Reviewed, UniProtKB/Swiss-Prot A7ZV69 (ULAF_ECO24)

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:	EcE24377A_4759

Organism

Escherichia coli O139:H28 (strain E24377A / ETEC) [Complete proteome] [HAMAP]

Taxonomic identifier

331111 [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_1000070636
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)
	A7ZV69-1 [UniParc]. Last modified October 23, 2007. Version 1. Checksum: 36C4B13C71DAFA33	FASTA	228	25,398
	10 20 30 40 50 60 MQKLKQQVFE ANMDLPRYGL VTFTWGNVSA IDRERGLVVI KPSGVAYETM KADDMVVVDM 70 80 90 100 110 120 SGKVVEGEYR PSSDTATHLE LYRRYPSLGG IVHTHSTHAT AWAQAGLAIP ALGTTHADYF 130 140 150 160 170 180 FGDIPYTRGL SEEEVQGEYE LNTGKVIIET LGNAEPLHTP GIVVYQHGPF AWGKDAHDAV 190 200 210 220 HNAVVMEEVA KMAWIARSIN PQLNHIDSFL MNKHFMRKHG PNAYYGQK

ReferencesHide

[1]

"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates." Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J. J. Bacteriol. 190:6881-6893(2008) [PubMed: 18676672] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-referencesHide

Sequence databases
EMBL GenBank DDBJ	CP000800 Genomic DNA. Translation: ABV16756.1.
RefSeq	YP_001465698.1.
3D structure databases
SMR	A7ZV69. Positions 1-219.
ModBase	Search...
Protein-protein interaction databases
STRING	A7ZV69.
Genome annotation databases
EnsemblBacteria	EBESCT00000020423; EBESCP00000019485; EBESCG00000019477.
GeneID	5590579.
GenomeReviews	Gene locus EcE24377A_4759 in contig CP000800_GR.
KEGG	ecw:EcE24377A_4759.
NMPDR	fig|331111.3.peg.2355.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0235.
HOGENOM	HBG541069.
OMA	AYVYRHM.
ProtClustDB	PRK12348.
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_ECO24

Accession

Primary (citable) accession number: A7ZV69

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	October 23, 2007
Last modified:	July 13, 2010
This is version 25 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)