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Q48485 (GLF1_KLEPN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 22, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:rfbD
OrganismKlebsiella pneumoniae
Taxonomic identifier573 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeKlebsiella

Protein attributes

Sequence length384 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the biosynthesis of the galactose-containing O-side-chain polysaccharide backbone structure of D-galactan I which is a key component of lipopolysaccharide (LPS). Catalyzes the interconversion through a 2-keto intermediate of uridine diphosphogalactopyranose (UDP-GalP) into uridine diphosphogalactofuranose (UDP-GalF) which is the biosynthetic precursor of galactofuranosyl residues. Ref.2

Catalytic activity

UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose. Ref.2

Cofactor

Binds 1 FAD per subunit. Ref.2 Ref.4 Ref.5 Ref.6 Ref.7

Pathway

Bacterial outer membrane biogenesis; LPS O-antigen biosynthesis.

Subunit structure

Homodimer. Ref.2 Ref.4 Ref.5 Ref.7

Disruption phenotype

Abolishes lipopolysaccharide (LPS) biosynthesis. Ref.2

Sequence similarities

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

Ontologies

Keywords
   Biological processLipopolysaccharide biosynthesis
   DomainSignal
   LigandFAD
Flavoprotein
   Molecular functionIsomerase
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processO antigen biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionUDP-galactopyranose mutase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 384361UDP-galactopyranose mutase
PRO_0000087506

Regions

Nucleotide binding33 – 342FAD
Nucleotide binding60 – 612FAD
Nucleotide binding350 – 3556FAD

Sites

Binding site141FAD
Binding site411FAD; via amide nitrogen
Binding site841UDP-GalP
Binding site1511UDP-GalP; via carbonyl oxygen
Binding site1561UDP-GalP
Binding site1601UDP-GalP
Binding site1851UDP-GalP
Binding site2191FAD; via amide nitrogen
Binding site2701UDP-GalP
Binding site2801UDP-GalP
Binding site3141UDP-GalP
Binding site3431FAD
Binding site3491UDP-GalP

Secondary structure

...................................................................... 384
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q48485 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: B74EC65EA5B751AB

FASTA38444,457
        10         20         30         40         50         60 
MKSKKILIVG AGFSGAVIGR QLAEKGHQVH IIDQRDHIGG NSYDARDSET NVMVHVYGPH 

        70         80         90        100        110        120 
IFHTDNETVW NYVNKHAEMM PYVNRVKATV NGQVFSLPIN LHTINQFFSK TCSPDEARAL 

       130        140        150        160        170        180 
IAEKGDSTIA DPQTFEEQAL RFIGKELYEA FFKGYTIKQW GMQPSELPAS ILKRLPVRFN 

       190        200        210        220        230        240 
YDDNYFNHKF QGMPKCGYTQ MIKSILNHEN IKVDLQREFI VEERTHYDHV FYSGPLDAFY 

       250        260        270        280        290        300 
GYQYGRLGYR TLDFKKFTYQ GDYQGCAVMN YCSVDVPYTR ITEHKYFSPW EQHDGSVCYK 

       310        320        330        340        350        360 
EYSRACEEND IPYYPIRQMG EMALLEKYLS LAENETNITF VGRLGTYRYL DMDVTIAEAL 

       370        380 
KTAEVYLNSL TENQPMPVFT VSVR 

« Hide

References

[1]"Role of Rfe and RfbF in the initiation of biosynthesis of D-galactan I, the lipopolysaccharide O antigen from Klebsiella pneumoniae serotype O1."
Clarke B.R., Bronner D., Keenleyside W.J., Severn W.B., Richards J.C., Whitfield C.
J. Bacteriol. 177:5411-5418(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K20 / Serotype O1.
[2]"UDP-galactofuranose precursor required for formation of the lipopolysaccharide O antigen of Klebsiella pneumoniae serotype O1 is synthesized by the product of the rfbDKPO1 gene."
Koplin R., Brisson J.R., Whitfield C.
J. Biol. Chem. 272:4121-4128(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, COFACTOR, SUBUNIT.
Strain: K20 / Serotype O1.
[3]"A unique catalytic mechanism for UDP-galactopyranose mutase."
Soltero-Higgin M., Carlson E.E., Gruber T.D., Kiessling L.L.
Nat. Struct. Mol. Biol. 11:539-543(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: REACTION MECHANISM.
Strain: K20 / Serotype O1.
[4]"Crystal structures of Mycobacteria tuberculosis and Klebsiella pneumoniae UDP-galactopyranose mutase in the oxidised state and Klebsiella pneumoniae UDP-galactopyranose mutase in the (active) reduced state."
Beis K., Srikannathasan V., Liu H., Fullerton S.W., Bamford V.A., Sanders D.A., Whitfield C., McNeil M.R., Naismith J.H.
J. Mol. Biol. 348:971-982(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH FAD, COFACTOR, SUBUNIT.
[5]"X-ray crystallography reveals a reduced substrate complex of UDP-galactopyranose mutase poised for covalent catalysis by flavin."
Gruber T.D., Westler W.M., Kiessling L.L., Forest K.T.
Biochemistry 48:9171-9173(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-383 IN COMPLEX WITH FAD AND SUBSTRATE, COFACTOR, SUBUNIT.
[6]"Ligand binding and substrate discrimination by UDP-galactopyranose mutase."
Gruber T.D., Borrok M.J., Westler W.M., Forest K.T., Kiessling L.L.
J. Mol. Biol. 391:327-340(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 1-383 IN COMPLEX WITH FAD AND SUBSTRATE, COFACTOR.
[7]"Structure of UDP-galactopyranose mutase bound to flavin mononucleotide."
Gruber T.D., Dimond M.C., Kiessling L.L., Forest K.T.
Submitted (DEC-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-383 IN COMPLEX WITH FAD, COFACTOR, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L31762 Genomic DNA. Translation: AAC98417.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WAMX-ray2.35A1-384[»]
2BI7X-ray2.00A1-384[»]
2BI8X-ray2.35A1-384[»]
3GF4X-ray2.45A/B1-383[»]
3INRX-ray2.30A/B1-383[»]
3INTX-ray2.51A/B1-383[»]
3KYBX-ray2.30A/B1-383[»]
ProteinModelPortalQ48485.
SMRQ48485. Positions 2-384.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00281.

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

EvolutionaryTraceQ48485.

Entry information

Entry nameGLF1_KLEPN
AccessionPrimary (citable) accession number: Q48485
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: January 22, 2014
This is version 77 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