ID   GUMH_KOMXY              Reviewed;         393 AA.
AC   Q44571;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=GDP-mannose:cellobiosyl-diphosphopolyprenol alpha-mannosyltransferase;
DE            EC=2.4.1.252;
GN   Name=aceC; Synonyms=aceA;
OS   Komagataeibacter xylinus (Gluconacetobacter xylinus).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Komagataeibacter.
OX   NCBI_TaxID=28448;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NRRL B42;
RX   PubMed=8761462; DOI=10.1042/bj3180133;
RA   Geremia R.A., Petroni E.A., Ielpi L., Henrissat B.;
RT   "Towards a classification of glycosyltransferases based on amino acid
RT   sequence similarities: prokaryotic alpha-mannosyltransferases.";
RL   Biochem. J. 318:133-138(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NRRL B42;
RX   PubMed=8759843; DOI=10.1128/jb.178.16.4814-4821.1996;
RA   Petroni E.A., Ielpi L.;
RT   "Isolation and nucleotide sequence of the GDP-mannose:cellobiosyl-
RT   diphosphopolyprenol alpha-mannosyltransferase gene from Acetobacter
RT   xylinum.";
RL   J. Bacteriol. 178:4814-4821(1996).
RN   [3]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=10485283; DOI=10.1007/s004380051040;
RA   Geremia R.A., Roux M., Ferreiro D.U., Dauphin-Dubois R., Lellouch A.C.,
RA   Ielpi L.;
RT   "Expression and biochemical characterisation of recombinant AceA, a
RT   bacterial alpha-mannosyltransferase.";
RL   Mol. Gen. Genet. 261:933-940(1999).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ASP-109; HIS-127; SER-162;
RP   LYS-211; LEU-270; GLU-287 AND GLU-295.
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 acetan,
CC       a water-soluble polysaccharide involved in production of bacterial
CC       cellulose (BC). {ECO:0000269|PubMed:10485283,
CC       ECO:0000269|PubMed:11001941}.
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:10485283,
CC         ECO:0000269|PubMed:11001941};
CC   -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC       Glycosyltransferase 4 subfamily. {ECO:0000305}.
CC   -!- CAUTION: The gene has been independently discovered by another group,
CC       who referred to it as aceA, causing confusion with the aceA gene which
CC       encodes a undecaprenyl-phosphate glucose phosphotransferase.
CC       {ECO:0000305|PubMed:10485283}.
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DR   EMBL; U37258; AAC44373.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q44571; -.
DR   SMR; Q44571; -.
DR   STRING; 1220579.GCA_001571345_00669; -.
DR   CAZy; GT4; Glycosyltransferase Family 4.
DR   BioCyc; MetaCyc:MON-15989; -.
DR   BRENDA; 2.4.1.252; 50.
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.
FT   CHAIN           1..393
FT                   /note="GDP-mannose:cellobiosyl-diphosphopolyprenol alpha-
FT                   mannosyltransferase"
FT                   /id="PRO_0000424203"
FT   MUTAGEN         109
FT                   /note="D->A: Decreases strongly catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:11001941"
FT   MUTAGEN         127
FT                   /note="H->A: Decreases strongly catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:11001941"
FT   MUTAGEN         162
FT                   /note="S->A: Decreases strongly catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:11001941"
FT   MUTAGEN         211
FT                   /note="K->A: Abolishes catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:11001941"
FT   MUTAGEN         270
FT                   /note="L->A: Decreases catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:11001941"
FT   MUTAGEN         287
FT                   /note="E->A: Abolishes catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:11001941"
FT   MUTAGEN         295
FT                   /note="E->A: Decreases strongly catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:11001941"
SQ   SEQUENCE   393 AA;  43222 MW;  5C89EC6A9562E8A7 CRC64;
     MNSKKRGDET LKVLHICRQF SPSVGGLEDS LLNLARSQRQ RLGIDAEVLT LDTVFGRPGK
     LPHRDVVDGI PVTRLAWRGS TKYPLAPQVL RHIGGFDLLH VHAIDFFFDF LAWTWPLHRK
     TMIASTHGGF FHTGALRRIK EIWFRTITPI SVRAYKKIVA CSYSDADLFR HVAAGRLITI
     ENGINQTRFR DAASRTPNRT ILAFGRFAVH KRLKLLFQLV ALLRAYNSGW NIIVAGQDSN
     LTADDLRAQA RACGIEDSLR IVSGPSDAEL RGLMGEASFF GCLSAHEGFG LAAVEAMSAG
     LVPILSNITP FARLMQQGAA GVMVNPDNLA PGAREAEDMA AALPETADAL RARNMDVASR
     YDWHSVAHEY ARLYQQVLGR ALPEANMAAA GAE