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AKNS_STRGJ
ID   AKNS_STRGJ              Reviewed;         443 AA.
AC   Q9L4U6;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Aklavinone 7-beta-L-rhodosaminyltransferase {ECO:0000303|PubMed:15911373};
DE            EC=2.4.1.326 {ECO:0000269|PubMed:15911373, ECO:0000269|PubMed:17685523};
DE   Flags: Precursor;
GN   Name=aknS {ECO:0000303|PubMed:15911373};
OS   Streptomyces galilaeus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=33899;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 31615;
RX   PubMed=11016846; DOI=10.1007/s004380000306;
RA   Raty K., Kunnari T., Hakala J., Mantsala P., Ylihonko K.;
RT   "A gene cluster from Streptomyces galilaeus involved in glycosylation of
RT   aclarubicin.";
RL   Mol. Gen. Genet. 264:164-172(2000).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP   REGULATION, AND SUBSTRATE SPECIFICITY.
RC   STRAIN=ATCC 31615;
RX   PubMed=15911373; DOI=10.1016/j.chembiol.2005.02.016;
RA   Lu W., Leimkuhler C., Gatto G.J. Jr., Kruger R.G., Oberthuer M., Kahne D.,
RA   Walsh C.T.;
RT   "AknT is an activating protein for the glycosyltransferase AknS in L-
RT   aminodeoxysugar transfer to the aglycone of aclacinomycin A.";
RL   Chem. Biol. 12:527-534(2005).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP   REGULATION, AND SUBSTRATE SPECIFICITY.
RC   STRAIN=ATCC 31615;
RX   PubMed=17685523; DOI=10.1021/ja072909o;
RA   Leimkuhler C., Fridman M., Lupoli T., Walker S., Walsh C.T., Kahne D.;
RT   "Characterization of rhodosaminyl transfer by the AknS/AknT glycosylation
RT   complex and its use in reconstituting the biosynthetic pathway of
RT   aclacinomycin A.";
RL   J. Am. Chem. Soc. 129:10546-10550(2007).
CC   -!- FUNCTION: Involved in the biosynthesis of the anthracycline antitumor
CC       agent aclacinomycin A. Catalyzes the transfer of the proximal
CC       deoxyhexose, L-rhodosamine, from dTDP-beta-L-rhodosamine to the C7-OH
CC       of aklavinone aglycone to yield aclacinomycin T (rhodosaminyl-
CC       aklavinone). It can also use dTDP-2-deoxy-beta-L-fucose, TDP-2-
CC       deoxyfucose, dTDP-4-amino-2-deoxyrhamnose, TDP-L-rhodosamine as sugar
CC       donor and epsilon-rhodomycinone as sugar acceptor.
CC       {ECO:0000269|PubMed:15911373, ECO:0000269|PubMed:17685523}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=aklavinone + dTDP-beta-L-rhodosamine = aclacinomycin T + dTDP
CC         + 2 H(+); Xref=Rhea:RHEA:41564, ChEBI:CHEBI:15378, ChEBI:CHEBI:31181,
CC         ChEBI:CHEBI:58369, ChEBI:CHEBI:77979, ChEBI:CHEBI:78301;
CC         EC=2.4.1.326; Evidence={ECO:0000269|PubMed:15911373,
CC         ECO:0000269|PubMed:17685523};
CC   -!- ACTIVITY REGULATION: The activity of AknS is substantially increased by
CC       the addition of the accessory protein AknT.
CC       {ECO:0000269|PubMed:15911373, ECO:0000269|PubMed:17685523}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=3.1 uM for aklavinone (with dTDP-4-amino-2-deoxyrhamnose as sugar
CC         donor) {ECO:0000269|PubMed:15911373};
CC         KM=3.5 uM for aklavinone (with TDP-2-deoxyfucose as sugar donor)
CC         {ECO:0000269|PubMed:15911373};
CC         KM=5.7 uM for aklavinone (with TDP-L-rhodosamine as sugar donor)
CC         {ECO:0000269|PubMed:17685523};
CC         KM=13 uM for aklavinone (without AknT and with TDP-L-rhodosamine as
CC         sugar donor) {ECO:0000269|PubMed:17685523};
CC         KM=46 uM for epsilon-rhodomycinone (with TDP-2-deoxyfucose as sugar
CC         donor) {ECO:0000269|PubMed:15911373};
CC         KM=156 uM for dTDP-2-deoxyfucose (with epsilon-rhodomycinone as sugar
CC         acceptor) {ECO:0000269|PubMed:15911373};
CC         KM=280 uM for TDP-L-rhodosamine (with aklavinone as sugar acceptor)
CC         {ECO:0000269|PubMed:17685523};
CC         KM=287 uM for TDP-2-deoxyfucose (with aklavinone as sugar acceptor)
CC         {ECO:0000269|PubMed:15911373};
CC         KM=349 uM for TDP-L-rhodosamine (without AknT and with aklavinone as
CC         sugar acceptor) {ECO:0000269|PubMed:17685523};
CC         KM=407 uM for dTDP-4-amino-2-deoxyrhamnose (with aklavinone as sugar
CC         acceptor) {ECO:0000269|PubMed:15911373};
CC         Note=kcat is 9.6 sec(-1) for glycosyltransferase activity with
CC         aklavinone as sugar acceptor and TDP-L-rhodosamine as sugar donor.
CC         kcat is 0.05 sec(-1) for glycosyltransferase activity without AknT
CC         and with aklavinone as sugar acceptor and TDP-L-rhodosamine as sugar
CC         donor. kcat is 0.17 min(-1) for glycosyltransferase activity with
CC         aklavinone as sugar acceptor and dTDP-4-amino-2-deoxyrhamnose as
CC         sugar donor. kcat is 0.082 min(-1) for glycosyltransferase activity
CC         with epsilon-rhodomycinone as sugar acceptor and TDP-2-deoxyfucose as
CC         sugar donor. {ECO:0000269|PubMed:15911373,
CC         ECO:0000269|PubMed:17685523};
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 28 family.
CC       {ECO:0000305}.
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DR   EMBL; AF264025; AAF73455.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9L4U6; -.
DR   SMR; Q9L4U6; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   KEGG; ag:AAF73455; -.
DR   BioCyc; MetaCyc:MON-18192; -.
DR   SABIO-RK; Q9L4U6; -.
DR   GO; GO:0016758; F:hexosyltransferase activity; IEA:UniProt.
DR   GO; GO:0008194; F:UDP-glycosyltransferase activity; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd03784; GT1_Gtf-like; 1.
DR   InterPro; IPR010610; DUF1205.
DR   InterPro; IPR030953; Glycosyl_450act.
DR   InterPro; IPR002213; UDP_glucos_trans.
DR   Pfam; PF06722; DUF1205; 1.
DR   TIGRFAMs; TIGR04516; glycosyl_450act; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Glycosyltransferase; Signal; Transferase.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..443
FT                   /note="Aklavinone 7-beta-L-rhodosaminyltransferase"
FT                   /id="PRO_0000430688"
SQ   SEQUENCE   443 AA;  47454 MW;  1BDAB3FBEEE05768 CRC64;
     MRVLLTSFAL DAHFNGSVPL AWALRAAGHE VRVASQPALT ASITAAGLTA VPVGADPRLD
     EMVKGVGDAV LSHHADQSLD ADTPGQLTPA FLQGWDTMMT ATFYTLINDD PMVDDLVAFA
     RGWEPDLILW EPFTFAGAVA AKVTGAAHAR LLSFPDLFMS MRRAYLAQLG AAPAGPAGGN
     GTTHPDDSLG QWLEWTLGRY GVPFDEEAVT GQWSVDQVPR SFRPPSDRPV VGMRYVPYNG
     PGPAVVPDWL RVPPTRPRVC VTLGMTARTS EFPNAVPVDL VLKAVEGLDI EVVATLDAEE
     RALLTHVPDN VRLVDHVPLH ALLPTCAAIV HHGGAGTWST ALVEGVPQIA MGWIWDAIDR
     AQRQQALGAG LHLPSHEVTV EGLRGRLVRL LDEPSFTAAA ARLRAEAESE PTPAQVVPVL
     ERLTAQHRAR EPRRPGGTSP CVS
 
 
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