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P37747 (GLF_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
UDP-galactopyranose mutase

Short name=UGM
EC=5.4.99.9
Alternative name(s):
UDP-GALP mutase
Uridine 5-diphosphate galactopyranose mutase
Gene names
Name:glf
Synonyms:yefE
Ordered Locus Names:b2036, JW2021
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length367 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the interconversion through a 2-keto intermediate of uridine diphosphogalactopyranose (UDP-GalP) into uridine diphosphogalactofuranose (UDP-GalF) By similarity. Ref.6 Ref.7

Catalytic activity

UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose. Ref.6

Cofactor

Binds 1 FAD per subunit. Ref.6

Pathway

Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis.

Subunit structure

Homodimer. Ref.8

Sequence similarities

Belongs to the UDP-galactopyranose/dTDP-fucopyranose mutase family.

Biophysicochemical properties

Kinetic parameters:

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

KM=194 µM for UDP-GalF Ref.7

Mass spectrometry

Molecular mass is 42960±8 Da from positions 1 - 367. Determined by ESI. Ref.6

Ontologies

Keywords
   Biological processLipopolysaccharide biosynthesis
   LigandFAD
Flavoprotein
   Molecular functionIsomerase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processlipopolysaccharide biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionUDP-galactopyranose mutase activity

Inferred from direct assay Ref.6. Source: EcoCyc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 367367UDP-galactopyranose mutase
PRO_0000087508

Regions

Nucleotide binding31 – 322FAD
Nucleotide binding56 – 572FAD
Nucleotide binding212 – 2132FAD
Nucleotide binding347 – 3526FAD

Sites

Binding site121FAD; via amide nitrogen
Binding site121UDP-GalP; via amide nitrogen By similarity
Binding site391FAD; via amide nitrogen
Binding site801UDP-GalP By similarity
Binding site1521UDP-GalP By similarity
Binding site1561UDP-GalP By similarity
Binding site1811UDP-GalP By similarity
Binding site2681UDP-GalP By similarity
Binding site2781UDP-GalP By similarity
Binding site3111UDP-GalP By similarity
Binding site3401FAD By similarity
Binding site3461UDP-GalP By similarity

Experimental info

Mutagenesis1511Y → F: 3-fold decrease in the mutase activity. Ref.8
Mutagenesis1561W → A: Loss of mutase activity. Ref.8
Mutagenesis1561W → Y: 2-fold decrease in the mutase activity. Ref.8
Mutagenesis1811Y → F: Increase in the mutase activity. Ref.8
Mutagenesis3111Y → F: Loss of mutase activity. Ref.8
Mutagenesis3461Y → F: Loss of mutase activity. Ref.8

Secondary structure

................................................................... 367
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P37747 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: C62F67A4682B2A06

FASTA36742,966
        10         20         30         40         50         60 
MYDYIIVGSG LFGAVCANEL KKLNKKVLVI EKRNHIGGNA YTEDCEGIQI HKYGAHIFHT 

        70         80         90        100        110        120 
NDKYIWDYVN DLVEFNRFTN SPLAIYKDKL FNLPFNMNTF HQMWGVKDPQ EAQNIINAQK 

       130        140        150        160        170        180 
KKYGDKVPEN LEEQAISLVG EDLYQALIKG YTEKQWGRSA KELPAFIIKR IPVRFTFDNN 

       190        200        210        220        230        240 
YFSDRYQGIP VGGYTKLIEK MLEGVDVKLG IDFLKDKDSL ASKAHRIIYT GPIDQYFDYR 

       250        260        270        280        290        300 
FGALEYRSLK FETERHEFPN FQGNAVINFT DANVPYTRII EHKHFDYVET KHTVVTKEYP 

       310        320        330        340        350        360 
LEWKVGDEPY YPVNDNKNME LFKKYRELAS REDKVIFGGR LAEYKYYDMH QVISAALYQV 


KNIMSTD 

« Hide

References

« Hide 'large scale' references
[1]"Genetic analysis of the O-specific lipopolysaccharide biosynthesis region (rfb) of Escherichia coli K-12 W3110: identification of genes that confer group 6 specificity to Shigella flexneri serotypes Y and 4a."
Yao Z., Valvano M.A.
J. Bacteriol. 176:4133-4143(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]"Structure of the O antigen of Escherichia coli K-12 and the sequence of its rfb gene cluster."
Stevenson G., Neal B., Liu D., Hobbs M., Packer N.H., Batley M., Redmond J.W., Lindquist L., Reeves P.R.
J. Bacteriol. 176:4144-4156(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12 / WG1.
[3]"A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map."
Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S. expand/collapse author list , Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:379-392(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]"Galactofuranose biosynthesis in Escherichia coli K-12: identification and cloning of UDP-galactopyranose mutase."
Nassau P.M., Martin S.L., Brown R.E., Weston A., Monsey D., McNeil M.R., Duncan K.
J. Bacteriol. 178:1047-1052(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-15, FUNCTION, CATALYTIC ACTIVITY, MASS SPECTROMETRY, COFACTOR, NOMENCLATURE.
[7]"Mechanistic investigation of UDP-galactopyranose mutase from Escherichia coli using 2- and 3-fluorinated UDP-galactofuranose as probes."
Zhang Q., Liu H.
J. Am. Chem. Soc. 123:6756-6766(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[8]"UDP-galactopyranose mutase has a novel structure and mechanism."
Sanders D.A., Staines A.G., McMahon S.A., McNeil M.R., Whitfield C., Naismith J.H.
Nat. Struct. Biol. 8:858-863(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH FAD, MUTAGENESIS OF TYR-151; TRP-156; TYR-181; TYR-311 AND TYR-346, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U03041 Genomic DNA. Translation: AAC31632.1.
U09876 Genomic DNA. Translation: AAB88403.1.
U00096 Genomic DNA. Translation: AAC75097.1.
AP009048 Genomic DNA. Translation: BAA15878.1.
PIRI69653.
RefSeqNP_416540.1. NC_000913.3.
YP_490278.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1I8TX-ray2.40A/B1-367[»]
ProteinModelPortalP37747.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-6863N.
IntActP37747. 4 interactions.
MINTMINT-1308638.
STRING511145.b2036.

Chemistry

ChEMBLCHEMBL1075076.

Proteomic databases

PaxDbP37747.
PRIDEP37747.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75097; AAC75097; b2036.
BAA15878; BAA15878; BAA15878.
GeneID12931654.
945235.
KEGGecj:Y75_p1999.
eco:b2036.
PATRIC32119405. VBIEscCol129921_2112.

Organism-specific databases

EchoBASEEB1924.
EcoGeneEG11981. glf.

Phylogenomic databases

eggNOGCOG0562.
HOGENOMHOG000247596.
KOK01854.
OMAGKQWQTD.
OrthoDBEOG62K1X2.
PhylomeDBP37747.

Enzyme and pathway databases

BioCycEcoCyc:GALPMUT-MONOMER.
ECOL316407:JW2021-MONOMER.
MetaCyc:GALPMUT-MONOMER.
UniPathwayUPA00030.

Gene expression databases

GenevestigatorP37747.

Family and domain databases

Gene3D3.40.50.720. 3 hits.
InterProIPR016040. NAD(P)-bd_dom.
IPR004379. UDP-GALP_mutase.
IPR015899. UDP-GalPyranose_mutase_C.
[Graphical view]
PANTHERPTHR21197. PTHR21197. 1 hit.
PfamPF03275. GLF. 1 hit.
[Graphical view]
TIGRFAMsTIGR00031. UDP-GALP_mutase. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP37747.
PROP37747.

Entry information

Entry nameGLF_ECOLI
AccessionPrimary (citable) accession number: P37747
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: June 11, 2014
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene