FCF1_ECOLX
ID FCF1_ECOLX Reviewed; 316 AA.
AC Q6E7F2;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=dTDP-4-dehydro-6-deoxyglucose reductase;
DE EC=1.1.1.266;
DE AltName: Full=dTDP-4-dehydro-6-deoxy-D-glucose reductase;
DE AltName: Full=dTDP-4-keto-6-deoxyglucose reductase;
DE AltName: Full=dTDP-6-deoxy-D-xylo-hex-4-ulopyranose reductase;
GN Name=fcf1;
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=O52 / G1066;
RX PubMed=15231783; DOI=10.1128/jb.186.14.4510-4519.2004;
RA Feng L., Senchenkova S.N., Yang J., Shashkov A.S., Tao J., Guo H.,
RA Cheng J., Ren Y., Knirel Y.A., Reeves P.R., Wang L.;
RT "Synthesis of the heteropolysaccharide O antigen of Escherichia coli O52
RT requires an ABC transporter: structural and genetic evidence.";
RL J. Bacteriol. 186:4510-4519(2004).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ROLE IN O ANTIGEN BIOSYNTHESIS,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION,
RP PATHWAY, AND DISRUPTION PHENOTYPE.
RC STRAIN=O52 / G1066;
RX PubMed=19019146; DOI=10.1111/j.1365-2958.2008.06449.x;
RA Wang Q., Ding P., Perepelov A.V., Xu Y., Wang Y., Knirel Y.A., Wang L.,
RA Feng L.;
RT "Characterization of the dTDP-D-fucofuranose biosynthetic pathway in
RT Escherichia coli O52.";
RL Mol. Microbiol. 70:1358-1367(2008).
CC -!- FUNCTION: Catalyzes the stereospecific reduction of the C-4 keto group
CC of dTDP-4-dehydro-6-deoxy-D-glucose, leading to dTDP-D-fucopyranose.
CC This is a step in the biosynthesis of D-fucofuranose, a component of
CC E.coli O52 O antigen. Is more efficient using NADH than NADPH as
CC cosubstrate. {ECO:0000269|PubMed:19019146}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dTDP-alpha-D-fucose + NAD(+) = dTDP-4-dehydro-6-deoxy-alpha-D-
CC glucose + H(+) + NADH; Xref=Rhea:RHEA:36579, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57649, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:73933; EC=1.1.1.266;
CC Evidence={ECO:0000269|PubMed:19019146};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dTDP-alpha-D-fucose + NADP(+) = dTDP-4-dehydro-6-deoxy-alpha-
CC D-glucose + H(+) + NADPH; Xref=Rhea:RHEA:36583, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57649, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:73933; EC=1.1.1.266;
CC Evidence={ECO:0000269|PubMed:19019146};
CC -!- ACTIVITY REGULATION: Inhibited by Cu(2+), while other divalent cations
CC such as Ca(2+), Co(2+), Fe(2+), Mn(2+) and Mg(2+) have no obvious
CC effects on enzyme activity. {ECO:0000269|PubMed:19019146}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.38 mM for dTDP-4-dehydro-6-deoxy-alpha-D-glucose
CC {ECO:0000269|PubMed:19019146};
CC KM=0.84 mM for NADPH {ECO:0000269|PubMed:19019146};
CC KM=0.89 mM for NADH {ECO:0000269|PubMed:19019146};
CC Note=kcat is 406 min(-1) for the reduction reaction with NADPH, and
CC 1594 min(-1) for that with NADH.;
CC Temperature dependence:
CC Optimum temperature is 15-37 degrees Celsius. Active over a broad
CC range of temperatures, from 4 to 80 degrees Celsius.
CC {ECO:0000269|PubMed:19019146};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC biosynthesis. {ECO:0000269|PubMed:19019146}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene produce semirough (SR-
CC type) LPS with only one O unit attached to the core-lipid A moiety
CC while the wild-type strain produces normal LPS.
CC {ECO:0000269|PubMed:19019146}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. {ECO:0000305}.
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DR EMBL; AY528413; AAS99161.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6E7F2; -.
DR SMR; Q6E7F2; -.
DR KEGG; ag:AAS99161; -.
DR BioCyc; MetaCyc:MON-18130; -.
DR UniPathway; UPA00281; -.
DR GO; GO:0050573; F:dTDP-4-dehydro-6-deoxyglucose reductase activity; IDA:UniProtKB.
DR GO; GO:0048029; F:monosaccharide binding; IDA:UniProtKB.
DR GO; GO:0070404; F:NADH binding; IDA:UniProtKB.
DR GO; GO:0070402; F:NADPH binding; IDA:UniProtKB.
DR GO; GO:0042353; P:fucose biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009243; P:O antigen biosynthetic process; IMP:UniProtKB.
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 Carbohydrate metabolism; Lipopolysaccharide biosynthesis; NAD; NADP;
KW Oxidoreductase.
FT CHAIN 1..316
FT /note="dTDP-4-dehydro-6-deoxyglucose reductase"
FT /id="PRO_0000425107"
FT ACT_SITE 151
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 16..17
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 316 AA; 35595 MW; F09DAF44D25A5E32 CRC64;
MDARKNGVLI TGGAGFIGKA LITEMVERQI PLVSFDISDK PDSLPELSEY FNWYKFSYLE
SSQRIKELHE IVSRHNIKTV IHLATTMFPH ESKKNIDKDC LENVYANVCF FKNLYENGCE
KIIFASSGGT VYGKSDTPFS EDDALLPEIS YGLSKVMTET YLRFIAKELN GKSISLRISN
PYGEGQRIDG KQGVIPIFLN KISNDIPIDI IGSIESKRDY IYISDLVQAF MCSLEYEGHE
DIFNIGSGES ITLKKLIETI EFKLNKKAVI GFQDPIHTNA NGIILDIKRA MAELGWRPTV
VLDDGIDKLI KSIRCK
