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Reviewed, UniProtKB/Swiss-Prot A7ZV69 (ULAF_ECO24)

Last modified July 13, 2010. Version 25. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
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Names and originHide

Protein namesRecommended 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
OrganismEscherichia coli O139:H28 (strain E24377A / ETEC) [Complete proteome] [HAMAP]
Taxonomic identifier331111 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
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Protein attributesHide

Sequence length228 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level.
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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.

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OntologiesHide

Keywords
   LigandMetal-binding
Zinc
   Molecular functionIsomerase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processL-ascorbic acid metabolic process

Inferred from electronic annotation. Source: HAMAP

   Molecular functionL-ribulose-phosphate 4-epimerase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...
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Sequence annotation (Features)Hide

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 228228L-ribulose-5-phosphate 4-epimerase ulaF HAMAP MF_01952
PRO_1000070636

Sites

Metal binding741Zinc By similarity
Metal binding931Zinc By similarity
Metal binding951Zinc By similarity
Metal binding1671Zinc By similarity
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SequencesHide

Sequence LengthMass (Da)Tools
A7ZV69-1 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: 36C4B13C71DAFA33

FASTA22825,398
        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 

« Hide

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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].
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Cross-referencesHide

Sequence databases

EMBL
GenBank
DDBJ
CP000800 Genomic DNA. Translation: ABV16756.1.
RefSeqYP_001465698.1.

3D structure databases

SMRA7ZV69. Positions 1-219.
ModBaseSearch...

Protein-protein interaction databases

STRINGA7ZV69.

Genome annotation databases

EnsemblBacteriaEBESCT00000020423; EBESCP00000019485; EBESCG00000019477.
GeneID5590579.
GenomeReviewsGene locus EcE24377A_4759 in contig CP000800_GR.
KEGGecw:EcE24377A_4759.
NMPDRfig|331111.3.peg.2355.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0235.
HOGENOMHBG541069.
OMAAYVYRHM.
ProtClustDBPRK12348.

Family and domain databases

HAMAPMF_01952. UlaF.
[Tree]
InterProIPR001303. Aldolase_II/adducin_N.
[Graphical view]
Gene3DG3DSA:3.40.225.10. Aldolase_II/adducin_N. 1 hit.
PfamPF00596. Aldolase_II. 1 hit.
[Graphical view]
SUPFAMSSF53639. Aldolase_II_N. 1 hit.
ProtoNetSearch...
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Entry informationHide

Entry nameULAF_ECO24
AccessionPrimary (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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)
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Relevant documentsHide

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents