GERF_STRSQ
ID GERF_STRSQ Reviewed; 196 AA.
AC Q331R1;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=dTDP-4-dehydro-6-deoxyglucose 3-epimerase {ECO:0000305|PubMed:15049360};
DE EC=5.1.3.27 {ECO:0000269|PubMed:17053005};
DE AltName: Full=dTDP-4-dehydro-6-deoxy-D-glucose 3-epimerase {ECO:0000305|PubMed:15049360};
DE AltName: Full=dTDP-4-keto-6-deoxyglucose epimerase {ECO:0000305|PubMed:15049360};
DE AltName: Full=dTDP-4-oxo-6-deoxy-D-glucose epimerase {ECO:0000305|PubMed:15049360};
GN Name=gerF {ECO:0000303|PubMed:15049360};
OS Streptomyces sp.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1931;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=KCTC 0041BP / GERI-155;
RA Jaishy B.P., Lim S.K., Yoo I.D., Yoo J.C., Sohng J.K., Nam D.H.;
RT "Cloning and characterization of a gene cluster for the production of the
RT polyketide macrolide antibiotic dihydrochalcomycin in Streptomyces sp. KCTC
RT 0041BP.";
RL J. Microbiol. Biotechnol. 16:764-770(2006).
RN [2]
RP FUNCTION, GENE NAME, AND PATHWAY.
RC STRAIN=KCTC 0041BP / GERI-155;
RX PubMed=15049360; DOI=10.1023/b:bile.0000013709.80691.97;
RA Sohng J.K., Kim H.J., Nam D.H., Lim D.O., Han J.M., Lee H.J., Yoo J.C.;
RT "Cloning, expression, and biological function of a dTDP-deoxyglucose
RT epimerase (gerF) gene from Streptomyces sp. GERI-155.";
RL Biotechnol. Lett. 26:185-191(2004).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=KCTC 0041BP / GERI-155;
RX PubMed=17053005; DOI=10.1093/glycob/cwl060;
RA Thuy T.T., Liou K., Oh T.J., Kim D.H., Nam D.H., Yoo J.C., Sohng J.K.;
RT "Biosynthesis of dTDP-6-deoxy-beta-D-allose, biochemical characterization
RT of dTDP-4-keto-6-deoxyglucose reductase (GerKI) from Streptomyces sp. KCTC
RT 0041BP.";
RL Glycobiology 17:119-126(2007).
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 dihydrochalcomycin (GERI-155). Catalyzes the
CC conversion of dTDP-4-oxo-6-deoxyglucose to dTDP-4-oxo-6-deoxyallose,
CC via a C-3 epimerization. {ECO:0000269|PubMed:15049360,
CC ECO:0000269|PubMed:17053005}.
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:17053005};
CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000305|PubMed:15049360}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q5SFD1}.
CC -!- SIMILARITY: Belongs to the dTDP-4-dehydrorhamnose 3,5-epimerase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY118081; ABB52524.1; -; Genomic_DNA.
DR AlphaFoldDB; Q331R1; -.
DR SMR; Q331R1; -.
DR KEGG; ag:ABB52524; -.
DR BioCyc; MetaCyc:MON-18349; -.
DR BRENDA; 5.1.3.27; 1284.
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 Antibiotic biosynthesis; Carbohydrate metabolism; Isomerase.
FT CHAIN 1..196
FT /note="dTDP-4-dehydro-6-deoxyglucose 3-epimerase"
FT /id="PRO_0000425105"
FT ACT_SITE 60
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT ACT_SITE 130
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT BINDING 21
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT BINDING 26
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT BINDING 45..47
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT BINDING 57
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT BINDING 70
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT BINDING 117
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q5SFD1"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9HU21"
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:0000250|UniProtKB:Q5SFD1"
SQ SEQUENCE 196 AA; 21722 MW; D7F6E5CAD9365B12 CRC64;
MHPLSIEGAW SQEPVIHSDH RGRSHEWFRG ERFRQTFGHD FPVAQVNVAV SHRGALRGIH
YTEIPPGQAK YSVCVRGAGL DVIVDVRIGS PTFGRWEIVP MDAERNTAVY LAAGLGRAFL
SLTDDATLVY LCSSGYAPER EHSVNPLDPD LGIVWPADIE PLLSDRDKNA PTLATAERLG
LLPTYQAWQE QQQAKA
