-(1->4)-alpha-D-Glc-di-trans,octa-cis-undecaprenyl
CC         diphosphate + GDP-alpha-D-mannose = alpha-D-Man-(1->3)-beta-D-Glc-
CC         (1->4)-alpha-D-Glc-1-di-trans,octa-cis-undecaprenyl diphosphate + GDP
CC         + H(+); Xref=Rhea:RHEA:28310, ChEBI:CHEBI:15378, ChEBI:CHEBI:57527,
CC         ChEBI:CHEBI:58189, ChEBI:CHEBI:61247, ChEBI:CHEBI:61252;
CC         EC=2.4.1.252; Evidence={ECO:0000269|PubMed:9537354};
CC   -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC       Glycosyltransferase 4 subfamily. {ECO:0000305}.
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DR   EMBL; U22511; AAA86376.1; -; Genomic_DNA.
DR   PIR; S67857; S67857.
DR   AlphaFoldDB; Q56774; -.
DR   SMR; Q56774; -.
DR   STRING; 1094184.KWO_0108705; -.
DR   CAZy; GT4; Glycosyltransferase Family 4.
DR   eggNOG; COG0438; Bacteria.
DR   BioCyc; MetaCyc:MON-15981; -.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000271; P:polysaccharide biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR001296; Glyco_trans_1.
DR   InterPro; IPR028098; Glyco_trans_4-like_N.
DR   Pfam; PF13439; Glyco_transf_4; 1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
PE   1: Evidence at protein level;
KW   Exopolysaccharide synthesis; Glycosyltransferase; Transferase; Virulence.
FT   CHAIN           1..380
FT                   /note="GDP-mannose:cellobiosyl-diphosphopolyprenol alpha-
FT                   mannosyltransferase"
FT                   /id="PRO_0000424204"
SQ   SEQUENCE   380 AA;  42110 MW;  2C0C415F63E5E201 CRC64;
     MKVVHVVRQF HPSIGGMEEV VLNVARQHQA NSADTVEIVT LDRVFTDPSA QLAQHELHQG
     LSITRIGYRG SSRYPIAPSV LGAIRSADVV HLHGIDFFYD YLALTKPLHG KPMVVSTHGG
     FFHTAYASRM KQIWFQTLTR TSALAYARVI ATSENDGDLF AKVVAPSRLR VIENGVDVEK
     YAGQGARAPG RTMLYFGRWS VNKGLIETLE LLQAALTRDP QWRLIIAGRE YDLNEADLRK
     AIAERGLQDK VQLSMSPSQQ QLCALMQQAQ FFVCLSRHEG FGIAAVEAMS AGLIPILSDI
     PPFVRLATES GQGVIVNRDR IQAAADSVQA LALQANADFD ARRTATMAYV ARYDWRHVVG
     RYIDEYHAAL GTPRTQEAVR