OLEE_STRAT
ID OLEE_STRAT Reviewed; 335 AA.
AC Q9RR28;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=dTDP-glucose 4,6-dehydratase {ECO:0000303|PubMed:10770761};
DE EC=4.2.1.46 {ECO:0000250|UniProtKB:P27830};
GN Name=oleE {ECO:0000303|PubMed:10770761};
OS Streptomyces antibioticus.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1890 {ECO:0000312|EMBL:AAD55454.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RC STRAIN=ATCC 11891 / DSM 40868 / BCRC 11580 / NCIMB 11506 / PSA 205
RC {ECO:0000312|EMBL:AAD55454.1};
RX PubMed=10770761; DOI=10.1128/aac.44.5.1266-1275.2000;
RA Aguirrezabalaga I., Olano C., Allende N., Rodriguez L., Brana A.F.,
RA Mendez C., Salas J.A.;
RT "Identification and expression of genes involved in biosynthesis of L-
RT oleandrose and its intermediate L-olivose in the oleandomycin producer
RT Streptomyces antibioticus.";
RL Antimicrob. Agents Chemother. 44:1266-1275(2000).
CC -!- FUNCTION: Involved in the biosynthesis of the two 2,6-deoxysugars,
CC dTDP-L-oleandrose and dTDP-D-desosamine, attached to the macrolactone
CC ring oleandolide to produce the aglycone antibiotic oleandomycin
CC (PubMed:10770761). Catalyzes the dehydration of dTDP-D-glucose to form
CC dTDP-6-deoxy-D-xylo-4-hexulose via a three-step process involving
CC oxidation, dehydration and reduction (By similarity).
CC {ECO:0000250|UniProtKB:P27830, ECO:0000269|PubMed:10770761}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dTDP-alpha-D-glucose = dTDP-4-dehydro-6-deoxy-alpha-D-glucose
CC + H2O; Xref=Rhea:RHEA:17221, ChEBI:CHEBI:15377, ChEBI:CHEBI:57477,
CC ChEBI:CHEBI:57649; EC=4.2.1.46;
CC Evidence={ECO:0000250|UniProtKB:P27830};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000250|UniProtKB:P27830};
CC Note=Binds 1 NAD(+) per subunit. {ECO:0000250|UniProtKB:P27830};
CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000305|PubMed:10770761}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. dTDP-glucose dehydratase subfamily. {ECO:0000305}.
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DR EMBL; AF055579; AAD55454.1; -; Genomic_DNA.
DR PIR; T51106; T51106.
DR AlphaFoldDB; Q9RR28; -.
DR SMR; Q9RR28; -.
DR BioCyc; MetaCyc:MON-17068; -.
DR GO; GO:0008460; F:dTDP-glucose 4,6-dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009225; P:nucleotide-sugar metabolic process; IEA:InterPro.
DR CDD; cd05246; dTDP_GD_SDR_e; 1.
DR InterPro; IPR005888; dTDP_Gluc_deHydtase.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR Pfam; PF16363; GDP_Man_Dehyd; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01181; dTDP_gluc_dehyt; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 3: Inferred from homology;
KW Antibiotic biosynthesis; Lyase; NAD.
FT CHAIN 1..335
FT /note="dTDP-glucose 4,6-dehydratase"
FT /id="PRO_0000444209"
FT ACT_SITE 126
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT ACT_SITE 127
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT ACT_SITE 149
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT BINDING 11..12
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT BINDING 38..41
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT BINDING 61..62
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT BINDING 81..85
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT BINDING 85
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26391"
FT BINDING 100
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26391"
FT BINDING 149..153
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26391"
FT BINDING 179
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT BINDING 188..189
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26391"
FT BINDING 204..206
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26391"
FT BINDING 213
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26391"
FT BINDING 248
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26391"
FT BINDING 271..275
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26391"
SQ SEQUENCE 335 AA; 36665 MW; 14DA18D6840C2A48 CRC64;
MNLLVTGAAG FIGSRYVHHL LEATRRGREP APVITVLDKL TYAGVLGNVP DDPAVTFVRG
DIADAPLVDS LMAEADQVVH FAAETHVDRS ITSPGTFVRT NVLGTQVLLD AALRHGVGPF
VHVSTDEVYG SIEHGSWPEH QPLCPNSPYS ASKASSDLLA LSYHRTHGLD VRVTRCSNNY
GPHQFPEKIV PLFVTNLLDG LRVPLYGDGL NVREWLHVDD HCLGVDLVRT QGRPGEVYHI
GGGTELTNRD LTGLLLDAFG VGWDVVDPVA DRKGHDRRYA LDCAKAADEL GYRPRRDFAE
GIARTIDWYR DNRAWWEPLK KRPAGPAAPP RGSGP
