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   24-JAN-2024, entry version 179.
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; Pseudomonadota; 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; 511145-b2036; -.
DR   EnsemblBacteria; AAC75097; AAC75097; b2036.
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   OrthoDB; 9815989at2; -.
DR   PhylomeDB; P37747; -.
DR   BioCyc; EcoCyc:GALPMUT-MONOMER; -.
DR   BioCyc; MetaCyc:GALPMUT-MONOMER; -.
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:0042803; F:protein homodimerization activity; 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   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 3.
DR   InterPro; IPR004379; UDP-GALP_mutase.
DR   InterPro; IPR015899; UDP-GalPyranose_mutase_C.
DR   NCBIfam; TIGR00031; UDP-GALP_mutase; 1.
DR   PANTHER; PTHR21197; UDP-GALACTOPYRANOSE MUTASE; 1.
DR   PANTHER; PTHR21197:SF0; UDP-GALACTOPYRANOSE MUTASE; 1.
DR   Pfam; PF03275; GLF; 1.
DR   Pfam; PF13450; NAD_binding_8; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51971; Nucleotide-binding domain; 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
//