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Protein

UDP-galactopyranose mutase

Gene

rfbD

Organism
Klebsiella pneumoniae
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

Cofactori

FAD5 PublicationsNote: Binds 1 FAD per subunit.5 Publications

Pathway: LPS O-antigen biosynthesis

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei14 – 141FAD4 Publications
Binding sitei41 – 411FAD; via amide nitrogen4 Publications
Binding sitei84 – 841UDP-GalP
Binding sitei151 – 1511UDP-GalP; via carbonyl oxygen
Binding sitei156 – 1561UDP-GalP
Binding sitei160 – 1601UDP-GalP
Binding sitei185 – 1851UDP-GalP
Binding sitei219 – 2191FAD; via amide nitrogen4 Publications
Binding sitei270 – 2701UDP-GalP
Binding sitei280 – 2801UDP-GalP
Binding sitei314 – 3141UDP-GalP
Binding sitei343 – 3431FAD4 Publications
Binding sitei349 – 3491UDP-GalP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi33 – 342FAD4 Publications
Nucleotide bindingi60 – 612FAD4 Publications
Nucleotide bindingi350 – 3556FAD4 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Lipopolysaccharide biosynthesis

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BRENDAi5.4.99.9. 2814.
UniPathwayiUPA00281.

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:rfbD
OrganismiKlebsiella pneumoniae
Taxonomic identifieri573 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeKlebsiella

Pathology & Biotechi

Disruption phenotypei

Abolishes lipopolysaccharide (LPS) biosynthesis.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 384361UDP-galactopyranose mutasePRO_0000087506Add
BLAST

Interactioni

Subunit structurei

Homodimer.5 Publications

Structurei

Secondary structure

1
384
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 95Combined sources
Helixi13 – 2311Combined sources
Turni24 – 263Combined sources
Beta strandi28 – 3912Combined sources
Helixi40 – 423Combined sources
Beta strandi44 – 463Combined sources
Turni48 – 503Combined sources
Beta strandi53 – 553Combined sources
Beta strandi62 – 654Combined sources
Helixi67 – 748Combined sources
Beta strandi79 – 813Combined sources
Beta strandi86 – 905Combined sources
Beta strandi93 – 986Combined sources
Helixi101 – 1077Combined sources
Helixi114 – 12411Combined sources
Helixi135 – 1439Combined sources
Helixi145 – 1517Combined sources
Helixi153 – 1608Combined sources
Helixi164 – 1663Combined sources
Helixi169 – 1713Combined sources
Beta strandi179 – 1813Combined sources
Beta strandi189 – 1946Combined sources
Helixi197 – 20610Combined sources
Beta strandi211 – 2166Combined sources
Helixi221 – 2266Combined sources
Beta strandi227 – 2326Combined sources
Helixi236 – 2394Combined sources
Turni240 – 2445Combined sources
Beta strandi249 – 26113Combined sources
Beta strandi263 – 2719Combined sources
Beta strandi276 – 2838Combined sources
Helixi284 – 2874Combined sources
Beta strandi294 – 30512Combined sources
Helixi319 – 33214Combined sources
Beta strandi336 – 3405Combined sources
Helixi342 – 3454Combined sources
Helixi352 – 37120Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WAMX-ray2.35A1-384[»]
2BI7X-ray2.00A1-384[»]
2BI8X-ray2.35A1-384[»]
3GF4X-ray2.45A/B1-384[»]
3INRX-ray2.30A/B1-383[»]
3INTX-ray2.51A/B1-384[»]
3KYBX-ray2.30A/B1-384[»]
ProteinModelPortaliQ48485.
SMRiQ48485. Positions 2-384.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ48485.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q48485-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKSKKILIVG AGFSGAVIGR QLAEKGHQVH IIDQRDHIGG NSYDARDSET
60 70 80 90 100
NVMVHVYGPH IFHTDNETVW NYVNKHAEMM PYVNRVKATV NGQVFSLPIN
110 120 130 140 150
LHTINQFFSK TCSPDEARAL IAEKGDSTIA DPQTFEEQAL RFIGKELYEA
160 170 180 190 200
FFKGYTIKQW GMQPSELPAS ILKRLPVRFN YDDNYFNHKF QGMPKCGYTQ
210 220 230 240 250
MIKSILNHEN IKVDLQREFI VEERTHYDHV FYSGPLDAFY GYQYGRLGYR
260 270 280 290 300
TLDFKKFTYQ GDYQGCAVMN YCSVDVPYTR ITEHKYFSPW EQHDGSVCYK
310 320 330 340 350
EYSRACEEND IPYYPIRQMG EMALLEKYLS LAENETNITF VGRLGTYRYL
360 370 380
DMDVTIAEAL KTAEVYLNSL TENQPMPVFT VSVR
Length:384
Mass (Da):44,457
Last modified:November 1, 1997 - v1
Checksum:iB74EC65EA5B751AB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L31762 Genomic DNA. Translation: AAC98417.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L31762 Genomic DNA. Translation: AAC98417.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WAMX-ray2.35A1-384[»]
2BI7X-ray2.00A1-384[»]
2BI8X-ray2.35A1-384[»]
3GF4X-ray2.45A/B1-384[»]
3INRX-ray2.30A/B1-383[»]
3INTX-ray2.51A/B1-384[»]
3KYBX-ray2.30A/B1-384[»]
ProteinModelPortaliQ48485.
SMRiQ48485. Positions 2-384.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00281.
BRENDAi5.4.99.9. 2814.

Miscellaneous databases

EvolutionaryTraceiQ48485.

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...

Publicationsi

  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. 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.

Entry informationi

Entry nameiGLF1_KLEPN
AccessioniPrimary (citable) accession number: Q48485
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: April 1, 2015
This is version 81 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.