CHMJ_STRBI
ID CHMJ_STRBI Reviewed; 196 AA.
AC Q5SFD1;
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-deoxyglucose 3-epimerase {ECO:0000305|PubMed:23116432};
DE EC=5.1.3.27 {ECO:0000269|PubMed:23116432};
DE AltName: Full=dTDP-4-dehydro-6-deoxy-D-glucose 3-epimerase {ECO:0000305|PubMed:23116432};
DE AltName: Full=dTDP-4-keto-6-deoxyglucose epimerase {ECO:0000305|PubMed:23116432};
DE AltName: Full=dTDP-4-oxo-6-deoxy-D-glucose epimerase {ECO:0000305|PubMed:23116432};
GN Name=chmJ {ECO:0000303|PubMed:15561847};
OS Streptomyces bikiniensis.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1896;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
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 X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF APOENZYME; COMPLEX WITH
RP DTDP-QUINOVOSE AND MUTANT ASN-60/PHE-130 IN COMPLEX WITH DTDP, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITES,
RP AND MUTAGENESIS OF HIS-60 AND TYR-130.
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: Involved in the biosynthesis of dTDP-6-deoxy-D-allose, an
CC intermediate in the biosynthesis of mycinose, which is one of the two
CC unusual sugars attached to the 16-membered macrolactone ring of the
CC aglycone antibiotic chalcomycin. Catalyzes the conversion of dTDP-4-
CC oxo-6-deoxyglucose to dTDP-4-oxo-6-deoxyallose, via a C-3
CC epimerization. {ECO:0000269|PubMed:23116432,
CC ECO:0000305|PubMed:15561847}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-6-
CC deoxy-alpha-D-allose; Xref=Rhea:RHEA:36971, ChEBI:CHEBI:57649,
CC ChEBI:CHEBI:76253; EC=5.1.3.27;
CC Evidence={ECO:0000269|PubMed:23116432};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.4 mM for dTDP-4-dehydro-6-deoxy-alpha-D-glucose
CC {ECO:0000269|PubMed:23116432};
CC Note=kcat is 6.4 sec(-1). {ECO:0000269|PubMed:23116432};
CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000305|PubMed:15561847}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:23116432}.
CC -!- SIMILARITY: Belongs to the dTDP-4-dehydrorhamnose 3,5-epimerase family.
CC {ECO:0000305}.
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DR EMBL; AY509120; AAS79451.1; -; Genomic_DNA.
DR PDB; 4HMZ; X-ray; 2.00 A; A/B/C/D=1-196.
DR PDB; 4HN0; X-ray; 2.20 A; A/B/C/D=1-196.
DR PDB; 4HN1; X-ray; 1.60 A; A/B/C/D=1-196.
DR PDBsum; 4HMZ; -.
DR PDBsum; 4HN0; -.
DR PDBsum; 4HN1; -.
DR AlphaFoldDB; Q5SFD1; -.
DR SMR; Q5SFD1; -.
DR GO; GO:0008830; F:dTDP-4-dehydrorhamnose 3,5-epimerase activity; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR000888; dTDP_sugar_isom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR PANTHER; PTHR21047; PTHR21047; 1.
DR Pfam; PF00908; dTDP_sugar_isom; 1.
DR SUPFAM; SSF51182; SSF51182; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic biosynthesis; Carbohydrate metabolism; Isomerase.
FT CHAIN 1..196
FT /note="dTDP-4-dehydro-6-deoxyglucose 3-epimerase"
FT /id="PRO_0000425106"
FT ACT_SITE 60
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:23116432"
FT ACT_SITE 130
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:23116432"
FT BINDING 21
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23116432,
FT ECO:0007744|PDB:4HN1"
FT BINDING 26
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23116432,
FT ECO:0007744|PDB:4HN1"
FT BINDING 45..47
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23116432,
FT ECO:0007744|PDB:4HMZ, ECO:0007744|PDB:4HN1"
FT BINDING 57
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23116432,
FT ECO:0007744|PDB:4HN1"
FT BINDING 70
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23116432,
FT ECO:0007744|PDB:4HN1"
FT BINDING 117
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23116432,
FT ECO:0007744|PDB:4HN1"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23116432,
FT ECO:0007744|PDB:4HN1"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT SITE 136
FT /note="Participates in a stacking interaction with the
FT thymidine ring of dTDP-4-oxo-6-deoxyglucose"
FT /evidence="ECO:0000269|PubMed:23116432,
FT ECO:0007744|PDB:4HN1"
FT MUTAGEN 60
FT /note="H->N: No effect on substrate affinity, but 2400-fold
FT reduction in activity."
FT /evidence="ECO:0000269|PubMed:23116432"
FT MUTAGEN 130
FT /note="Y->F: Slight decrease in substrate affinity, and
FT 1650-fold reduction in activity."
FT /evidence="ECO:0000269|PubMed:23116432"
FT STRAND 9..12
FT /evidence="ECO:0007829|PDB:4HN1"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:4HN1"
FT STRAND 22..29
FT /evidence="ECO:0007829|PDB:4HN1"
FT HELIX 30..37
FT /evidence="ECO:0007829|PDB:4HN1"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:4HN1"
FT STRAND 55..62
FT /evidence="ECO:0007829|PDB:4HN1"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:4HN1"
FT STRAND 70..84
FT /evidence="ECO:0007829|PDB:4HN1"
FT TURN 91..94
FT /evidence="ECO:0007829|PDB:4HN1"
FT STRAND 96..102
FT /evidence="ECO:0007829|PDB:4HN1"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:4HN1"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:4HN1"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:4HN1"
FT STRAND 126..134
FT /evidence="ECO:0007829|PDB:4HN1"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:4HN1"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:4HN1"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:4HN1"
FT HELIX 165..168
FT /evidence="ECO:0007829|PDB:4HN1"
FT HELIX 173..178
FT /evidence="ECO:0007829|PDB:4HN1"
FT HELIX 185..196
FT /evidence="ECO:0007829|PDB:4HN1"
SQ SEQUENCE 196 AA; 21683 MW; 26C8CD880701F1CA CRC64;
MHPLSIEGAW SQEPVIHSDH RGRSHEWFRG ESFRQAFGHD FPVAQVNVAV SHRGALRGIH
YTEIPPGQAK YSVCVRGAGL DVVVDVRIGS PTFGRWEIVP MDAERNTAVY LTAGLGRAFL
SLTDDATLVY LCSSGYAPAR EHSVNPLDPD LGIAWPDDIE PLLSDRDENA PTLATAERLG
LLPTYQAWQE QQQAQR
