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Protein

UDP-galactopyranose mutase

Gene

glf

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the interconversion through a 2-keto intermediate of uridine diphosphogalactopyranose (UDP-GalP) into uridine diphosphogalactofuranose (UDP-GalF).By similarity2 Publications

Catalytic activityi

UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose.1 Publication

Cofactori

FAD1 PublicationNote: Binds 1 FAD per subunit.1 Publication

Kineticsi

Kcat is 1.5 (sec-1) for UDP-GalF.

  1. KM=194 µM for UDP-GalF1 Publication

    Pathwayi: lipopolysaccharide biosynthesis

    This protein is involved in the pathway lipopolysaccharide biosynthesis, which is part of Bacterial outer membrane biogenesis.
    View all proteins of this organism that are known to be involved in the pathway lipopolysaccharide biosynthesis and in Bacterial outer membrane biogenesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei12FAD; via amide nitrogen1 Publication1
    Binding sitei12UDP-GalP; via amide nitrogenBy similarity1
    Binding sitei39FAD; via amide nitrogen1 Publication1
    Binding sitei80UDP-GalPBy similarity1
    Binding sitei152UDP-GalPBy similarity1
    Binding sitei156UDP-GalPBy similarity1
    Binding sitei181UDP-GalPBy similarity1
    Binding sitei268UDP-GalPBy similarity1
    Binding sitei278UDP-GalPBy similarity1
    Binding sitei311UDP-GalPBy similarity1
    Binding sitei340FADBy similarity1
    Binding sitei346UDP-GalPBy similarity1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi31 – 32FAD1 Publication2
    Nucleotide bindingi56 – 57FAD1 Publication2
    Nucleotide bindingi212 – 213FAD1 Publication2
    Nucleotide bindingi347 – 352FAD1 Publication6

    GO - Molecular functioni

    • flavin adenine dinucleotide binding Source: EcoCyc
    • UDP-galactopyranose mutase activity Source: EcoCyc

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    Lipopolysaccharide biosynthesis

    Keywords - Ligandi

    FAD, Flavoprotein

    Enzyme and pathway databases

    BioCyciEcoCyc:GALPMUT-MONOMER.
    ECOL316407:JW2021-MONOMER.
    MetaCyc:GALPMUT-MONOMER.
    BRENDAi5.4.99.9. 2026.
    UniPathwayiUPA00030.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    UDP-galactopyranose mutase (EC:5.4.99.9)
    Short name:
    UGM
    Alternative name(s):
    UDP-GALP mutase
    Uridine 5-diphosphate galactopyranose mutase
    Gene namesi
    Name:glf
    Synonyms:yefE
    Ordered Locus Names:b2036, JW2021
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG11981. glf.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: EcoCyc
    Complete GO annotation...

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi151Y → F: 3-fold decrease in the mutase activity. 1 Publication1
    Mutagenesisi156W → A: Loss of mutase activity. 1 Publication1
    Mutagenesisi156W → Y: 2-fold decrease in the mutase activity. 1 Publication1
    Mutagenesisi181Y → F: Increase in the mutase activity. 1 Publication1
    Mutagenesisi311Y → F: Loss of mutase activity. 1 Publication1
    Mutagenesisi346Y → F: Loss of mutase activity. 1 Publication1

    Chemistry databases

    ChEMBLiCHEMBL1075076.
    DrugBankiDB03147. Flavin adenine dinucleotide.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000875081 – 367UDP-galactopyranose mutaseAdd BLAST367

    Proteomic databases

    PaxDbiP37747.
    PRIDEiP37747.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi4260648. 99 interactors.
    DIPiDIP-6863N.
    IntActiP37747. 4 interactors.
    MINTiMINT-1308638.
    STRINGi511145.b2036.

    Structurei

    Secondary structure

    1367
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi2 – 7Combined sources6
    Helixi11 – 20Combined sources10
    Helixi21 – 23Combined sources3
    Beta strandi27 – 30Combined sources4
    Beta strandi32 – 37Combined sources6
    Helixi38 – 40Combined sources3
    Beta strandi42 – 45Combined sources4
    Beta strandi48 – 51Combined sources4
    Beta strandi58 – 61Combined sources4
    Helixi63 – 70Combined sources8
    Beta strandi83 – 86Combined sources4
    Beta strandi89 – 96Combined sources8
    Helixi97 – 104Combined sources8
    Helixi109 – 119Combined sources11
    Turni120 – 123Combined sources4
    Helixi131 – 147Combined sources17
    Helixi149 – 156Combined sources8
    Helixi160 – 162Combined sources3
    Beta strandi175 – 177Combined sources3
    Beta strandi185 – 188Combined sources4
    Helixi194 – 202Combined sources9
    Beta strandi205 – 208Combined sources4
    Helixi213 – 215Combined sources3
    Helixi217 – 221Combined sources5
    Beta strandi224 – 229Combined sources6
    Helixi233 – 236Combined sources4
    Turni237 – 241Combined sources5
    Beta strandi246 – 259Combined sources14
    Beta strandi261 – 269Combined sources9
    Beta strandi277 – 281Combined sources5
    Helixi282 – 285Combined sources4
    Beta strandi293 – 302Combined sources10
    Helixi316 – 331Combined sources16
    Beta strandi335 – 337Combined sources3
    Turni340 – 344Combined sources5
    Helixi349 – 364Combined sources16

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1I8TX-ray2.40A/B1-367[»]
    ProteinModelPortaliP37747.
    SMRiP37747.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP37747.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105D5D. Bacteria.
    COG0562. LUCA.
    HOGENOMiHOG000247596.
    InParanoidiP37747.
    KOiK01854.
    OMAiGKQWQTD.
    PhylomeDBiP37747.

    Family and domain databases

    Gene3Di3.40.50.720. 3 hits.
    InterProiIPR016040. NAD(P)-bd_dom.
    IPR004379. UDP-GALP_mutase.
    IPR015899. UDP-GalPyranose_mutase_C.
    [Graphical view]
    PANTHERiPTHR21197. PTHR21197. 1 hit.
    PfamiPF03275. GLF. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR00031. UDP-GALP_mutase. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P37747-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MYDYIIVGSG LFGAVCANEL KKLNKKVLVI EKRNHIGGNA YTEDCEGIQI
    60 70 80 90 100
    HKYGAHIFHT NDKYIWDYVN DLVEFNRFTN SPLAIYKDKL FNLPFNMNTF
    110 120 130 140 150
    HQMWGVKDPQ EAQNIINAQK KKYGDKVPEN LEEQAISLVG EDLYQALIKG
    160 170 180 190 200
    YTEKQWGRSA KELPAFIIKR IPVRFTFDNN YFSDRYQGIP VGGYTKLIEK
    210 220 230 240 250
    MLEGVDVKLG IDFLKDKDSL ASKAHRIIYT GPIDQYFDYR FGALEYRSLK
    260 270 280 290 300
    FETERHEFPN FQGNAVINFT DANVPYTRII EHKHFDYVET KHTVVTKEYP
    310 320 330 340 350
    LEWKVGDEPY YPVNDNKNME LFKKYRELAS REDKVIFGGR LAEYKYYDMH
    360
    QVISAALYQV KNIMSTD
    Length:367
    Mass (Da):42,966
    Last modified:October 1, 1994 - v1
    Checksum:iC62F67A4682B2A06
    GO

    Mass spectrometryi

    Molecular mass is 42960±8 Da from positions 1 - 367. Determined by ESI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U03041 Genomic DNA. Translation: AAC31632.1.
    U09876 Genomic DNA. Translation: AAB88403.1.
    U00096 Genomic DNA. Translation: AAC75097.1.
    AP009048 Genomic DNA. Translation: BAA15878.1.
    PIRiI69653.
    RefSeqiNP_416540.1. NC_000913.3.
    WP_000272486.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75097; AAC75097; b2036.
    BAA15878; BAA15878; BAA15878.
    GeneIDi945235.
    KEGGiecj:JW2021.
    eco:b2036.
    PATRICi32119405. VBIEscCol129921_2112.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U03041 Genomic DNA. Translation: AAC31632.1.
    U09876 Genomic DNA. Translation: AAB88403.1.
    U00096 Genomic DNA. Translation: AAC75097.1.
    AP009048 Genomic DNA. Translation: BAA15878.1.
    PIRiI69653.
    RefSeqiNP_416540.1. NC_000913.3.
    WP_000272486.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1I8TX-ray2.40A/B1-367[»]
    ProteinModelPortaliP37747.
    SMRiP37747.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4260648. 99 interactors.
    DIPiDIP-6863N.
    IntActiP37747. 4 interactors.
    MINTiMINT-1308638.
    STRINGi511145.b2036.

    Chemistry databases

    ChEMBLiCHEMBL1075076.
    DrugBankiDB03147. Flavin adenine dinucleotide.

    Proteomic databases

    PaxDbiP37747.
    PRIDEiP37747.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC75097; AAC75097; b2036.
    BAA15878; BAA15878; BAA15878.
    GeneIDi945235.
    KEGGiecj:JW2021.
    eco:b2036.
    PATRICi32119405. VBIEscCol129921_2112.

    Organism-specific databases

    EchoBASEiEB1924.
    EcoGeneiEG11981. glf.

    Phylogenomic databases

    eggNOGiENOG4105D5D. Bacteria.
    COG0562. LUCA.
    HOGENOMiHOG000247596.
    InParanoidiP37747.
    KOiK01854.
    OMAiGKQWQTD.
    PhylomeDBiP37747.

    Enzyme and pathway databases

    UniPathwayiUPA00030.
    BioCyciEcoCyc:GALPMUT-MONOMER.
    ECOL316407:JW2021-MONOMER.
    MetaCyc:GALPMUT-MONOMER.
    BRENDAi5.4.99.9. 2026.

    Miscellaneous databases

    EvolutionaryTraceiP37747.
    PROiP37747.

    Family and domain databases

    Gene3Di3.40.50.720. 3 hits.
    InterProiIPR016040. NAD(P)-bd_dom.
    IPR004379. UDP-GALP_mutase.
    IPR015899. UDP-GalPyranose_mutase_C.
    [Graphical view]
    PANTHERiPTHR21197. PTHR21197. 1 hit.
    PfamiPF03275. GLF. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR00031. UDP-GALP_mutase. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiGLF_ECOLI
    AccessioniPrimary (citable) accession number: P37747
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: October 1, 1994
    Last modified: November 2, 2016
    This is version 144 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.