Q8Z167 (ULAF_SALTI) 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:	STY4744, t4439

Organism

Salmonella typhi [Complete proteome] [HAMAP]

Taxonomic identifier

90370 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella

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_0000233246
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)
	Q8Z167 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 16399D60CE4E55A8	FASTA	228	25,313
	10 20 30 40 50 60 MQKLKQQVFD ANMDLPRYGL VTFTWGNVSA IDRERGLVVI KPSGVAYETM KVDDMVVVDM 70 80 90 100 110 120 DGKVVEGRYR PSSDTATHLA LYQRYPSLGG VVHTHSTHAT AWAQAGMAIP ALGTTHADYF 130 140 150 160 170 180 FGDIPCTRAL SEEEVQGEYE LNTGKVIIET LGEVEPLHTP GIVVYQHGPF AWGKDAHDAV 190 200 210 220 HNAVVMEEVA RMAWIARGIN PGLNPIDDYL MNKHFMRKHG PNAYYGQK

References

[1]

"Complete genome sequence of a multiple drug resistant Salmonella enterica serovar Typhi CT18." Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J., Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M., Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A., Davis P. , Davies R.M., Dowd L., White N., Farrar J., Feltwell T., Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A., Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G. Nature 413:848-852(2001) [PubMed: 11677608] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CT18.

[2]

"Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and CT18." Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V., Kodoyianni V., Schwartz D.C., Blattner F.R. J. Bacteriol. 185:2330-2337(2003) [PubMed: 12644504] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700931 / Ty2.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL627283 Genomic DNA. Translation: CAD06865.1. AE014613 Genomic DNA. Translation: AAO71886.1.
RefSeq	NP_458822.1. NC_003198.1. NP_808026.1. NC_004631.1.
3D structure databases
ProteinModelPortal	Q8Z167.
SMR	Q8Z167. Positions 1-219.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1068196. 1250946.
GenomeReviews	Gene locus t4439 in contig AE014613_GR. Gene locus STY4744 in contig AL513382_GR.
KEGG	stt:t4439. sty:STY4744.
PATRIC	18547740. VBISalEnt120419_4845.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG541069.
OMA	IDSYLMN.
ProtClustDB	PRK12348.
Enzyme and pathway databases
BioCyc	SENT209261:T4439-MONOMER. SENT220341:STY4744-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_SALTI

Accession

Primary (citable) accession number: Q8Z167
Secondary accession number(s): Q7C542

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2006
Last sequence update:	March 1, 2002
Last modified:	January 25, 2012
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program