ID   CHMD_STRBI              Reviewed;         326 AA.
AC   Q5SFA6;
DT   22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=dTDP-4-dehydro-6-deoxy-D-allose reductase {ECO:0000305|PubMed:23116432};
DE            EC=1.1.1.364 {ECO:0000269|PubMed:23116432};
DE   AltName: Full=dTDP-4-dehydro-6-deoxy-alpha-D-gulose 4-ketoreductase {ECO:0000305};
DE   AltName: Full=dTDP-4-keto-6-deoxyallose reductase {ECO:0000303|PubMed:23116432};
GN   Name=chmD;
OS   Streptomyces bikiniensis.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1896;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NRRL 2737;
RX   PubMed=15561847; DOI=10.1128/aac.48.12.4703-4712.2004;
RA   Ward S.L., Hu Z., Schirmer A., Reid R., Revill W.P., Reeves C.D.,
RA   Petrakovsky O.V., Dong S.D., Katz L.;
RT   "Chalcomycin biosynthesis gene cluster from Streptomyces bikiniensis: novel
RT   features of an unusual ketolide produced through expression of the chm
RT   polyketide synthase in Streptomyces fradiae.";
RL   Antimicrob. Agents Chemother. 48:4703-4712(2004).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=NRRL 2737;
RX   PubMed=23116432; DOI=10.1021/bi3012737;
RA   Kubiak R.L., Phillips R.K., Zmudka M.W., Ahn M.R., Maka E.M., Pyeatt G.L.,
RA   Roggensack S.J., Holden H.M.;
RT   "Structural and functional studies on a 3'-epimerase involved in the
RT   biosynthesis of dTDP-6-deoxy-D-allose.";
RL   Biochemistry 51:9375-9383(2012).
CC   -!- FUNCTION: Catalyzes the stereospecific reduction of the C-4 keto group
CC       of dTDP-4-dehydro-6-deoxy-D-allose, leading to dTDP-6-deoxy-D-allose,
CC       an intermediate in the biosynthesis of the mycinose moiety of the
CC       chalcomycin antibiotic. {ECO:0000269|PubMed:23116432}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dTDP-6-deoxy-alpha-D-allose + NAD(+) = dTDP-4-dehydro-6-deoxy-
CC         alpha-D-allose + H(+) + NADH; Xref=Rhea:RHEA:36679,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:74143, ChEBI:CHEBI:76253; EC=1.1.1.364;
CC         Evidence={ECO:0000269|PubMed:23116432};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dTDP-6-deoxy-alpha-D-allose + NADP(+) = dTDP-4-dehydro-6-
CC         deoxy-alpha-D-allose + H(+) + NADPH; Xref=Rhea:RHEA:39883,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:74143, ChEBI:CHEBI:76253; EC=1.1.1.364;
CC         Evidence={ECO:0000269|PubMed:23116432};
CC   -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC       family. {ECO:0000305}.
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DR   EMBL; AY509120; AAS79455.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5SFA6; -.
DR   SMR; Q5SFA6; -.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR001509; Epimerase_deHydtase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF01370; Epimerase; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Carbohydrate metabolism; NADP; Oxidoreductase.
FT   CHAIN           1..326
FT                   /note="dTDP-4-dehydro-6-deoxy-D-allose reductase"
FT                   /id="PRO_0000425104"
FT   ACT_SITE        160
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         15..21
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         129..132
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         164
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         187..190
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   SITE            164
FT                   /note="Lowers pKa of active site Tyr"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   326 AA;  36411 MW;  8F5CA0CBB64BD70B CRC64;
     MTADRWAGRT VLVTGALGFI GSHFVRQLEA RGAEVLALYR TERPQLQAEL AALDRVRLIR
     TELRDESDVR GAFKYLAPSI DTVVHCAAMD GNAQFKLERS AEILDSNQRT ISHLLNCVRD
     FGVGEAVVMS SSELYCAPPT AAAHEDDDFR RSMRYTDNGY VLSKTYGEIL ARLHREQFGT
     NVFLVRPGNV YGPGDGYDPS RGRVIPSMLA KADAGEEIEI WGDGSQTRSF IHVTDLVRAS
     LRLLETGKYP EMNVAGAEQV SILELARMVM AVLGRPERIR LDPGRPVGAP SRLLDLTRMS
     EVIDFEPQPL RTGLEETARW FRHHTR