ID   GUMH_XANOP              Reviewed;         380 AA.
AC   B2SUK8;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 63.
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; OrderedLocusNames=PXO_01398;
OS   Xanthomonas oryzae pv. oryzae (strain PXO99A).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=360094;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PXO99A;
RX   PubMed=18452608; DOI=10.1186/1471-2164-9-204;
RA   Salzberg S.L., Sommer D.D., Schatz M.C., Phillippy A.M., Rabinowicz P.D.,
RA   Tsuge S., Furutani A., Ochiai H., Delcher A.L., Kelley D., Madupu R.,
RA   Puiu D., Radune D., Shumway M., Trapnell C., Aparna G., Jha G., Pandey A.,
RA   Patil P.B., Ishihara H., Meyer D.F., Szurek B., Verdier V., Koebnik R.,
RA   Dow J.M., Ryan R.P., Hirata H., Tsuyumu S., Won Lee S., Seo Y.-S.,
RA   Sriariyanum M., Ronald P.C., Sonti R.V., Van Sluys M.-A., Leach J.E.,
RA   White F.F., Bogdanove A.J.;
RT   "Genome sequence and rapid evolution of the rice pathogen Xanthomonas
RT   oryzae pv. oryzae PXO99A.";
RL   BMC Genomics 9:204-204(2008).
RN   [2]
RP   FUNCTION.
RX   PubMed=18854951; DOI=10.1007/s10529-008-9858-3;
RA   Kim S.Y., Kim J.G., Lee B.M., Cho J.Y.;
RT   "Mutational analysis of the gum gene cluster required for xanthan
RT   biosynthesis in Xanthomonas oryzae pv oryzae.";
RL   Biotechnol. Lett. 31:265-270(2009).
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:18854951}.
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;
CC   -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC       Glycosyltransferase 4 subfamily. {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; CP000967; ACD59981.1; -; Genomic_DNA.
DR   RefSeq; WP_011259696.1; NC_010717.2.
DR   AlphaFoldDB; B2SUK8; -.
DR   SMR; B2SUK8; -.
DR   STRING; 360094.PXO_01398; -.
DR   CAZy; GT4; Glycosyltransferase Family 4.
DR   EnsemblBacteria; ACD59981; ACD59981; PXO_01398.
DR   KEGG; xop:PXO_01398; -.
DR   eggNOG; COG0438; Bacteria.
DR   HOGENOM; CLU_739069_0_0_6; -.
DR   OMA; SYYENFG; -.
DR   OrthoDB; 694191at2; -.
DR   Proteomes; UP000001740; Chromosome.
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   3: Inferred from homology;
KW   Exopolysaccharide synthesis; Glycosyltransferase; Transferase.
FT   CHAIN           1..380
FT                   /note="GDP-mannose:cellobiosyl-diphosphopolyprenol alpha-
FT                   mannosyltransferase"
FT                   /id="PRO_0000424205"
SQ   SEQUENCE   380 AA;  42237 MW;  85B5D0F44755DC03 CRC64;
     MKVVHVVRQF HPSIGGMEEV VLNVARQHQA TSADTVEVVT LDRVFTDPSG RLSAHDTHQG
     LPIRRIGYRG SSRYPLAPSV LDAIRSADVV HLHGIDFFYD YLALTKPLHG KPMVVSTHGG
     FFHTAYASCM KQLWFQTLTR ISALAYARVI ATSENDGDLF AEVVAPSRLR VIENGVDVQK
     YAGQGATTPG RTMLYFGRWS VNKGLIETLA LLQAALKRDP QWRLIIAGRE YDLNESDLRK
     AIAERGLQDK VQLSMSPSQE QLRALMQQAQ FFVCLSRHEG FGIAAVEAMS AGLIPILSDI
     PPFVRLASES GQGVIVNRDK IEAAADQVQA LALHADNDFD TRRTASMAYV SRYDWKHVVG
     RYIDEYHDAL GIPRVQEAVR