Reviewed, UniProtKB/Swiss-Prot Q0T9J5 (ULAF_ECOL5)

Names and originHide

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
Ordered Locus Names:	ECP_4443

Organism

Escherichia coli O6:K15:H31 (strain 536 / UPEC) [Complete proteome] [HAMAP]

Taxonomic identifier

362663 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributesHide

Sequence length	228 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level.

General annotation (Comments)Hide

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. HAMAP MF_01952
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.

OntologiesHide

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 metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)Hide

	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_1000070639
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

SequencesHide

	Sequence		Length	Mass (Da)
	Q0T9J5-1 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: C2C942553FF3B464	FASTA	228	25,306
	10 20 30 40 50 60 MQKLKQQVFE ANMDLPHYGL VTFTWGNVSA IDRERGLVVI KPSGVAYETM KADDMVVVDM 70 80 90 100 110 120 SGNVVEGEYR PSSDTATHLE LYRRYPSLGG IVHTHSTHAT AWAQAGLAIP ALGTTHADYF 130 140 150 160 170 180 FGDIPCTRGL SEEEVQGEYE LNTGKVIIET LGDAEPLHTP GIVVYQHGPF AWGKDAHDAV 190 200 210 220 HNAVVMEEVA KMAWIARSIN PQLNHIDSFL MNKHFMRKHG PNAYYGQK

ReferencesHide

[1]

"Role of pathogenicity island-associated integrases in the genome plasticity of uropathogenic Escherichia coli strain 536." Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U., Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J. Mol. Microbiol. 61:584-595(2006) [PubMed: 16879640] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-referencesHide

Sequence databases
EMBL GenBank DDBJ	CP000247 Genomic DNA. Translation: ABG72384.1.
RefSeq	YP_672285.1.
3D structure databases
SMR	Q0T9J5. Positions 1-219.
ModBase	Search...
Protein-protein interaction databases
STRING	Q0T9J5.
Genome annotation databases
EnsemblBacteria	EBESCT00000047014; EBESCP00000045203; EBESCG00000046064.
GeneID	4190035.
GenomeReviews	Gene locus ECP_4443 in contig CP000247_GR.
KEGG	ecp:ECP_4443.
NMPDR	fig|340197.3.peg.946.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0235.
HOGENOM	HBG541069.
OMA	AYVYRHM.
PhylomeDB	Q0T9J5.
ProtClustDB	PRK12348.
Enzyme and pathway databases
BioCyc	ECOL362663:ECP_4443-MONOMER.
Family and domain databases
HAMAP	MF_01952. UlaF. [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]
SUPFAM	SSF53639. Aldolase_II_N. 1 hit.
ProtoNet	Search...

Entry informationHide

Entry name

ULAF_ECOL5

Accession

Primary (citable) accession number: Q0T9J5

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	September 5, 2006
Last modified:	July 13, 2010
This is version 32 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)