B6I2A3 (ULAF_ECOSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
L-ribulose-5-phosphate 4-epimerase UlaF
EC=5.1.3.4

Alternative name(s):
L-ascorbate utilization protein F
Phosphoribulose isomerase

Gene names

Name:	ulaF
Ordered Locus Names:	ECSE_4496

Organism

Escherichia coli (strain SE11) [Complete proteome] [HAMAP]

Taxonomic identifier

409438 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	228 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript 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 By similarity. HAMAP MF_01952
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 By similarity. 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)
Molecular function	L-ribulose-phosphate 4-epimerase activity Inferred from electronic annotation. Source: EC metal 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_1000188848
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)
	B6I2A3 [UniParc]. Last modified December 16, 2008. Version 1. Checksum: 98FB4AAF2A30ACCC	FASTA	228	25,293
	10 20 30 40 50 60 MLKLKQQVFE ANMDLPRYGL VTFTWGNVSA IDRERGLVVI KPSGVAYETM KADDMVVVDM 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

[1]

"Complete genome sequence and comparative analysis of the wild-type commensal Escherichia coli strain SE11 isolated from a healthy adult." Oshima K., Toh H., Ogura Y., Sasamoto H., Morita H., Park S.-H., Ooka T., Iyoda S., Taylor T.D., Hayashi T., Itoh K., Hattori M. DNA Res. 15:375-386(2008) [PubMed: 18931093] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SE11.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP009240 Genomic DNA. Translation: BAG80020.1.
RefSeq	YP_002295771.1. NC_011415.1.
3D structure databases
ProteinModelPortal	B6I2A3.
SMR	B6I2A3. Positions 4-219.
ModBase	Search...
Protein-protein interaction databases
STRING	B6I2A3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000106587; EBESCP00000099002; EBESCG00000106266.
GeneID	7002881.
GenomeReviews	Gene locus ECSE_4496 in contig AP009240_GR.
KEGG	ecy:ECSE_4496.
PATRIC	18427720. VBIEscCol83070_4678.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000009319.
HOGENOM	HBG541069.
OMA	IDSYLMN.
ProtClustDB	PRK12348.
Enzyme and pathway databases
BioCyc	ECOL409438:ECSE_4496-MONOMER.
Family and domain databases
HAMAP	MF_01952. UlaF. [Tree]
InterPro	IPR001303. Aldolase_II/adducin_N. IPR023499. UlaF. [Graphical view]
Gene3D	G3DSA:3.40.225.10. Aldolase_II/adducin_N. 1 hit.
KO	K03077.
Pfam	PF00596. Aldolase_II. 1 hit. [Graphical view]
SMART	SM01007. Aldolase_II. 1 hit. [Graphical view]
SUPFAM	SSF53639. Aldolase_II_N. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ULAF_ECOSE

Accession

Primary (citable) accession number: B6I2A3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 28, 2009
Last sequence update:	December 16, 2008
Last modified:	January 25, 2012
This is version 25 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program