GUMI_XANCE
ID GUMI_XANCE Reviewed; 349 AA.
AC Q56775;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 2.
DT 03-AUG-2022, entry version 49.
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;
OS Xanthomonas campestris pv. campestris.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=340;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13951 / NCIB 11803 / NRRL B-1459;
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 DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 13951 / NCIB 11803 / NRRL B-1459;
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, CATALYTIC ACTIVITY, ROLE IN XANTHAN BIOSYNTHESIS, SUBSTRATE
RP SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION,
RP DISRUPTION PHENOTYPE, PATHWAY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 13951 / NCIB 11803 / NRRL B-1459;
RX PubMed=21367879; DOI=10.1093/glycob/cwr022;
RA Salinas S.R., Bianco M.I., Barreras M., Ielpi L.;
RT "Expression, purification and biochemical characterization of GumI, a
RT monotopic membrane GDP-mannose:glycolipid 4-beta-D-mannosyltransferase from
RT Xanthomonas campestris pv. campestris.";
RL Glycobiology 21:903-913(2011).
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. To a lesser extent, can also use ADP-Man and
CC even GDP-Glc as sugar donor substrates in vitro. Is unable to transfer
CC a Man residue to the free-tetrasaccharide GlcA-Man-Glc(2) used as an
CC acceptor, which indicates that the diphosphate group and the lipid
CC moiety in the acceptor substrate are of major importance for acceptor
CC binding and catalysis. {ECO:0000269|PubMed:21367879}.
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 Evidence={ECO:0000269|PubMed:21367879};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is around 8. Activity decreases below pH 7.5 and above pH
CC 9.5. {ECO:0000269|PubMed:21367879};
CC Temperature dependence:
CC Optimum temperature is aroud 35 degrees Celsius with a 20% drop at 20
CC degrees Celsius and a near-complete inhibition at 60 degrees Celsius,
CC probably due to enzyme denaturation. {ECO:0000269|PubMed:21367879};
CC -!- PATHWAY: Glycan biosynthesis; xanthan biosynthesis.
CC {ECO:0000269|PubMed:21367879}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:21367879}. Note=Monotopic integral membrane
CC protein, mostly cytoplasmic.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene display a non-mucoid
CC phenotype, indicating that they have a reduced abundance of
CC polysaccharides relative to the wild-type strain. More precisely,
CC mutational interruption of the gumI gene leads to accumulation of GlcA-
CC beta-1,2-Man-alpha-1,3-Glc-beta-1,4-Glc-PP-polyisoprenyl (GlcA-Man-
CC Glc2-PP-Pol), and a decrease in xanthan production of more than 95%.
CC {ECO:0000269|PubMed:21367879, ECO:0000269|PubMed:9537354}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 94 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA86377.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U22511; AAA86377.1; ALT_FRAME; Genomic_DNA.
DR PIR; S67858; S67858.
DR CAZy; GT94; Glycosyltransferase Family 94.
DR BioCyc; MetaCyc:MON-15983; -.
DR BRENDA; 2.4.1.251; 6708.
DR UniPathway; UPA01017; -.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0019187; F:beta-1,4-mannosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0000271; P:polysaccharide biosynthetic process; IMP:UniProtKB.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cell inner membrane; Cell membrane;
KW Glycosyltransferase; Membrane; 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_0000414017"
SQ SEQUENCE 349 AA; 39089 MW; 8CBDCFB368766896 CRC64;
MSASASLPVT RAAAAPRITV LFSTEKPNAN TNPYLTQLYD ALPDAVQPRF FSMREALLSR
YDVLHLHWPE YLLRHPSKMG TLAKQACAAL LLMKLQLTGT PVVRTLHNLA PHEDRGWRER
ALLRWIDQLT RRWIRINATT PVRPPFTDTI LHGHYRDWFA TMEQSTTLPG RLLHFGLIRP
YKGVEVLLDV MRDVQDPRLS LRIVGNPATP XMRTLVETAC AQDARISALL AYVEEPVLAR
EVSACELVVL PYKQMHNSGT LLLALSLARP VLAPWSESNA AIADEVGPGW VFLYEGEFDA
ALLSGMLDQV RAAPRGPAPD LSQRDWPRIG QLHYRTYLEA LGKDGDAAL
