KANE_STRKN
ID KANE_STRKN Reviewed; 386 AA.
AC Q65CC7;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Alpha-D-kanosaminyltransferase;
DE EC=2.4.1.301;
DE AltName: Full=2'-deamino-2'-hydroxyneamine 1-alpha-D-kanosaminyltransferase;
DE AltName: Full=Glycosyltransferase KanE;
DE AltName: Full=Kanamycin biosynthesis protein E;
GN Name=kanE;
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
CC kanamycins by catalyzing the transfer of the hexose kanosamine from
CC UDP-alpha-D-kanosamine to disaccharide precursors. Can also use UDP-
CC alpha-D-glucose as sugar donor with much lower efficiency.
CC {ECO:0000269|PubMed:21983602}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deamino-2'-hydroxyneamine + UDP-alpha-D-kanosamine = H(+) +
CC kanamycin A + UDP; Xref=Rhea:RHEA:35795, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58214, ChEBI:CHEBI:58223, ChEBI:CHEBI:67213,
CC ChEBI:CHEBI:71964; EC=2.4.1.301;
CC Evidence={ECO:0000269|PubMed:21983602};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=neamine + UDP-alpha-D-kanosamine = H(+) + kanamycin B + UDP;
CC Xref=Rhea:RHEA:35783, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:58549, ChEBI:CHEBI:65076, ChEBI:CHEBI:71964;
CC EC=2.4.1.301; Evidence={ECO:0000269|PubMed:21983602};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=paromamine + UDP-alpha-D-kanosamine = H(+) + kanamycin C +
CC UDP; Xref=Rhea:RHEA:35787, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:65015, ChEBI:CHEBI:71964, ChEBI:CHEBI:72755;
CC EC=2.4.1.301; Evidence={ECO:0000269|PubMed:21983602};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deamino-2'-hydroxyparomamine + UDP-alpha-D-kanosamine =
CC H(+) + kanamycin X + UDP; Xref=Rhea:RHEA:35791, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:65071, ChEBI:CHEBI:71964,
CC ChEBI:CHEBI:72756; EC=2.4.1.301;
CC Evidence={ECO:0000269|PubMed:21983602};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.03 mM for UDP-alpha-D-kanosamine {ECO:0000269|PubMed:21983602};
CC KM=0.26 mM for UDP-alpha-D-glucose {ECO:0000269|PubMed:21983602};
CC KM=0.05 mM for paromamine (in the presence of UDP-alpha-D-kanosamine
CC as cosubstrate) {ECO:0000269|PubMed:21983602};
CC KM=0.25 mM for paromamine (in the presence of UDP-alpha-D-glucose as
CC cosubstrate) {ECO:0000269|PubMed:21983602};
CC Note=kcat is 3.36 min(-1) and 3.18 min(-1) for the reaction with
CC paromamine as acceptor and UDP-alpha-D-kanosamine or UDP-alpha-D-
CC glucose as donor, respectively.;
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; CAE46941.1; -; Genomic_DNA.
DR AlphaFoldDB; Q65CC7; -.
DR SMR; Q65CC7; -.
DR KEGG; ag:CAE46941; -.
DR BioCyc; MetaCyc:MON-17222; -.
DR BRENDA; 2.4.1.301; 6046.
DR UniPathway; UPA00965; -.
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; PF13439; Glyco_transf_4; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
PE 1: Evidence at protein level;
KW Antibiotic biosynthesis; Glycosyltransferase; Transferase.
FT CHAIN 1..386
FT /note="Alpha-D-kanosaminyltransferase"
FT /id="PRO_0000421739"
SQ SEQUENCE 386 AA; 43218 MW; 855AE79832E7EB0E CRC64;
MHLLVRALVE EMAGRGVPHR VLTMSPPKVP KDIRIGQRIK VHARRLPVLP IPSDLEGYFG
LVGAWAKGSL LWVLRNRKRL RREIGARVHA HCDGSGAAAF YPYLMSRILG VPLVVQIHSS
RYLSQHPTTL FERVTDPIAK WAERHAVRKA AAVLMLTDRA RDEMRRKAQL PAERVHRLAY
LASDQFKDAD TEARRAELRE RYGLDDRPIV LYVGRIAAEK GVEYYIEAAA ELTRRGRDCQ
FVIAGDGPAR PDLEKLIGAR GLRDRVTITG FMSHEFIPSM ISLGELVVLP SRYEELGIVI
LECMTMRRPL VAHDVNGVNK LIEDGTTGIV VPPFRTPEMA DAVERLLDDP ELRERMAENA
APLPAAKYSL SAAGDQLAGI YREIGL
