RMLB_STRGR
ID RMLB_STRGR Reviewed; 328 AA.
AC P29782;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=dTDP-glucose 4,6-dehydratase {ECO:0000250|UniProtKB:P27830};
DE EC=4.2.1.46 {ECO:0000250|UniProtKB:P27830};
GN Name=strE {ECO:0000303|PubMed:1661369};
OS Streptomyces griseus.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1911;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN BIOSYNTHESIS OF THE
RP STREPTOSE MOIETY OF STREPTOMYCIN, AND PATHWAY.
RC STRAIN=N2-3-11;
RX PubMed=1661369; DOI=10.1007/bf00293829;
RA Pissowotzki K., Mansouri K., Piepersberg W.;
RT "Genetics of streptomycin production in Streptomyces griseus: molecular
RT structure and putative function of genes strELMB2N.";
RL Mol. Gen. Genet. 231:113-123(1991).
CC -!- FUNCTION: Involved in the biosynthesis of the streptose moiety of
CC streptomycin (PubMed:1661369). Catalyzes the dehydration of dTDP-D-
CC glucose to form dTDP-6-deoxy-D-xylo-4-hexulose via a three-step process
CC involving oxidation, dehydration and reduction (By similarity).
CC {ECO:0000250|UniProtKB:P27830, ECO:0000269|PubMed:1661369}.
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; streptomycin biosynthesis.
CC {ECO:0000305|PubMed:1661369}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P27830}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. dTDP-glucose dehydratase subfamily. {ECO:0000305}.
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DR EMBL; X62567; CAA44444.1; -; Genomic_DNA.
DR PIR; S18617; DWSMGG.
DR AlphaFoldDB; P29782; -.
DR SMR; P29782; -.
DR UniPathway; UPA00066; -.
DR GO; GO:0008460; F:dTDP-glucose 4,6-dehydratase activity; ISS:UniProtKB.
DR GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; ISS:UniProtKB.
DR GO; GO:0009225; P:nucleotide-sugar metabolic process; IEA:InterPro.
DR GO; GO:0019872; P:streptomycin biosynthetic process; IEA:UniProtKB-UniPathway.
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 Pfam; PF16363; GDP_Man_Dehyd; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01181; dTDP_gluc_dehyt; 1.
PE 1: Evidence at protein level;
KW Antibiotic biosynthesis; Lyase; NAD; Streptomycin biosynthesis.
FT CHAIN 1..328
FT /note="dTDP-glucose 4,6-dehydratase"
FT /id="PRO_0000183248"
FT ACT_SITE 127
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT ACT_SITE 128
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT ACT_SITE 150
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT BINDING 13..14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT BINDING 37..40
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT BINDING 63..64
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT BINDING 82..86
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26391"
FT BINDING 101
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT BINDING 126
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26391"
FT BINDING 150..154
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT BINDING 179
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26391"
FT BINDING 180
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT BINDING 189..190
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26391"
FT BINDING 205..207
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26391"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26391"
FT BINDING 249
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26391"
FT BINDING 272..276
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26391"
SQ SEQUENCE 328 AA; 35669 MW; AA259ED8F109E581 CRC64;
MTTHLLVTGA AGFIGSQYVR TLLGPGGPPD VVVTALDALT YAGNPDNLAA VRGHPRYRFE
RGDICDAPGR RVMAGQDQVV HLAAESHVDR SLLDASVFVR TNVHGTQTLL DAATRHGVAS
FVQVSTDEVY GSLEHGSWTE DEPLRPNSPY SASKASGDLL ALAHHVSHGL DVRVTRCSNN
YGPRQFPEKL IPRFITLLMD GHRVPLYGDG LNVREWLHVD DHVRGIEAVR TRGRAGRVYN
IGGGATLSNK ELVGLLLEAA GADWGSVEYV EDRKGHDRRY AVDSTRIQRE LGFAPAVDLA
DGLAATVAWY HKHRSWWEPL VPAGSLPA
