ID   KANF_STRKN              Reviewed;         387 AA.
AC   Q65CC1;
DT   06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=2-deoxystreptamine glucosyltransferase;
DE            EC=2.4.1.284;
DE   AltName: Full=2-deoxystreptamine N-acetyl-D-glucosaminyltransferase;
DE            EC=2.4.1.283;
DE   AltName: Full=Kanamycin biosynthesis protein F;
GN   Name=kanF;
OS   Streptomyces kanamyceticus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1967;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 12853 / DSM 40500 / NBRC 13414 / NCIMB 9343 / NRRL B-2535 / VKM
RC   Ac-837;
RX   PubMed=15313224; DOI=10.1016/j.abb.2004.06.009;
RA   Kharel M.K., Subba B., Basnet D.B., Woo J.S., Lee H.C., Liou K.,
RA   Sohng J.K.;
RT   "A gene cluster for biosynthesis of kanamycin from Streptomyces
RT   kanamyceticus: comparison with gentamicin biosynthetic gene cluster.";
RL   Arch. Biochem. Biophys. 429:204-214(2004).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=ATCC 12853 / DSM 40500 / NBRC 13414 / NCIMB 9343 / NRRL B-2535 / VKM
RC   Ac-837;
RX   PubMed=21983602; DOI=10.1038/nchembio.671;
RA   Park J.W., Park S.R., Nepal K.K., Han A.R., Ban Y.H., Yoo Y.J., Kim E.J.,
RA   Kim E.M., Kim D., Sohng J.K., Yoon Y.J.;
RT   "Discovery of parallel pathways of kanamycin biosynthesis allows antibiotic
RT   manipulation.";
RL   Nat. Chem. Biol. 7:843-852(2011).
CC   -!- FUNCTION: Glycosyltransferase involved in the biosynthesis of kanamycin
CC       by mediating conversion of 2-deoxystreptamine (2-DOS) to 2'-N-
CC       acetylparomamine using UDP-alpha-D-glucose as sugar donor. Can also
CC       accept UDP-alpha-D-glucosamine, but with a much lower activity compared
CC       to UDP-alpha-D-glucose. {ECO:0000269|PubMed:21983602}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-deoxystreptamine + UDP-N-acetyl-alpha-D-glucosamine = 2'-N-
CC         acetylparomamine + H(+) + UDP; Xref=Rhea:RHEA:33947,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:65010, ChEBI:CHEBI:65069; EC=2.4.1.283;
CC         Evidence={ECO:0000269|PubMed:21983602};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-deoxystreptamine + UDP-alpha-D-glucose = 2'-deamino-2'-
CC         hydroxyparomamine + H(+) + UDP; Xref=Rhea:RHEA:34063,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885,
CC         ChEBI:CHEBI:65069, ChEBI:CHEBI:65071; EC=2.4.1.284;
CC         Evidence={ECO:0000269|PubMed:21983602};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.32 mM for UDP-N-acetyl-alpha-D-glucosamine
CC         {ECO:0000269|PubMed:21983602};
CC         KM=0.28 mM for UDP-alpha-D-glucose {ECO:0000269|PubMed:21983602};
CC   -!- PATHWAY: Antibiotic biosynthesis; kanamycin biosynthesis.
CC       {ECO:0000269|PubMed:21983602}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC       {ECO:0000305}.
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DR   EMBL; AJ582817; CAE46947.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q65CC1; -.
DR   SMR; Q65CC1; -.
DR   KEGG; ag:CAE46947; -.
DR   BioCyc; MetaCyc:MON-17218; -.
DR   UniPathway; UPA00965; -.
DR   GO; GO:0102318; F:2-deoxystreptamine glucosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102319; F:2-deoxystreptamine N-acetyl-D-glucosaminyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016758; F:hexosyltransferase activity; IDA:UniProtKB.
DR   GO; GO:1901133; P:kanamycin biosynthetic process; IDA:UniProtKB.
DR   InterPro; IPR001296; Glyco_trans_1.
DR   InterPro; IPR028098; Glyco_trans_4-like_N.
DR   Pfam; PF13579; Glyco_trans_4_4; 1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Glycosyltransferase; Transferase.
FT   CHAIN           1..387
FT                   /note="2-deoxystreptamine glucosyltransferase"
FT                   /id="PRO_0000421740"
SQ   SEQUENCE   387 AA;  41613 MW;  7B6CE91313A63CB0 CRC64;
     MQVQILRMSR ALAELGVRQQ VLTVGFPGLP RVRRDSENLV VRITRAPLPR LRSRITGLVG
     LNQAWLAAAL TECVKLRRRW PADLIQVHLD GQLWALLAGP VAARLVGVPY TVTVHCSRLA
     VYQPMSTVDR IQHPLVTAVE RWALRRAAGI TTLTERTATV LAAELGAAQR VIDVVPDAVD
     PDRAEAAPAE VERLKKRFGL PQEGGPVIGF VGRIAHEKGW RHAVQAVAEL ADAGRDFTFL
     VVGDGPQRAD MEAAVAEAGL TDRFVFTGFL PNDEIPAVMT ALDVLLMPSV HEELGGSAVE
     AMLAGTPVAA YGVGGLCDTV GKVTPSLLAA PGQVAELART VKRVLDDPAP VLAELRAGRE
     WLADEFGVHH AAGLALAHYE RVLGKER