ID   AKNT_STRGJ              Reviewed;         443 AA.
AC   Q9L4U5;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Protein AknT {ECO:0000303|PubMed:15911373};
GN   Name=AknT {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.
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.
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. AknT is required for the glycosylation of
CC       aklavinone aglycone by AknS to yield aclacinomycin T (rhodosaminyl-
CC       aklavinone). {ECO:0000269|PubMed:15911373,
CC       ECO:0000269|PubMed:17685523}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC   -!- CAUTION: Although AknT shows significant similarity to cytochrome P450
CC       family, it lacks the heme-binding sites. The conservation of amino acid
CC       sequence is confined primarily to the C-terminal half of the protein.
CC       {ECO:0000305}.
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DR   EMBL; AF264025; AAF73456.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9L4U5; -.
DR   SMR; Q9L4U5; -.
DR   KEGG; ag:AAF73456; -.
DR   SABIO-RK; Q9L4U5; -.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR002397; Cyt_P450_B.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   InterPro; IPR030958; P450-rel_GT_act.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00359; BP450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   TIGRFAMs; TIGR04515; P450_rel_GT_act; 1.
PE   3: Inferred from homology;
KW   Antibiotic biosynthesis.
FT   CHAIN           1..443
FT                   /note="Protein AknT"
FT                   /id="PRO_0000430687"
SQ   SEQUENCE   443 AA;  46835 MW;  73892468793140DD CRC64;
     MQTQNAPETA ENQQTDSELG RHLLTARGFH WIYGTSGDPY ALTLRAESDD PALLTRRIRE
     AGTPLWQSTT GAWVTGRHGV AAEALADPRL ALRHADLPGP QRHVFSDAWS NPQLCHIIPL
     DRAFLHASDA DHTRWARSAS AVLGSAGGAP AEGVREHAGR VHREAADRTG DSFDLMADYS
     RPVATEAAAE LLGVPAAQRE RFAATCLALG VALDAALCPQ PLAVTRRLTE AVEDVRALVG
     DLVEARRTQP GDDLLSAVLH AGSSAASAGQ DALAVGVLTA VVGVEVTAGL INNTLESLLT
     RPVQWARLGE NPELAAGAVE EALRFAPPVR LESRIAAEDL TLGGQDLPAG AQVVVHVGAA
     NRDPEAFLAP DHFDLDRPAG QGQLSLSGPH TALFGAFARL QAETAVRTLR ERRPVLAPAG
     AVLRRMRSPV LGAVLRFPLT TSA