FCF2_ECOLX
ID FCF2_ECOLX Reviewed; 377 AA.
AC Q6E7F1;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=dTDP-fucopyranose mutase;
DE EC=5.4.99.59;
DE AltName: Full=dTDP-alpha-D-fucopyranose mutase;
GN Name=fcf2;
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, ACTIVITY REGULATION, PATHWAY, AND DISRUPTION
RP 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 conversion of dTDP-alpha-D-fucopyranose to
CC dTDP-alpha-D-fucofuranose. This is a step in the biosynthesis of D-
CC fucofuranose, a component of E.coli O52 O antigen.
CC {ECO:0000269|PubMed:19019146}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dTDP-alpha-D-fucose = dTDP-alpha-D-fucofuranose;
CC Xref=Rhea:RHEA:36815, ChEBI:CHEBI:73933, ChEBI:CHEBI:76275;
CC EC=5.4.99.59; Evidence={ECO:0000269|PubMed:19019146};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by Cu(2+), while other divalent cations
CC such as Ca(2+), Co(2+), Fe(2+) and Mg(2+) have no obvious effects on
CC enzyme activity. {ECO:0000269|PubMed:19019146}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.43 mM for dTDP-alpha-D-fucopyranose
CC {ECO:0000269|PubMed:19019146};
CC Note=kcat is 3.3 min(-1).;
CC Temperature dependence:
CC Optimum temperature is 15-37 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 UDP-galactopyranose/dTDP-fucopyranose mutase
CC family. {ECO:0000305}.
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DR EMBL; AY528413; AAS99162.1; -; Genomic_DNA.
DR RefSeq; WP_001575910.1; NZ_UIHN01000014.1.
DR AlphaFoldDB; Q6E7F1; -.
DR SMR; Q6E7F1; -.
DR KEGG; ag:AAS99162; -.
DR BioCyc; MetaCyc:MON-18131; -.
DR BRENDA; 5.4.99.59; 2026.
DR UniPathway; UPA00281; -.
DR GO; GO:0016866; F:intramolecular transferase activity; IDA:UniProtKB.
DR GO; GO:0048029; F:monosaccharide binding; IDA:UniProtKB.
DR GO; GO:0008767; F:UDP-galactopyranose mutase activity; IEA:InterPro.
DR GO; GO:0042353; P:fucose biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009243; P:O antigen biosynthetic process; IMP:UniProtKB.
DR InterPro; IPR004379; UDP-GALP_mutase.
DR InterPro; IPR015899; UDP-GalPyranose_mutase_C.
DR Pfam; PF03275; GLF; 1.
DR TIGRFAMs; TIGR00031; UDP-GALP_mutase; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; FAD; Flavoprotein; Isomerase;
KW Lipopolysaccharide biosynthesis.
FT CHAIN 1..377
FT /note="dTDP-fucopyranose mutase"
FT /id="PRO_0000425109"
FT BINDING 12
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 31..32
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 39
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 58..59
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 348
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 355..360
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
SQ SEQUENCE 377 AA; 44195 MW; FF6530A33AEAF1A0 CRC64;
MNKVLIIGSG FSGATIARLL AEENIKVKII DDRKHIGGNC YDERDEKTGI NVHVYGPHIF
HTDNEDVWNF VNKYGTFQPY TTRLKANAKG QIYSLPVNLH TINQYYKTAL SPTEARKLIA
SKGDQTINDP QSFEEQALKF VGEDLYKTFF YGYPKKQWGM EPKEIPASVL KRLPVRFNYD
DNYFFHKFQG IPRDGYTPLF QNLLNHPNIE FELGKKVNRA TVEELITSEQ YGHVFFSGAI
DHFYDYEFGM LQYRTLDFEK FYSEDDDYQG CVVMSYCDED VPYTRVTEHK YFTPWEEHKG
SVLYKEFSRS CDKEDIPYYP VRLVSGNSIW NKYEQKAKEE TNITFIGRLA TYRYLDMDVC
IKEAIECAQL YIKNNKE
