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InterPro: IPR013022 Xylose isomerase-like, TIM barrel domain
Protein matches
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UniProtKB Matches: 8189 proteins |
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Accession
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IPR013022 Xyl_isomerase-like_TIM-brl |
Type
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Domain |
Signatures
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InterPro Relationships
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Children
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IPR012307 Xylose isomerase, TIM barrel domain
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Found in
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IPR004560 Putative hexulose-6-phosphate isomerase
IPR004601 UV-endonuclease UvdE
IPR004628 Mannonate dehydratase
IPR007801 Protein of unknown function DUF692
IPR009308 Rhamnose isomerase
IPR013451 L-rhamnose catabolism isomerase
IPR013452 Xylose isomerase, bacterial type
IPR013453 Xylose isomerase, actinobacteria
IPR013457 Rhamnose isomerase related
IPR014621 Uncharacterised conserved protein, sugar epimerase domain-containing
IPR017643 Hydroxypyruvate isomerase
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Contains
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IPR011418 AP endonuclease, family 2, C-terminal
IPR018246 AP endonuclease, family 2, zinc binding site
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InterPro annotation
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Entry Details in BioMart
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Abstract
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This entry represents a structural motif with a beta/alpha TIM barrel found in several proteins families:
- Endonuclease IV (EC:3.1.21.2), an AP (apurinic/apyrimidinic) endonuclease that primes DNA repair synthesis by cleaving the DNA backbone 5' of AP sites [1].
- L-rhamnose isomerase (EC:5.3.1.14), a tetramer of four TIM barrels that catalyses the isomerisation between aldoses and ketoses, such as between L-rhamnose and L-rhamnulose [2].
- Xylose isomerase (EC:5.3.1.5), which catalyses the first reaction in the catabolism of D-xylose by converting D-xylose to D-xylulose [3].
- Mannonate dehydratase UxuA, which along with mannonate oxidoreductase converts D-fructuronate to 2-keto-3-deoxy-D-gluconate [4].
These proteins share similar, but not identical, metal-binding sites. In addition, xylose isomerase and L-rhamnose isomerase each have additional alpha-helical domains involved in tetramer formation. This entry differs from IPR012307 in having a wider coverage of TIM-barrel protein families.
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Structural links
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Publications
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1.
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Hosfield DJ, Guan Y, Haas BJ, Cunningham RP, Tainer JA.
Structure of the DNA repair enzyme endonuclease IV and its DNA complex: double-nucleotide flipping at abasic sites and three-metal-ion catalysis.
Cell 98 397-408 1999
[PubMed: 10458614]
http://dx.doi.org/10.1016/S0092-8674(00)81968-6
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2.
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Yoshida H, Yamada M, Ohyama Y, Takada G, Izumori K, Kamitori S.
The structures of L-rhamnose isomerase from Pseudomonas stutzeri in complexes with L-rhamnose and D-allose provide insights into broad substrate specificity.
J. Mol. Biol. 365 1505-16 2007
[PubMed: 17141803]
http://dx.doi.org/10.1016/j.jmb.2006.11.004
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3.
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Meilleur F, Snell EH, van der Woerd MJ, Judge RA, Myles DA.
A quasi-Laue neutron crystallographic study of D-xylose isomerase.
Eur. Biophys. J. 35 601-9 2006
[PubMed: 16673077]
http://dx.doi.org/10.1007/s00249-006-0066-6
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4.
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Robert-Baudouy J, Portalier R, Stoeber F.
Regulation of hexuronate system genes in Escherichia coli K-12: multiple regulation of the uxu operon by exuR and uxuR gene products.
J. Bacteriol. 145 211-20 1981
[PubMed: 7007313]
http://ukpmc.ac.uk/articlerender.cgi?tool=EBI&pubmedid=7007313
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Additional Reading
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Mueller-Dieckmann C, Panjikar S, Schmidt A, Mueller S, Kuper J, Geerlof A, Wilmanns M, Singh RK, Tucker PA, Weiss MS.
On the routine use of soft X-rays in macromolecular crystallography. Part IV. Efficient determination of anomalous substructures in biomacromolecules using longer X-ray wavelengths.
Acta Crystallogr. D Biol. Crystallogr. 63 2007 366-80
[PubMed: 17327674]
http://dx.doi.org/10.1107/S0907444906055624
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Garcin ED, Hosfield DJ, Desai SA, Haas BJ, Bjoras M, Cunningham RP, Tainer JA.
DNA apurinic-apyrimidinic site binding and excision by endonuclease IV.
Nat. Struct. Mol. Biol. 15 2008 515-22
[PubMed: 18408731]
http://dx.doi.org/10.1038/nsmb.1414
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Ramagopal UA, Dauter M, Dauter Z.
SAD manganese in two crystal forms of glucose isomerase.
Acta Crystallogr. D Biol. Crystallogr. 59 2003 868-75
[PubMed: 12777803]
http://dx.doi.org/10.1107/S0907444903005663
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Katz AK, Li X, Carrell HL, Hanson BL, Langan P, Coates L, Schoenborn BP, Glusker JP, Bunick GJ.
Locating active-site hydrogen atoms in D-xylose isomerase: time-of-flight neutron diffraction.
Proc. Natl. Acad. Sci. U.S.A. 103 2006 8342-7
[PubMed: 16707576]
http://dx.doi.org/10.1073/pnas.0602598103
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Fenn TD, Ringe D, Petsko GA.
Xylose isomerase in substrate and inhibitor michaelis states: atomic resolution studies of a metal-mediated hydride shift.
Biochemistry 43 2004 6464-74
[PubMed: 15157080]
http://dx.doi.org/10.1021/bi049812o
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InterPro 23.1
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