GLF_ECOLI
ID GLF_ECOLI Reviewed; 367 AA.
AC P37747;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=UDP-galactopyranose mutase;
DE Short=UGM;
DE EC=5.4.99.9;
DE AltName: Full=UDP-GALP mutase;
DE AltName: Full=Uridine 5-diphosphate galactopyranose mutase;
GN Name=glf; Synonyms=yefE; OrderedLocusNames=b2036, JW2021;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=7517390; DOI=10.1128/jb.176.13.4133-4143.1994;
RA Yao Z., Valvano M.A.;
RT "Genetic analysis of the O-specific lipopolysaccharide biosynthesis region
RT (rfb) of Escherichia coli K-12 W3110: identification of genes that confer
RT group 6 specificity to Shigella flexneri serotypes Y and 4a.";
RL J. Bacteriol. 176:4133-4143(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / WG1;
RX PubMed=7517391; DOI=10.1128/jb.176.13.4144-4156.1994;
RA Stevenson G., Neal B., Liu D., Hobbs M., Packer N.H., Batley M.,
RA Redmond J.W., Lindquist L., Reeves P.R.;
RT "Structure of the O antigen of Escherichia coli K-12 and the sequence of
RT its rfb gene cluster.";
RL J. Bacteriol. 176:4144-4156(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP PROTEIN SEQUENCE OF 1-15, FUNCTION, CATALYTIC ACTIVITY, MASS SPECTROMETRY,
RP COFACTOR, AND NOMENCLATURE.
RX PubMed=8576037; DOI=10.1128/jb.178.4.1047-1052.1996;
RA Nassau P.M., Martin S.L., Brown R.E., Weston A., Monsey D., McNeil M.R.,
RA Duncan K.;
RT "Galactofuranose biosynthesis in Escherichia coli K-12: identification and
RT cloning of UDP-galactopyranose mutase.";
RL J. Bacteriol. 178:1047-1052(1996).
RN [7]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=11448178; DOI=10.1021/ja010473l;
RA Zhang Q., Liu H.;
RT "Mechanistic investigation of UDP-galactopyranose mutase from Escherichia
RT coli using 2- and 3-fluorinated UDP-galactofuranose as probes.";
RL J. Am. Chem. Soc. 123:6756-6766(2001).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH FAD, MUTAGENESIS OF
RP TYR-151; TRP-156; TYR-181; TYR-311 AND TYR-346, AND SUBUNIT.
RX PubMed=11573090; DOI=10.1038/nsb1001-858;
RA Sanders D.A., Staines A.G., McMahon S.A., McNeil M.R., Whitfield C.,
RA Naismith J.H.;
RT "UDP-galactopyranose mutase has a novel structure and mechanism.";
RL Nat. Struct. Biol. 8:858-863(2001).
CC -!- FUNCTION: Catalyzes the interconversion through a 2-keto intermediate
CC of uridine diphosphogalactopyranose (UDP-GalP) into uridine
CC diphosphogalactofuranose (UDP-GalF). {ECO:0000250,
CC ECO:0000269|PubMed:11448178, ECO:0000269|PubMed:8576037}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=UDP-alpha-D-galactose = UDP-alpha-D-galactofuranose;
CC Xref=Rhea:RHEA:24132, ChEBI:CHEBI:66914, ChEBI:CHEBI:66915;
CC EC=5.4.99.9; Evidence={ECO:0000269|PubMed:8576037};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:8576037};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:8576037};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=194 uM for UDP-GalF {ECO:0000269|PubMed:11448178};
CC Note=kcat is 1.5 sec(-1) for UDP-GalF.;
CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11573090}.
CC -!- INTERACTION:
CC P37747; P11868: tdcD; NbExp=2; IntAct=EBI-558730, EBI-553884;
CC -!- MASS SPECTROMETRY: Mass=42960; Mass_error=8; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:8576037};
CC -!- SIMILARITY: Belongs to the UDP-galactopyranose/dTDP-fucopyranose mutase
CC family. {ECO:0000305}.
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DR EMBL; U03041; AAC31632.1; -; Genomic_DNA.
DR EMBL; U09876; AAB88403.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75097.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15878.1; -; Genomic_DNA.
DR PIR; I69653; I69653.
DR RefSeq; NP_416540.1; NC_000913.3.
DR RefSeq; WP_000272486.1; NZ_LN832404.1.
DR PDB; 1I8T; X-ray; 2.40 A; A/B=1-367.
DR PDBsum; 1I8T; -.
DR AlphaFoldDB; P37747; -.
DR SMR; P37747; -.
DR BioGRID; 4260648; 105.
DR DIP; DIP-6863N; -.
DR IntAct; P37747; 4.
DR STRING; 511145.b2036; -.
DR ChEMBL; CHEMBL1075076; -.
DR DrugBank; DB03147; Flavin adenine dinucleotide.
DR jPOST; P37747; -.
DR PaxDb; P37747; -.
DR PRIDE; P37747; -.
DR EnsemblBacteria; AAC75097; AAC75097; b2036.
DR EnsemblBacteria; BAA15878; BAA15878; BAA15878.
DR GeneID; 945235; -.
DR KEGG; ecj:JW2021; -.
DR KEGG; eco:b2036; -.
DR PATRIC; fig|1411691.4.peg.215; -.
DR EchoBASE; EB1924; -.
DR eggNOG; COG0562; Bacteria.
DR HOGENOM; CLU_042118_0_0_6; -.
DR InParanoid; P37747; -.
DR OMA; INVHKYG; -.
DR PhylomeDB; P37747; -.
DR BioCyc; EcoCyc:GALPMUT-MON; -.
DR BioCyc; MetaCyc:GALPMUT-MON; -.
DR BRENDA; 5.4.99.9; 2026.
DR UniPathway; UPA00030; -.
DR EvolutionaryTrace; P37747; -.
DR PRO; PR:P37747; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:EcoCyc.
DR GO; GO:0008767; F:UDP-galactopyranose mutase activity; IDA:EcoCyc.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
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 3D-structure; Direct protein sequencing; FAD; Flavoprotein; Isomerase;
KW Lipopolysaccharide biosynthesis; Reference proteome.
FT CHAIN 1..367
FT /note="UDP-galactopyranose mutase"
FT /id="PRO_0000087508"
FT BINDING 12
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:11573090"
FT BINDING 12
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 31..32
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:11573090"
FT BINDING 39
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:11573090"
FT BINDING 56..57
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:11573090"
FT BINDING 80
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 212..213
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:11573090"
FT BINDING 268
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 278
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 311
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 340
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 346
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 347..352
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:11573090"
FT MUTAGEN 151
FT /note="Y->F: 3-fold decrease in the mutase activity."
FT /evidence="ECO:0000269|PubMed:11573090"
FT MUTAGEN 156
FT /note="W->A: Loss of mutase activity."
FT /evidence="ECO:0000269|PubMed:11573090"
FT MUTAGEN 156
FT /note="W->Y: 2-fold decrease in the mutase activity."
FT /evidence="ECO:0000269|PubMed:11573090"
FT MUTAGEN 181
FT /note="Y->F: Increase in the mutase activity."
FT /evidence="ECO:0000269|PubMed:11573090"
FT MUTAGEN 311
FT /note="Y->F: Loss of mutase activity."
FT /evidence="ECO:0000269|PubMed:11573090"
FT MUTAGEN 346
FT /note="Y->F: Loss of mutase activity."
FT /evidence="ECO:0000269|PubMed:11573090"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:1I8T"
FT HELIX 11..20
FT /evidence="ECO:0007829|PDB:1I8T"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:1I8T"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:1I8T"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:1I8T"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:1I8T"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:1I8T"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:1I8T"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:1I8T"
FT HELIX 63..70
FT /evidence="ECO:0007829|PDB:1I8T"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:1I8T"
FT STRAND 89..96
FT /evidence="ECO:0007829|PDB:1I8T"
FT HELIX 97..104
FT /evidence="ECO:0007829|PDB:1I8T"
FT HELIX 109..119
FT /evidence="ECO:0007829|PDB:1I8T"
FT TURN 120..123
FT /evidence="ECO:0007829|PDB:1I8T"
FT HELIX 131..147
FT /evidence="ECO:0007829|PDB:1I8T"
FT HELIX 149..156
FT /evidence="ECO:0007829|PDB:1I8T"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:1I8T"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:1I8T"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:1I8T"
FT HELIX 194..202
FT /evidence="ECO:0007829|PDB:1I8T"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:1I8T"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:1I8T"
FT HELIX 217..221
FT /evidence="ECO:0007829|PDB:1I8T"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:1I8T"
FT HELIX 233..236
FT /evidence="ECO:0007829|PDB:1I8T"
FT TURN 237..241
FT /evidence="ECO:0007829|PDB:1I8T"
FT STRAND 246..259
FT /evidence="ECO:0007829|PDB:1I8T"
FT STRAND 261..269
FT /evidence="ECO:0007829|PDB:1I8T"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:1I8T"
FT HELIX 282..285
FT /evidence="ECO:0007829|PDB:1I8T"
FT STRAND 293..302
FT /evidence="ECO:0007829|PDB:1I8T"
FT HELIX 316..331
FT /evidence="ECO:0007829|PDB:1I8T"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:1I8T"
FT TURN 340..344
FT /evidence="ECO:0007829|PDB:1I8T"
FT HELIX 349..364
FT /evidence="ECO:0007829|PDB:1I8T"
SQ SEQUENCE 367 AA; 42966 MW; C62F67A4682B2A06 CRC64;
MYDYIIVGSG LFGAVCANEL KKLNKKVLVI EKRNHIGGNA YTEDCEGIQI HKYGAHIFHT
NDKYIWDYVN DLVEFNRFTN SPLAIYKDKL FNLPFNMNTF HQMWGVKDPQ EAQNIINAQK
KKYGDKVPEN LEEQAISLVG EDLYQALIKG YTEKQWGRSA KELPAFIIKR IPVRFTFDNN
YFSDRYQGIP VGGYTKLIEK MLEGVDVKLG IDFLKDKDSL ASKAHRIIYT GPIDQYFDYR
FGALEYRSLK FETERHEFPN FQGNAVINFT DANVPYTRII EHKHFDYVET KHTVVTKEYP
LEWKVGDEPY YPVNDNKNME LFKKYRELAS REDKVIFGGR LAEYKYYDMH QVISAALYQV
KNIMSTD
