P37747 (GLF_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	367 AA.
Sequence status	Complete.
Protein existence	Evidence 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
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 process	Lipopolysaccharide biosynthesis
Ligand	FAD Flavoprotein
Molecular function	Isomerase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	lipopolysaccharide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	UDP-galactopyranose mutase activity Inferred from direct assay Ref.6. Source: EcoCyc nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 367

367

UDP-galactopyranose mutase

PRO_0000087508

Regions

Nucleotide binding

31 – 32

2

FAD

Nucleotide binding

56 – 57

2

FAD

Nucleotide binding

212 – 213

2

FAD

Nucleotide binding

347 – 352

6

FAD

Sites

Binding site

12

1

FAD; via amide nitrogen

Binding site

12

1

UDP-GalP; via amide nitrogen By similarity

Binding site

39

1

FAD; via amide nitrogen

Binding site

80

1

UDP-GalP By similarity

Binding site

152

1

UDP-GalP By similarity

Binding site

156

1

UDP-GalP By similarity

Binding site

181

1

UDP-GalP By similarity

Binding site

268

1

UDP-GalP By similarity

Binding site

278

1

UDP-GalP By similarity

Binding site

311

1

UDP-GalP By similarity

Binding site

340

1

FAD By similarity

Binding site

346

1

UDP-GalP By similarity

Experimental info

Mutagenesis

151

1

Y → F: 3-fold decrease in the mutase activity. Ref.8

Mutagenesis

156

1

W → A: Loss of mutase activity. Ref.8

Mutagenesis

156

1

W → Y: 2-fold decrease in the mutase activity. Ref.8

Mutagenesis

181

1

Y → F: Increase in the mutase activity. Ref.8

Mutagenesis

311

1

Y → F: Loss of mutase activity. Ref.8

Mutagenesis

346

1

Y → F: Loss of mutase activity. Ref.8

Secondary structure

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367

Helix Strand Turn

Details...

Beta strand

2 – 7

6

Helix

11 – 20

10

Helix

21 – 23

3

Beta strand

27 – 30

4

Beta strand

32 – 37

6

Helix

38 – 40

3

Beta strand

42 – 45

4

Beta strand

48 – 51

4

Beta strand

58 – 61

4

Helix

63 – 70

8

Beta strand

83 – 86

4

Beta strand

89 – 96

8

Helix

97 – 104

8

Helix

109 – 119

11

Turn

120 – 123

4

Helix

131 – 147

17

Helix

149 – 156

8

Helix

160 – 162

3

Beta strand

175 – 177

3

Beta strand

185 – 188

4

Helix

194 – 202

9

Beta strand

205 – 208

4

Helix

213 – 215

3

Helix

217 – 221

5

Beta strand

224 – 229

6

Helix

233 – 236

4

Turn

237 – 241

5

Beta strand

246 – 259

14

Beta strand

261 – 269

9

Beta strand

277 – 281

5

Helix

282 – 285

4

Beta strand

293 – 302

10

Helix

316 – 331

16

Beta strand

335 – 337

3

Turn

340 – 344

5

Helix

349 – 364

16

Sequences

	Sequence		Length	Mass (Da)
	P37747 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: C62F67A4682B2A06	FASTA	367	42,966
	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

References

	« Hide 'large scale' referencesShow '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. , 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 277:1453-1474(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.

PIR

I69653.

RefSeq

NP_416540.1. NC_000913.2.
YP_490278.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1I8T	X-ray	2.40	A/B	1-367	[»]

ProteinModelPortal

P37747.

SMR

P37747. Positions 1-367.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6863N.

IntAct

P37747. 4 interactions.

MINT

MINT-1308638.

STRING

511145.b2036.

Proteomic databases

PaxDb

P37747.

PRIDE

P37747.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC75097; AAC75097; b2036.
BAA15878; BAA15878; BAA15878.

GeneID

12931654.
945235.

KEGG

ecj:Y75_p1999.
eco:b2036.

PATRIC

32119405. VBIEscCol129921_2112.

Organism-specific databases

EchoBASE

EB1924.

EcoGene

EG11981. glf.

Phylogenomic databases

eggNOG

COG0562.

HOGENOM

HOG000247596.

KO

K01854.

OMA

KYLDMHM.

ProtClustDB

CLSK879257.

Enzyme and pathway databases

BioCyc

EcoCyc:GALPMUT-MONOMER.
ECOL316407:JW2021-MONOMER.
MetaCyc:GALPMUT-MONOMER.

UniPathway

UPA00030.

Gene expression databases

Genevestigator

P37747.

Family and domain databases

Gene3D

3.40.50.720. 3 hits.

InterPro

IPR016040. NAD(P)-bd_dom.
IPR004379. UDP-GALP_mutase.
IPR015899. UDP-GalPyranose_mutase_C.
[Graphical view]

PANTHER

PTHR21197. PTHR21197. 1 hit.

Pfam

PF03275. GLF. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00031. UDP-GALP_mutase. 1 hit.

ProtoNet

Search...

Other

ChEMBL

CHEMBL1075076.

EvolutionaryTrace

P37747.

Entry information

Entry name

GLF_ECOLI

Accession

Primary (citable) accession number: P37747

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	May 1, 2013
This is version 120 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program