UniProtKB - P39306 (ULAF_ECOLI)
Protein
L-ribulose-5-phosphate 4-epimerase UlaF
Gene
ulaF
Organism
Escherichia coli (strain K12)
Status
Functioni
Catalyzes the isomerization of L-ribulose 5-phosphate to D-xylulose 5-phosphate. Is involved in the anaerobic L-ascorbate utilization.UniRule annotation1 Publication
Catalytic activityi
- EC:5.1.3.4UniRule annotation1 Publication
Cofactori
Zn2+UniRule annotationBy similarityNote: Binds 1 zinc ion per subunit.UniRule annotationBy similarity
Kineticsi
Kcat is 25 sec(-1) with L-ribulose 5-phosphate (LRu5P) as substrate.1 Publication
- KM=657 µM for L-ribulose 5-phosphate (LRu5P)1 Publication
: L-ascorbate degradation Pathwayi
This protein is involved in step 4 of the subpathway that synthesizes D-xylulose 5-phosphate from L-ascorbate.UniRule annotation1 PublicationProteins known to be involved in the 4 steps of the subpathway in this organism are:
- Probable L-ascorbate-6-phosphate lactonase UlaG (ulaG), Probable L-ascorbate-6-phosphate lactonase UlaG (ulaG)
- 3-keto-L-gulonate-6-phosphate decarboxylase UlaD (ulaD), 3-keto-L-gulonate-6-phosphate decarboxylase UlaD (ulaD)
- L-ribulose-5-phosphate 3-epimerase UlaE (ulaE), L-ribulose-5-phosphate 3-epimerase UlaE (ulaE)
- L-ribulose-5-phosphate 4-epimerase UlaF (ulaF), L-ribulose-5-phosphate 4-epimerase UlaF (ulaF)
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-xylulose 5-phosphate from L-ascorbate, the pathway L-ascorbate degradation and in Cofactor degradation.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 74 | ZincUniRule annotationBy similarity | 1 | |
Metal bindingi | 93 | Zinc; via tele nitrogenUniRule annotationBy similarity | 1 | |
Metal bindingi | 95 | Zinc; via tele nitrogenUniRule annotationBy similarity | 1 | |
Active sitei | 118 | Proton donor/acceptorUniRule annotationBy similarity | 1 | |
Metal bindingi | 167 | Zinc; via tele nitrogenUniRule annotationBy similarity | 1 | |
Active sitei | 225 | Proton donor/acceptorUniRule annotationBy similarity | 1 |
GO - Molecular functioni
- aldehyde-lyase activity Source: GO_Central
- L-ribulose-phosphate 4-epimerase activity Source: EcoCyc
- zinc ion binding Source: UniProtKB
GO - Biological processi
- L-ascorbic acid catabolic process Source: UniProtKB-UniPathway
- L-ascorbic acid metabolic process Source: EcoCyc
- pentose catabolic process Source: GO_Central
Keywordsi
Molecular function | Isomerase |
Biological process | Carbohydrate metabolism |
Ligand | Metal-binding, Zinc |
Enzyme and pathway databases
BioCyci | EcoCyc:G7860-MONOMER MetaCyc:G7860-MONOMER |
UniPathwayi | UPA00263;UER00380 |
Names & Taxonomyi
Protein namesi | Recommended name: L-ribulose-5-phosphate 4-epimerase UlaF1 PublicationUniRule annotation (EC:5.1.3.4UniRule annotation1 Publication)Alternative name(s): L-ascorbate utilization protein F1 PublicationUniRule annotation Phosphoribulose isomeraseUniRule annotation |
Gene namesi | Name:ulaF1 PublicationUniRule annotation Synonyms:sgaE, yjfX Ordered Locus Names:b4198, JW4156 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000162921 | 1 – 228 | L-ribulose-5-phosphate 4-epimerase UlaFAdd BLAST | 228 |
Proteomic databases
PaxDbi | P39306 |
PRIDEi | P39306 |
Expressioni
Inductioni
Induced by L-ascorbate. Repressed by UlaR.UniRule annotation2 Publications
Interactioni
Protein-protein interaction databases
BioGRIDi | 4262716, 6 interactors |
DIPi | DIP-10868N |
IntActi | P39306, 12 interactors |
STRINGi | 511145.b4198 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 26 – 27 | Substrate bindingUniRule annotationBy similarity | 2 | |
Regioni | 43 – 44 | Substrate bindingUniRule annotationBy similarity | 2 | |
Regioni | 72 – 73 | Substrate bindingUniRule annotationBy similarity | 2 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG0235, Bacteria |
HOGENOMi | CLU_006033_5_0_6 |
InParanoidi | P39306 |
PhylomeDBi | P39306 |
Family and domain databases
Gene3Di | 3.40.225.10, 1 hit |
HAMAPi | MF_01952, UlaF, 1 hit |
InterProi | View protein in InterPro IPR001303, Aldolase_II/adducin_N IPR036409, Aldolase_II/adducin_N_sf IPR023499, UlaF |
Pfami | View protein in Pfam PF00596, Aldolase_II, 1 hit |
SMARTi | View protein in SMART SM01007, Aldolase_II, 1 hit |
SUPFAMi | SSF53639, SSF53639, 1 hit |
i Sequence
Sequence statusi: Complete.
P39306-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MQKLKQQVFE ANMELPRYGL VTFTWGNVSA IDRERGLVVI KPSGVAYETM
60 70 80 90 100
KAADMVVVDM SGKVVEGEYR PSSDTATHLE LYRRYPSLGG IVHTHSTHAT
110 120 130 140 150
AWAQAGLAIP ALGTTHADYF FGDIPCTRGL SEEEVQGEYE LNTGKVIIET
160 170 180 190 200
LGNAEPLHTP GIVVYQHGPF AWGKDAHDAV HNAVVMEEVA KMAWIARGIN
210 220
PQLNHIDSFL MNKHFMRKHG PNAYYGQK
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U14003 Genomic DNA Translation: AAA97094.1 U00096 Genomic DNA Translation: AAC77155.1 AP009048 Genomic DNA Translation: BAE78199.1 |
PIRi | S56423 |
RefSeqi | NP_418619.1, NC_000913.3 WP_001170847.1, NZ_LN832404.1 |
Genome annotation databases
EnsemblBacteriai | AAC77155; AAC77155; b4198 BAE78199; BAE78199; BAE78199 |
GeneIDi | 948711 |
KEGGi | ecj:JW4156 eco:b4198 |
PATRICi | fig|1411691.4.peg.2503 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U14003 Genomic DNA Translation: AAA97094.1 U00096 Genomic DNA Translation: AAC77155.1 AP009048 Genomic DNA Translation: BAE78199.1 |
PIRi | S56423 |
RefSeqi | NP_418619.1, NC_000913.3 WP_001170847.1, NZ_LN832404.1 |
3D structure databases
SMRi | P39306 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 4262716, 6 interactors |
DIPi | DIP-10868N |
IntActi | P39306, 12 interactors |
STRINGi | 511145.b4198 |
Proteomic databases
PaxDbi | P39306 |
PRIDEi | P39306 |
Genome annotation databases
EnsemblBacteriai | AAC77155; AAC77155; b4198 BAE78199; BAE78199; BAE78199 |
GeneIDi | 948711 |
KEGGi | ecj:JW4156 eco:b4198 |
PATRICi | fig|1411691.4.peg.2503 |
Organism-specific databases
EchoBASEi | EB2391 |
Phylogenomic databases
eggNOGi | COG0235, Bacteria |
HOGENOMi | CLU_006033_5_0_6 |
InParanoidi | P39306 |
PhylomeDBi | P39306 |
Enzyme and pathway databases
UniPathwayi | UPA00263;UER00380 |
BioCyci | EcoCyc:G7860-MONOMER MetaCyc:G7860-MONOMER |
Miscellaneous databases
PROi | PR:P39306 |
Family and domain databases
Gene3Di | 3.40.225.10, 1 hit |
HAMAPi | MF_01952, UlaF, 1 hit |
InterProi | View protein in InterPro IPR001303, Aldolase_II/adducin_N IPR036409, Aldolase_II/adducin_N_sf IPR023499, UlaF |
Pfami | View protein in Pfam PF00596, Aldolase_II, 1 hit |
SMARTi | View protein in SMART SM01007, Aldolase_II, 1 hit |
SUPFAMi | SSF53639, SSF53639, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | ULAF_ECOLI | |
Accessioni | P39306Primary (citable) accession number: P39306 Secondary accession number(s): Q2M6A7 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | February 1, 1995 |
Last sequence update: | February 1, 1995 | |
Last modified: | December 2, 2020 | |
This is version 151 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families