Reviewed, UniProtKB/Swiss-Prot P39306 (ULAF_ECOLI)

Names and origin

Protein names

Recommended name:
    L-ribulose-5-phosphate 4-epimerase ulaF
    EC=5.1.3.4
Alternative name(s):
    Phosphoribulose isomerase
    L-ascorbate utilization protein F

Gene names

Name:	ulaF
Synonyms:	sgaE, yjfX
Ordered Locus Names:	b4198, JW4156

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	228 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the isomerization of L-ribulose 5-phosphate to D-xylulose 5-phosphate. Is involved in the anaerobic L-ascorbate utilization. Ref.5
Catalytic activity	L-ribulose 5-phosphate = D-xylulose 5-phosphate. HAMAP MF_01952
Cofactor	Binds 1 zinc ion per subunit Potential.
Pathway	Cofactor degradation; L-ascorbate degradation; D-xylulose 5-phosphate from L-ascorbate: step 4/4. HAMAP MF_01952
Induction	Induced by L-ascorbate. Repressed by ulaR. HAMAP MF_01952
Sequence similarities	Belongs to the aldolase class II family. AraD/fucA subfamily.

Ontologies

Keywords
Ligand	Metal-binding Zinc
Molecular function	Isomerase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	L-ascorbic acid metabolic process Inferred from electronic annotation. Source: HAMAP
Molecular function	L-ribulose-phosphate 4-epimerase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 228	228	L-ribulose-5-phosphate 4-epimerase ulaF HAMAP MF_01952		PRO_0000162921
Sites
	Metal binding	74	1	Zinc By similarity
	Metal binding	93	1	Zinc By similarity
	Metal binding	95	1	Zinc By similarity
	Metal binding	167	1	Zinc By similarity

Sequences

	Sequence		Length	Mass (Da)
	P39306-1 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 3E96E7E0261E36B6	FASTA	228	25,278
	10 20 30 40 50 60 MQKLKQQVFE ANMELPRYGL VTFTWGNVSA IDRERGLVVI KPSGVAYETM KAADMVVVDM 70 80 90 100 110 120 SGKVVEGEYR PSSDTATHLE LYRRYPSLGG IVHTHSTHAT AWAQAGLAIP ALGTTHADYF 130 140 150 160 170 180 FGDIPCTRGL SEEEVQGEYE LNTGKVIIET LGNAEPLHTP GIVVYQHGPF AWGKDAHDAV 190 200 210 220 HNAVVMEEVA KMAWIARGIN PQLNHIDSFL MNKHFMRKHG PNAYYGQK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes." Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R. Nucleic Acids Res. 23:2105-2119(1995) [PubMed: 7610040] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[2]	"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: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"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: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"Novel phosphotransferases system genes revealed by bacterial genome analysis: operons encoding homologues of sugar-specific permease domains of the phosphotransferase system and pentose catabolic enzymes." Reizer J., Charbit A., Reizer A., Saier M.H. Jr. Genome Sci. Technol. 1:53-75(1996) Cited for: DISCUSSION OF SEQUENCE.
[5]	"Utilization of L-ascorbate by Escherichia coli K-12: assignments of functions to products of the yjf-sga and yia-sgb operons." Yew W.S., Gerlt J.A. J. Bacteriol. 184:302-306(2002) [PubMed: 11741871] [Abstract] Cited for: FUNCTION, CHARACTERIZATION. Strain: K12 / MG1655 / ATCC 47076.
[6]	"The gene yjfQ encodes the repressor of the yjfR-X regulon (ula), which is involved in L-ascorbate metabolism in Escherichia coli." Campos E., Aguilar J., Baldoma L., Badia J. J. Bacteriol. 184:6065-6068(2002) [PubMed: 12374842] [Abstract] Cited for: TRANSCRIPTIONAL REGULATION.
[7]	"Regulation of expression of the divergent ulaG and ulaABCDEF operons involved in L-ascorbate dissimilation in Escherichia coli." Campos E., Baldoma L., Aguilar J., Badia J. J. Bacteriol. 186:1720-1728(2004) [PubMed: 14996803] [Abstract] Cited for: TRANSCRIPTIONAL REGULATION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U14003 Genomic DNA. Translation: AAA97094.1. U00096 Genomic DNA. Translation: AAC77155.1. AP009048 Genomic DNA. Translation: BAE78199.1.
PIR	S56423.
RefSeq	AP_004698.1. NP_418619.1.
3D structure databases
HSSP	HSSP built from PDB template 1K0W based on UniProtKB P08203.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:10868N.
STRING	P39306.
Genome annotation databases
GeneID	948711.
GenomeReviews	Gene locus JW4156 in contig AP009048_GR. Gene locus b4198 in contig U00096_GR.
KEGG	ecj:JW4156. eco:b4198.
Organism-specific databases
EchoBASE	EB2391.
EcoGene	EG12498. ulaF.
CMR	Search...
Phylogenomic databases
HOGENOM	P39306.
OMA	DAEPLHT.
Enzyme and pathway databases
BioCyc	EcoCyc:G7860-MON. MetaCyc:G7860-MON.
Gene expression databases
Genevestigator	P39306.
Family and domain databases
HAMAP	MF_01952. [Tree]
InterPro	IPR001303. Aldolase_II/adducin_N. [Graphical view]
Gene3D	G3DSA:3.40.225.10. Aldolase_II/adducin_N. 1 hit.
Pfam	PF00596. Aldolase_II. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ULAF_ECOLI

Accession

Primary (citable) accession number: P39306
Secondary accession number(s): Q2M6A7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	November 3, 2009
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)