ID   DES8_STRVZ              Reviewed;         402 AA.
AC   Q9ZGH8;
DT   16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Protein DesVIII {ECO:0000303|PubMed:15161264};
DE   AltName: Full=Inactive cytochrome DesVIII;
GN   Name=desVIII {ECO:0000303|PubMed:9770448};
OS   Streptomyces venezuelae.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=54571;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 15439 / DSM 41110 / IMRU3627 / M-2140;
RX   PubMed=9770448; DOI=10.1073/pnas.95.21.12111;
RA   Xue Y., Zhao L., Liu H.W., Sherman D.H.;
RT   "A gene cluster for macrolide antibiotic biosynthesis in Streptomyces
RT   venezuelae: architecture of metabolic diversity.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:12111-12116(1998).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=15161264; DOI=10.1021/ja049967j;
RA   Borisova S.A., Zhao L., Melancon C.E. III, Kao C.L., Liu H.W.;
RT   "Characterization of the glycosyltransferase activity of desVII: analysis
RT   of and implications for the biosynthesis of macrolide antibiotics.";
RL   J. Am. Chem. Soc. 126:6534-6535(2004).
RN   [3]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 15439 / DSM 41110 / IMRU3627 / M-2140;
RX   PubMed=17049185; DOI=10.1016/j.gene.2006.08.021;
RA   Hong J.S., Park S.J., Parajuli N., Park S.R., Koh H.S., Jung W.S.,
RA   Choi C.Y., Yoon Y.J.;
RT   "Functional analysis of desVIII homologues involved in glycosylation of
RT   macrolide antibiotics by interspecies complementation.";
RL   Gene 386:123-130(2007).
RN   [4]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND SUBUNIT.
RC   STRAIN=ATCC 15439 / DSM 41110 / IMRU3627 / M-2140;
RX   PubMed=20695498; DOI=10.1021/bi1007657;
RA   Borisova S.A., Liu H.W.;
RT   "Characterization of glycosyltransferase DesVII and its auxiliary partner
RT   protein DesVIII in the methymycin/picromycin biosynthetic pathway.";
RL   Biochemistry 49:8071-8084(2010).
CC   -!- FUNCTION: Involved in the biosynthesis of the macrolide antibiotics
CC       methymycin, neomethymycin, narbomycin, and pikromycin. DesVIII assists
CC       the folding of the DesVII polypeptide. However, unlike chaperones, it
CC       remains bound to DesVII during catalysis, forming a tight
CC       DesVII/DesVIII complex. Although the formation of the DesVII/DesVIII
CC       complex is essential for the catalytic activity, DesVIII is unlikely to
CC       be involved in catalysis directly. {ECO:0000269|PubMed:15161264,
CC       ECO:0000269|PubMed:17049185, ECO:0000269|PubMed:20695498}.
CC   -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000305|PubMed:20695498}.
CC   -!- SUBUNIT: Forms a complex with DesVII. {ECO:0000269|PubMed:20695498}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene are not able to produce
CC       glycosylated macrolides. {ECO:0000269|PubMed:15161264,
CC       ECO:0000269|PubMed:17049185, ECO:0000269|PubMed:20695498}.
CC   -!- MISCELLANEOUS: EryCII, OleP1 and DnrQ are able to replace DesVIII,
CC       however the total amount of glycosylated compounds is significantly
CC       reduced. {ECO:0000269|PubMed:17049185, ECO:0000269|PubMed:20695498}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC   -!- CAUTION: Although DesVIII shows significant similarity to cytochrome
CC       P450 family, it lacks the heme-binding sites. The conservation of amino
CC       acid sequence is confined primarily to the C-terminal half of the
CC       protein. {ECO:0000305}.
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DR   EMBL; AF079762; AAC68676.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9ZGH8; -.
DR   SMR; Q9ZGH8; -.
DR   KEGG; ag:AAC68676; -.
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; IMP:UniProtKB.
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   1: Evidence at protein level;
KW   Antibiotic biosynthesis.
FT   CHAIN           1..402
FT                   /note="Protein DesVIII"
FT                   /id="PRO_0000435702"
SQ   SEQUENCE   402 AA;  41996 MW;  A0EF6967886672A0 CRC64;
     MTDDLTGALT QPPLGRTVRA VADRELGTHL LETRGIHWIH AANGDPYATV LRGQADDPYP
     AYERVRARGA LSFSPTGSWV TADHALAASI LCSTDFGVSG ADGVPVPQQV LSYGEGCPLE
     REQVLPAAGD VPEGGQRAVV EGIHRETLEG LAPDPSASYA FELLGGFVRP AVTAAAAAVL
     GVPADRRADF ADLLERLRPL SDSLLAPQSL RTVRAADGAL AELTALLADS DDSPGALLSA
     LGVTAAVQLT GNAVLALLAH PEQWRELCDR PGLAAAAVEE TLRYDPPVQL DARVVRGETE
     LAGRRLPAGA HVVVLTAATG RDPEVFTDPE RFDLARPDAA AHLALHPAGP YGPVASLVRL
     QAEVALRTLA GRFPGLRQAG DVLRPRRAPV GRGPLSVPVS SS