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UniProtKB - Q9WYP7 (IOLO_THEMA)
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>sp|Q9WYP7|IOLO_THEMA 5-keto-L-gluconate epimerase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=iolO PE=1 SV=1 MKLSLVISTSDAAFDALAFKGDLRKGMELAKRVGYQAVEIAVRDPSIVDWNEVKILSEEL NLPICAIGTGQAYLADGLSLTHPNDEIRKKAIERVVKHTEVAGMFGALVIIGLVRGRREG RSYEETEELFIESMKRLLELTEHAKFVIEPLNRYETDFINTIDDALRILRKINSNRVGIL ADTFHMNIEEVNIPESLKRAGEKLYHFHVADSNRWAPGCGHFDFRSVFNTLKEIGYNRYV SVECLPLPGGMEEAAEIAFKTLKELIIKLTCommunity curation ()Add a publicationFeedback
Protein
5-keto-L-gluconate epimerase
Gene
iolO
Organism
Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
Status
Reviewed-Annotation score:
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
Catalyzes the reversible epimerization between 5-keto-L-gluconate (5-dehydro-L-gluconate) and D-tagaturonate, and thus probably functions in a myo-inositol degradation pathway together with IolG, IolM and IolN (PubMed:23441918).
Is not active on the enantiomer 5-keto-D-gluconate (PubMed:23441918).
Was also shown to be a nonphosphorylated sugar isomerase with broad substrate specificity in vitro (PubMed:28258150).
Is able to catalyze the reversible C3-epimerization of L-ribulose to L-xylulose, D-ribulose to D-xylulose, D-psicose to D-fructose, and D-tagatose to D-sorbose, with a substrate preference for ketopentoses rather than ketohexoses (PubMed:28258150).
Also catalyzes the aldose-ketose isomerization reaction from either D-erythrose or D-threose to D-erythrulose (PubMed:28258150).
Exhibits no activity for C4-epimerization of D-tagatose to D-fructose (PubMed:28258150).
2 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.2"Novel inositol catabolic pathway in Thermotoga maritima."
Rodionova I.A., Leyn S.A., Burkart M.D., Boucher N., Noll K.M., Osterman A.L., Rodionov D.A.
Environ. Microbiol. 15:2254-2266(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY. - Ref.4"TM0416 is a hyperthermophilic promiscuous non-phosphorylated sugar isomerase that catalyzes various C5 and C6 epimerization reactions."
Shin S.M., Cao T.P., Choi J.M., Kim S.B., Lee S.J., Lee S.H., Lee D.W.
Appl. Environ. Microbiol. 0:0-0(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS) IN COMPLEXES WITH COBALT IONS; NICKEL IONS; COPPER IONS; MANGANESE IONS AND L-ERYTHRULOSE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT, BIOTECHNOLOGY, ACTIVE SITE, REACTION MECHANISM.
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
- 5-dehydro-L-gluconate
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Manual assertion based on experiment ini
- Ref.2"Novel inositol catabolic pathway in Thermotoga maritima."
Rodionova I.A., Leyn S.A., Burkart M.D., Boucher N., Noll K.M., Osterman A.L., Rodionov D.A.
Environ. Microbiol. 15:2254-2266(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY.
Source: Rhea- Search for this reaction in UniProtKB.
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5-dehydro-L-gluconate- Search proteins in UniProtKB for this molecule.
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=keto-D-tagaturonate- Search proteins in UniProtKB for this molecule.
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- L-ribulose
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Manual assertion based on experiment ini
- Ref.4"TM0416 is a hyperthermophilic promiscuous non-phosphorylated sugar isomerase that catalyzes various C5 and C6 epimerization reactions."
Shin S.M., Cao T.P., Choi J.M., Kim S.B., Lee S.J., Lee S.H., Lee D.W.
Appl. Environ. Microbiol. 0:0-0(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS) IN COMPLEXES WITH COBALT IONS; NICKEL IONS; COPPER IONS; MANGANESE IONS AND L-ERYTHRULOSE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT, BIOTECHNOLOGY, ACTIVE SITE, REACTION MECHANISM.
Source: Rhea- Search for this reaction in UniProtKB.
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L-ribulose- Search proteins in UniProtKB for this molecule.
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=L-xylulose- Search proteins in UniProtKB for this molecule.
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- D-ribulose
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Manual assertion based on experiment ini
- Ref.4"TM0416 is a hyperthermophilic promiscuous non-phosphorylated sugar isomerase that catalyzes various C5 and C6 epimerization reactions."
Shin S.M., Cao T.P., Choi J.M., Kim S.B., Lee S.J., Lee S.H., Lee D.W.
Appl. Environ. Microbiol. 0:0-0(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS) IN COMPLEXES WITH COBALT IONS; NICKEL IONS; COPPER IONS; MANGANESE IONS AND L-ERYTHRULOSE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT, BIOTECHNOLOGY, ACTIVE SITE, REACTION MECHANISM.
Source: Rhea- Search for this reaction in UniProtKB.
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D-ribulose- Search proteins in UniProtKB for this molecule.
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=D-xylulose- Search proteins in UniProtKB for this molecule.
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- keto-D-tagatose
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Manual assertion based on experiment ini
- Ref.4"TM0416 is a hyperthermophilic promiscuous non-phosphorylated sugar isomerase that catalyzes various C5 and C6 epimerization reactions."
Shin S.M., Cao T.P., Choi J.M., Kim S.B., Lee S.J., Lee S.H., Lee D.W.
Appl. Environ. Microbiol. 0:0-0(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS) IN COMPLEXES WITH COBALT IONS; NICKEL IONS; COPPER IONS; MANGANESE IONS AND L-ERYTHRULOSE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT, BIOTECHNOLOGY, ACTIVE SITE, REACTION MECHANISM.
Source: Rhea- Search for this reaction in UniProtKB.
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keto-D-tagatose- Search proteins in UniProtKB for this molecule.
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=keto-D-sorbose- Search proteins in UniProtKB for this molecule.
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- D-allulose
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Manual assertion based on experiment ini
- Ref.4"TM0416 is a hyperthermophilic promiscuous non-phosphorylated sugar isomerase that catalyzes various C5 and C6 epimerization reactions."
Shin S.M., Cao T.P., Choi J.M., Kim S.B., Lee S.J., Lee S.H., Lee D.W.
Appl. Environ. Microbiol. 0:0-0(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS) IN COMPLEXES WITH COBALT IONS; NICKEL IONS; COPPER IONS; MANGANESE IONS AND L-ERYTHRULOSE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT, BIOTECHNOLOGY, ACTIVE SITE, REACTION MECHANISM.
Source: Rhea- Search for this reaction in UniProtKB.
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D-allulose- Search proteins in UniProtKB for this molecule.
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=keto-D-fructose- Search proteins in UniProtKB for this molecule.
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- D-erythrose
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Manual assertion based on experiment ini
- Ref.4"TM0416 is a hyperthermophilic promiscuous non-phosphorylated sugar isomerase that catalyzes various C5 and C6 epimerization reactions."
Shin S.M., Cao T.P., Choi J.M., Kim S.B., Lee S.J., Lee S.H., Lee D.W.
Appl. Environ. Microbiol. 0:0-0(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS) IN COMPLEXES WITH COBALT IONS; NICKEL IONS; COPPER IONS; MANGANESE IONS AND L-ERYTHRULOSE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT, BIOTECHNOLOGY, ACTIVE SITE, REACTION MECHANISM.
Source: Rhea- Search for this reaction in UniProtKB.
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D-erythrose- Search proteins in UniProtKB for this molecule.
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=D-erythrulose- Search proteins in UniProtKB for this molecule.
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- D-threose
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Manual assertion based on experiment ini
- Ref.4"TM0416 is a hyperthermophilic promiscuous non-phosphorylated sugar isomerase that catalyzes various C5 and C6 epimerization reactions."
Shin S.M., Cao T.P., Choi J.M., Kim S.B., Lee S.J., Lee S.H., Lee D.W.
Appl. Environ. Microbiol. 0:0-0(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS) IN COMPLEXES WITH COBALT IONS; NICKEL IONS; COPPER IONS; MANGANESE IONS AND L-ERYTHRULOSE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT, BIOTECHNOLOGY, ACTIVE SITE, REACTION MECHANISM.
Source: Rhea- Search for this reaction in UniProtKB.
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D-threose- Search proteins in UniProtKB for this molecule.
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=D-erythrulose- Search proteins in UniProtKB for this molecule.
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<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori
Mn2+
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Manual assertion based on experiment ini
- Ref.4"TM0416 is a hyperthermophilic promiscuous non-phosphorylated sugar isomerase that catalyzes various C5 and C6 epimerization reactions."
Shin S.M., Cao T.P., Choi J.M., Kim S.B., Lee S.J., Lee S.H., Lee D.W.
Appl. Environ. Microbiol. 0:0-0(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS) IN COMPLEXES WITH COBALT IONS; NICKEL IONS; COPPER IONS; MANGANESE IONS AND L-ERYTHRULOSE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT, BIOTECHNOLOGY, ACTIVE SITE, REACTION MECHANISM.
- Search proteins in UniProtKB for this molecule.
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Manual assertion based on experiment ini
- Ref.4"TM0416 is a hyperthermophilic promiscuous non-phosphorylated sugar isomerase that catalyzes various C5 and C6 epimerization reactions."
Shin S.M., Cao T.P., Choi J.M., Kim S.B., Lee S.J., Lee S.H., Lee D.W.
Appl. Environ. Microbiol. 0:0-0(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS) IN COMPLEXES WITH COBALT IONS; NICKEL IONS; COPPER IONS; MANGANESE IONS AND L-ERYTHRULOSE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT, BIOTECHNOLOGY, ACTIVE SITE, REACTION MECHANISM.
- Search proteins in UniProtKB for this molecule.
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Manual assertion based on experiment ini
- Ref.4"TM0416 is a hyperthermophilic promiscuous non-phosphorylated sugar isomerase that catalyzes various C5 and C6 epimerization reactions."
Shin S.M., Cao T.P., Choi J.M., Kim S.B., Lee S.J., Lee S.H., Lee D.W.
Appl. Environ. Microbiol. 0:0-0(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS) IN COMPLEXES WITH COBALT IONS; NICKEL IONS; COPPER IONS; MANGANESE IONS AND L-ERYTHRULOSE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT, BIOTECHNOLOGY, ACTIVE SITE, REACTION MECHANISM.
Manual assertion based on experiment ini
- Ref.4"TM0416 is a hyperthermophilic promiscuous non-phosphorylated sugar isomerase that catalyzes various C5 and C6 epimerization reactions."
Shin S.M., Cao T.P., Choi J.M., Kim S.B., Lee S.J., Lee S.H., Lee D.W.
Appl. Environ. Microbiol. 0:0-0(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS) IN COMPLEXES WITH COBALT IONS; NICKEL IONS; COPPER IONS; MANGANESE IONS AND L-ERYTHRULOSE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT, BIOTECHNOLOGY, ACTIVE SITE, REACTION MECHANISM.
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi
Is completely inhibited by EDTA in vitro.1 Publication
Manual assertion based on experiment ini
- Ref.4"TM0416 is a hyperthermophilic promiscuous non-phosphorylated sugar isomerase that catalyzes various C5 and C6 epimerization reactions."
Shin S.M., Cao T.P., Choi J.M., Kim S.B., Lee S.J., Lee S.H., Lee D.W.
Appl. Environ. Microbiol. 0:0-0(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS) IN COMPLEXES WITH COBALT IONS; NICKEL IONS; COPPER IONS; MANGANESE IONS AND L-ERYTHRULOSE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT, BIOTECHNOLOGY, ACTIVE SITE, REACTION MECHANISM.
<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi
- KM=452 mM for D-erythrose (at pH 7 and 70 degrees Celsius)1 Publication
Manual assertion based on experiment ini
- Ref.4"TM0416 is a hyperthermophilic promiscuous non-phosphorylated sugar isomerase that catalyzes various C5 and C6 epimerization reactions."
Shin S.M., Cao T.P., Choi J.M., Kim S.B., Lee S.J., Lee S.H., Lee D.W.
Appl. Environ. Microbiol. 0:0-0(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS) IN COMPLEXES WITH COBALT IONS; NICKEL IONS; COPPER IONS; MANGANESE IONS AND L-ERYTHRULOSE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT, BIOTECHNOLOGY, ACTIVE SITE, REACTION MECHANISM.
- KM=232 mM for D-threose (at pH 7 and 70 degrees Celsius)1 Publication
Manual assertion based on experiment ini
- Ref.4"TM0416 is a hyperthermophilic promiscuous non-phosphorylated sugar isomerase that catalyzes various C5 and C6 epimerization reactions."
Shin S.M., Cao T.P., Choi J.M., Kim S.B., Lee S.J., Lee S.H., Lee D.W.
Appl. Environ. Microbiol. 0:0-0(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS) IN COMPLEXES WITH COBALT IONS; NICKEL IONS; COPPER IONS; MANGANESE IONS AND L-ERYTHRULOSE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT, BIOTECHNOLOGY, ACTIVE SITE, REACTION MECHANISM.
- KM=78 mM for D-erythrulose (at pH 7 and 70 degrees Celsius)1 Publication
Manual assertion based on experiment ini
- Ref.4"TM0416 is a hyperthermophilic promiscuous non-phosphorylated sugar isomerase that catalyzes various C5 and C6 epimerization reactions."
Shin S.M., Cao T.P., Choi J.M., Kim S.B., Lee S.J., Lee S.H., Lee D.W.
Appl. Environ. Microbiol. 0:0-0(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS) IN COMPLEXES WITH COBALT IONS; NICKEL IONS; COPPER IONS; MANGANESE IONS AND L-ERYTHRULOSE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT, BIOTECHNOLOGY, ACTIVE SITE, REACTION MECHANISM.
- KM=46 mM for L-ribulose (at pH 7 and 70 degrees Celsius)1 Publication
Manual assertion based on experiment ini
- Ref.4"TM0416 is a hyperthermophilic promiscuous non-phosphorylated sugar isomerase that catalyzes various C5 and C6 epimerization reactions."
Shin S.M., Cao T.P., Choi J.M., Kim S.B., Lee S.J., Lee S.H., Lee D.W.
Appl. Environ. Microbiol. 0:0-0(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS) IN COMPLEXES WITH COBALT IONS; NICKEL IONS; COPPER IONS; MANGANESE IONS AND L-ERYTHRULOSE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT, BIOTECHNOLOGY, ACTIVE SITE, REACTION MECHANISM.
- KM=348 mM for D-ribulose (at pH 7 and 70 degrees Celsius)1 Publication
Manual assertion based on experiment ini
- Ref.4"TM0416 is a hyperthermophilic promiscuous non-phosphorylated sugar isomerase that catalyzes various C5 and C6 epimerization reactions."
Shin S.M., Cao T.P., Choi J.M., Kim S.B., Lee S.J., Lee S.H., Lee D.W.
Appl. Environ. Microbiol. 0:0-0(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS) IN COMPLEXES WITH COBALT IONS; NICKEL IONS; COPPER IONS; MANGANESE IONS AND L-ERYTHRULOSE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT, BIOTECHNOLOGY, ACTIVE SITE, REACTION MECHANISM.
- KM=459 mM for L-xylulose (at pH 7 and 70 degrees Celsius)1 Publication
Manual assertion based on experiment ini
- Ref.4"TM0416 is a hyperthermophilic promiscuous non-phosphorylated sugar isomerase that catalyzes various C5 and C6 epimerization reactions."
Shin S.M., Cao T.P., Choi J.M., Kim S.B., Lee S.J., Lee S.H., Lee D.W.
Appl. Environ. Microbiol. 0:0-0(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS) IN COMPLEXES WITH COBALT IONS; NICKEL IONS; COPPER IONS; MANGANESE IONS AND L-ERYTHRULOSE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT, BIOTECHNOLOGY, ACTIVE SITE, REACTION MECHANISM.
- KM=2332 mM for D-xylulose (at pH 7 and 70 degrees Celsius)1 Publication
Manual assertion based on experiment ini
- Ref.4"TM0416 is a hyperthermophilic promiscuous non-phosphorylated sugar isomerase that catalyzes various C5 and C6 epimerization reactions."
Shin S.M., Cao T.P., Choi J.M., Kim S.B., Lee S.J., Lee S.H., Lee D.W.
Appl. Environ. Microbiol. 0:0-0(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS) IN COMPLEXES WITH COBALT IONS; NICKEL IONS; COPPER IONS; MANGANESE IONS AND L-ERYTHRULOSE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT, BIOTECHNOLOGY, ACTIVE SITE, REACTION MECHANISM.
- Vmax=1.23 µmol/min/mg enzyme with D-erythrose as substrate (at pH 7 and 70 degrees Celsius)1 Publication
Manual assertion based on experiment ini
- Ref.4"TM0416 is a hyperthermophilic promiscuous non-phosphorylated sugar isomerase that catalyzes various C5 and C6 epimerization reactions."
Shin S.M., Cao T.P., Choi J.M., Kim S.B., Lee S.J., Lee S.H., Lee D.W.
Appl. Environ. Microbiol. 0:0-0(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS) IN COMPLEXES WITH COBALT IONS; NICKEL IONS; COPPER IONS; MANGANESE IONS AND L-ERYTHRULOSE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT, BIOTECHNOLOGY, ACTIVE SITE, REACTION MECHANISM.
- Vmax=0.64 µmol/min/mg enzyme with D-threose as substrate (at pH 7 and 70 degrees Celsius)1 Publication
Manual assertion based on experiment ini
- Ref.4"TM0416 is a hyperthermophilic promiscuous non-phosphorylated sugar isomerase that catalyzes various C5 and C6 epimerization reactions."
Shin S.M., Cao T.P., Choi J.M., Kim S.B., Lee S.J., Lee S.H., Lee D.W.
Appl. Environ. Microbiol. 0:0-0(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS) IN COMPLEXES WITH COBALT IONS; NICKEL IONS; COPPER IONS; MANGANESE IONS AND L-ERYTHRULOSE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT, BIOTECHNOLOGY, ACTIVE SITE, REACTION MECHANISM.
- Vmax=0.08 µmol/min/mg enzyme with D-erythrulose as substrate (at pH 7 and 70 degrees Celsius)1 Publication
Manual assertion based on experiment ini
- Ref.4"TM0416 is a hyperthermophilic promiscuous non-phosphorylated sugar isomerase that catalyzes various C5 and C6 epimerization reactions."
Shin S.M., Cao T.P., Choi J.M., Kim S.B., Lee S.J., Lee S.H., Lee D.W.
Appl. Environ. Microbiol. 0:0-0(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS) IN COMPLEXES WITH COBALT IONS; NICKEL IONS; COPPER IONS; MANGANESE IONS AND L-ERYTHRULOSE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT, BIOTECHNOLOGY, ACTIVE SITE, REACTION MECHANISM.
- Vmax=0.23 µmol/min/mg enzyme with L-ribulose as substrate (at pH 7 and 70 degrees Celsius)1 Publication
Manual assertion based on experiment ini
- Ref.4"TM0416 is a hyperthermophilic promiscuous non-phosphorylated sugar isomerase that catalyzes various C5 and C6 epimerization reactions."
Shin S.M., Cao T.P., Choi J.M., Kim S.B., Lee S.J., Lee S.H., Lee D.W.
Appl. Environ. Microbiol. 0:0-0(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS) IN COMPLEXES WITH COBALT IONS; NICKEL IONS; COPPER IONS; MANGANESE IONS AND L-ERYTHRULOSE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT, BIOTECHNOLOGY, ACTIVE SITE, REACTION MECHANISM.
- Vmax=0.62 µmol/min/mg enzyme with D-ribulose as substrate (at pH 7 and 70 degrees Celsius)1 Publication
Manual assertion based on experiment ini
- Ref.4"TM0416 is a hyperthermophilic promiscuous non-phosphorylated sugar isomerase that catalyzes various C5 and C6 epimerization reactions."
Shin S.M., Cao T.P., Choi J.M., Kim S.B., Lee S.J., Lee S.H., Lee D.W.
Appl. Environ. Microbiol. 0:0-0(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS) IN COMPLEXES WITH COBALT IONS; NICKEL IONS; COPPER IONS; MANGANESE IONS AND L-ERYTHRULOSE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT, BIOTECHNOLOGY, ACTIVE SITE, REACTION MECHANISM.
- Vmax=1.4 µmol/min/mg enzyme with L-xylulose as substrate (at pH 7 and 70 degrees Celsius)1 Publication
Manual assertion based on experiment ini
- Ref.4"TM0416 is a hyperthermophilic promiscuous non-phosphorylated sugar isomerase that catalyzes various C5 and C6 epimerization reactions."
Shin S.M., Cao T.P., Choi J.M., Kim S.B., Lee S.J., Lee S.H., Lee D.W.
Appl. Environ. Microbiol. 0:0-0(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS) IN COMPLEXES WITH COBALT IONS; NICKEL IONS; COPPER IONS; MANGANESE IONS AND L-ERYTHRULOSE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT, BIOTECHNOLOGY, ACTIVE SITE, REACTION MECHANISM.
- Vmax=0.26 µmol/min/mg enzyme with D-xylulose as substrate (at pH 7 and 70 degrees Celsius)1 Publication
Manual assertion based on experiment ini
- Ref.4"TM0416 is a hyperthermophilic promiscuous non-phosphorylated sugar isomerase that catalyzes various C5 and C6 epimerization reactions."
Shin S.M., Cao T.P., Choi J.M., Kim S.B., Lee S.J., Lee S.H., Lee D.W.
Appl. Environ. Microbiol. 0:0-0(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS) IN COMPLEXES WITH COBALT IONS; NICKEL IONS; COPPER IONS; MANGANESE IONS AND L-ERYTHRULOSE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT, BIOTECHNOLOGY, ACTIVE SITE, REACTION MECHANISM.
pH dependencei
Optimum pH is 6.5-7.0 with L-ribulose as substrate.1 Publication
Manual assertion based on experiment ini
- Ref.4"TM0416 is a hyperthermophilic promiscuous non-phosphorylated sugar isomerase that catalyzes various C5 and C6 epimerization reactions."
Shin S.M., Cao T.P., Choi J.M., Kim S.B., Lee S.J., Lee S.H., Lee D.W.
Appl. Environ. Microbiol. 0:0-0(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS) IN COMPLEXES WITH COBALT IONS; NICKEL IONS; COPPER IONS; MANGANESE IONS AND L-ERYTHRULOSE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT, BIOTECHNOLOGY, ACTIVE SITE, REACTION MECHANISM.
Temperature dependencei
Optimum temperature is about 80 degrees Celsius with L-ribulose as substrate. Is hyperthermostable, with an apparent melting temperature (Tm) of 102.4 degrees Celsius.1 Publication
Manual assertion based on experiment ini
- Ref.4"TM0416 is a hyperthermophilic promiscuous non-phosphorylated sugar isomerase that catalyzes various C5 and C6 epimerization reactions."
Shin S.M., Cao T.P., Choi J.M., Kim S.B., Lee S.J., Lee S.H., Lee D.W.
Appl. Environ. Microbiol. 0:0-0(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS) IN COMPLEXES WITH COBALT IONS; NICKEL IONS; COPPER IONS; MANGANESE IONS AND L-ERYTHRULOSE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT, BIOTECHNOLOGY, ACTIVE SITE, REACTION MECHANISM.
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: myo-inositol metabolism
This protein is involved in the pathway myo-inositol metabolism, which is part of Polyol metabolism.1 Publication<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
- Ref.2"Novel inositol catabolic pathway in Thermotoga maritima."
Rodionova I.A., Leyn S.A., Burkart M.D., Boucher N., Noll K.M., Osterman A.L., Rodionov D.A.
Environ. Microbiol. 15:2254-2266(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY.
View all proteins of this organism that are known to be involved in the pathway myo-inositol metabolism and in Polyol metabolism.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 149 | Proton donor/acceptor1 Publication Manual assertion inferred by curator fromi
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 149 | ManganeseCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0007744">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 155 | SubstrateCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
| Metal bindingi | 182 | ManganeseCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
| Binding sitei | 185 | Substrate; via tele nitrogenCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
| Metal bindingi | 208 | Manganese; via pros nitrogenCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
| Binding sitei | 214 | SubstrateCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
| Active sitei | 243 | Proton donor/acceptor1 Publication Manual assertion inferred by curator fromi
| 1 | |
| Metal bindingi | 243 | ManganeseCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- isomerase activity Source: UniProtKB-KW
- metal ion binding Source: UniProtKB-KW
GO - Biological processi
- inositol metabolic process Source: UniProtKB-UniPathway
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Isomerase |
| Biological process | Carbohydrate metabolism |
| Ligand | Manganese, Metal-binding |
Enzyme and pathway databases
UniPathway: a resource for the exploration and annotation of metabolic pathways More...UniPathwayi | UPA00914 |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: 5-keto-L-gluconate epimerase1 Publication<p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
Manual assertion based on experiment ini
Alternative name(s): Bifunctional nonphosphorylated sugar isomerase1 Publication Manual assertion based on opinion ini
D-erythrose/D-threose isomerase1 Publication Manual assertion based on opinion ini
L-ribulose 3-epimerase1 Publication Manual assertion based on opinion ini
Short name: R3E1 Publication Manual assertion based on opinion ini
Nonphosphorylated sugar 3-epimerase1 Publication Manual assertion inferred by curator fromi
Manual assertion based on experiment ini
Nonphosphorylated sugar aldose-ketose isomerase1 Publication Manual assertion inferred by curator fromi
Manual assertion based on experiment ini
|
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:iolO1 Publication Manual assertion based on opinion ini
Ordered Locus Names:TM_0416 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 243274 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Bacteria › Thermotogae › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga › Thermotoga maritima |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>This subsection of the 'Pathology and Biotech' section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei
High thermostability and very broad substrate specificity of this enzyme make it a potential candidate for the production of rare sugars for the food and pharmaceutical industries.1 Publication
Manual assertion inferred by curator fromi
- Ref.4"TM0416 is a hyperthermophilic promiscuous non-phosphorylated sugar isomerase that catalyzes various C5 and C6 epimerization reactions."
Shin S.M., Cao T.P., Choi J.M., Kim S.B., Lee S.J., Lee S.H., Lee D.W.
Appl. Environ. Microbiol. 0:0-0(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS) IN COMPLEXES WITH COBALT IONS; NICKEL IONS; COPPER IONS; MANGANESE IONS AND L-ERYTHRULOSE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT, BIOTECHNOLOGY, ACTIVE SITE, REACTION MECHANISM.
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000209114 | 1 – 270 | 5-keto-L-gluconate epimeraseAdd BLAST | 270 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
Homodimer.
1 PublicationManual assertion based on experiment ini
- Ref.4"TM0416 is a hyperthermophilic promiscuous non-phosphorylated sugar isomerase that catalyzes various C5 and C6 epimerization reactions."
Shin S.M., Cao T.P., Choi J.M., Kim S.B., Lee S.J., Lee S.H., Lee D.W.
Appl. Environ. Microbiol. 0:0-0(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS) IN COMPLEXES WITH COBALT IONS; NICKEL IONS; COPPER IONS; MANGANESE IONS AND L-ERYTHRULOSE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT, BIOTECHNOLOGY, ACTIVE SITE, REACTION MECHANISM.
Protein-protein interaction databases
STRING: functional protein association networks More...STRINGi | 243274.THEMA_02645 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsHide details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 2 – 6 | Combined sources <p>Information inferred from a combination of experimental and computational evidence, without manual validation.</p> <p><a href="/manual/evidences#ECO:0000213">More...</a></p> Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 12 – 14 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 16 – 33 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 18 | |
| Beta strandi | 36 – 41 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Helixi | 45 – 47 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 50 – 60 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 11 | |
| Beta strandi | 64 – 68 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 71 – 74 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 85 – 105 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 21 | |
| Beta strandi | 108 – 112 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 113 – 115 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 123 – 140 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 18 | |
| Beta strandi | 146 – 148 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code 'T'.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 153 – 155 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 162 – 172 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 11 | |
| Beta strandi | 177 – 182 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Helixi | 183 – 189 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
| Helixi | 193 – 200 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
| Helixi | 201 – 203 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 204 – 209 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 214 – 216 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 224 – 233 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 10 | |
| Beta strandi | 238 – 242 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| Turni | 247 – 249 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 251 – 267 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 17 |
3D structure databases
AlphaFold Protein Structure Database More...AlphaFoldDBi | Q9WYP7 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q9WYP7 |
Database of comparative protein structure models More...ModBasei | Search... |
Protein Data Bank in Europe - Knowledge Base More...PDBe-KBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q9WYP7 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Belongs to the hyi family.Curated
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | COG1082, Bacteria |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q9WYP7 |
Identification of Orthologs from Complete Genome Data More...OMAi | AMFDTHH |
Database of Orthologous Groups More...OrthoDBi | 1007505at2 |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR036237, Xyl_isomerase-like_sf IPR013022, Xyl_isomerase-like_TIM-brl |
Pfam protein domain database More...Pfami | View protein in Pfam PF01261, AP_endonuc_2, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF51658, SSF51658, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
Q9WYP7-1 [UniParc]FASTAAdd to basketAdded to basket
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MKLSLVISTS DAAFDALAFK GDLRKGMELA KRVGYQAVEI AVRDPSIVDW
60 70 80 90 100
NEVKILSEEL NLPICAIGTG QAYLADGLSL THPNDEIRKK AIERVVKHTE
110 120 130 140 150
VAGMFGALVI IGLVRGRREG RSYEETEELF IESMKRLLEL TEHAKFVIEP
160 170 180 190 200
LNRYETDFIN TIDDALRILR KINSNRVGIL ADTFHMNIEE VNIPESLKRA
210 220 230 240 250
GEKLYHFHVA DSNRWAPGCG HFDFRSVFNT LKEIGYNRYV SVECLPLPGG
260 270
MEEAAEIAFK TLKELIIKLT
Length:270
Mass (Da):30,464
Last modified:November 1, 1999 - v1
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i10948413A7624158
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | AE000512 Genomic DNA Translation: AAD35501.1 |
Protein sequence database of the Protein Information Resource More...PIRi | F72381 |
NCBI Reference Sequences More...RefSeqi | NP_228226.1, NC_000853.1 WP_004083268.1, NZ_CP011107.1 |
Genome annotation databases
Ensembl bacterial and archaeal genome annotation project More...EnsemblBacteriai | AAD35501; AAD35501; TM_0416 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | tma:TM0416 |
<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| Q9WYP7 | Inosose isomerase | 270 | UniRef100_Q9WYP7 | |||
| +1 | ||||||
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| Q9WYP7 | Inosose isomerase | 270 | UniRef90_Q9WYP7 | |||
| +1 | ||||||
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| Q9WYP7 | Inosose isomerase | 270 | UniRef50_Q9WYP7 | |||
| Sugar phosphate isomerase/epimerase | 271 | |||||
| Xylose isomerase domain-containing protein TIM barrel | 271 | |||||
| Sugar phosphate isomerase/epimerase | 271 | |||||
| Xylose isomerase | 271 | |||||
| +20 | ||||||
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
Sequence databases
| Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AE000512 Genomic DNA Translation: AAD35501.1 |
| PIRi | F72381 |
| RefSeqi | NP_228226.1, NC_000853.1 WP_004083268.1, NZ_CP011107.1 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 2ZVR | X-ray | 2.20 | A/B | 1-270 | [»] | |
| 5B7Y | X-ray | 1.32 | A/B | 1-270 | [»] | |
| 5B7Z | X-ray | 1.50 | A/B | 1-270 | [»] | |
| 5B80 | X-ray | 1.70 | A/B | 1-270 | [»] | |
| 5H1W | X-ray | 1.63 | A/B | 1-270 | [»] | |
| 5H6H | X-ray | 1.45 | A/B | 1-270 | [»] | |
| AlphaFoldDBi | Q9WYP7 | |||||
| SMRi | Q9WYP7 | |||||
| ModBasei | Search... | |||||
| PDBe-KBi | Search... | |||||
Protein-protein interaction databases
| STRINGi | 243274.THEMA_02645 |
Genome annotation databases
| EnsemblBacteriai | AAD35501; AAD35501; TM_0416 |
| KEGGi | tma:TM0416 |
Phylogenomic databases
| eggNOGi | COG1082, Bacteria |
| InParanoidi | Q9WYP7 |
| OMAi | AMFDTHH |
| OrthoDBi | 1007505at2 |
Enzyme and pathway databases
| UniPathwayi | UPA00914 |
Miscellaneous databases
| EvolutionaryTracei | Q9WYP7 |
Family and domain databases
| InterProi | View protein in InterPro IPR036237, Xyl_isomerase-like_sf IPR013022, Xyl_isomerase-like_TIM-brl |
| Pfami | View protein in Pfam PF01261, AP_endonuc_2, 1 hit |
| SUPFAMi | SSF51658, SSF51658, 1 hit |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | IOLO_THEMA | |
| <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | Q9WYP7Primary (citable) accession number: Q9WYP7 | |
| <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | December 1, 2000 |
| Last sequence update: | November 1, 1999 | |
| Last modified: | May 25, 2022 | |
| This is version 109 of the entry and version 1 of the sequence. See complete history. | ||
| <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Prokaryotic Protein Annotation Program | |
<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
