ID GUMI_XANCP Reviewed; 349 AA.
AC Q8P804;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=GDP-mannose:glycolipid 4-beta-D-mannosyltransferase;
DE EC=2.4.1.251;
DE AltName: Full=GlcA-beta-(1->2)-D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphoundecaprenol 4-beta-mannosyltransferase;
DE Flags: Precursor;
GN Name=gumI; OrderedLocusNames=XCC2447;
OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS 528 / LMG 568 / P 25).
OC Bacteria; Pseudomonadota; 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: Nonprocessive beta-mannosyltransferase that catalyzes the
CC transfer of a mannose residue from GDP-mannose to glucuronic acid-beta-
CC 1,2-mannose-alpha-1,3-glucose-beta-1,4-glucose-PP-polyisoprenyl to form
CC the lipid-linked pentasaccharide repeating unit of xanthan, Man-GlcA-
CC Man-Glc(2)-PP-Pol. Is involved in the biosynthesis of the
CC exopolysaccharide xanthan (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-GlcA-(1->2)-alpha-D-Man-(1->3)-beta-D-Glc-(1->4)-alpha-
CC D-Glc-di-trans,octa-cis-undecaprenyl diphosphate + GDP-alpha-D-
CC mannose = beta-D-Man-(1->4)-beta-D-GlcA-(1->2)-alpha-D-Man-(1->3)-
CC beta-D-Glc-(1->4)-alpha-D-Glc-di-trans,octa-cis-undecaprenyl
CC diphosphate + GDP + H(+); Xref=Rhea:RHEA:28306, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57527, ChEBI:CHEBI:58189, ChEBI:CHEBI:61227,
CC ChEBI:CHEBI:61230; EC=2.4.1.251;
CC -!- PATHWAY: Glycan biosynthesis; xanthan biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 94 family.
CC {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; AAM41724.1; -; Genomic_DNA.
DR RefSeq; NP_637800.1; NC_003902.1.
DR RefSeq; WP_011037588.1; NC_003902.1.
DR AlphaFoldDB; Q8P804; -.
DR SMR; Q8P804; -.
DR STRING; 190485.XCC2447; -.
DR CAZy; GT94; Glycosyltransferase Family 94.
DR EnsemblBacteria; AAM41724; AAM41724; XCC2447.
DR KEGG; xcc:XCC2447; -.
DR PATRIC; fig|190485.4.peg.2611; -.
DR eggNOG; COG0438; Bacteria.
DR HOGENOM; CLU_009583_6_0_6; -.
DR OrthoDB; 9790710at2; -.
DR UniPathway; UPA01017; -.
DR PHI-base; PHI:6665; -.
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.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR Pfam; PF13692; Glyco_trans_1_4; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cell inner membrane; Cell membrane;
KW Glycosyltransferase; Membrane; Reference proteome; Signal; Transferase.
FT SIGNAL 1..14
FT /evidence="ECO:0000255"
FT CHAIN 15..349
FT /note="GDP-mannose:glycolipid 4-beta-D-mannosyltransferase"
FT /id="PRO_0000414018"
SQ SEQUENCE 349 AA; 39076 MW; 7F8779B341750E52 CRC64;
MSASASLPVT RAAAAPRITV LFSTEKPNAN TNPYLTQLYD ALPDAVQPRF FSMREALLSR
YDVLHLHWPE YLLRHPSKMG TLAKQACAAL LLMKLQLTGT PVVRTLHNLA PHEDRGWRER
ALLRWIDQLT RRWIRINATT PVRPPFTDTI LHGHYRDWFA TMEQGTTVPG RLLHFGLIRP
YKGVEVLLDV MRDVQDPRLS LRIVGNPATP QMRTLVETAC AQDARISALL AYVEEPVLAR
EVSACELVVL PYKQMHNSGT LLLALSLARP VLAPWSESNA AIAEEVGPGW VFLYEGEFDA
ALLSGMLDQV RAAPRGPAPD LSQRDWPRIG QLHYRTYLEA LGKDGDAAL
//
