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InterPro: IPR013785 Aldolase-type TIM barrel
Protein matches
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UniProtKB Matches: 79200 proteins |
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Accession
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IPR013785 Aldolase_TIM |
Type
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Domain |
Signatures
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InterPro Relationships
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Children
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IPR000262 FMN-dependent dehydrogenase
IPR000891 Pyruvate carboxyltransferase
IPR001093 IMP dehydrogenase/GMP reductase
IPR001155 NADH:flavin oxidoreductase/NADH oxidase, N-terminal
IPR001381 Dehydroquinase class I
IPR002220 Dihydrodipicolinate synthetase
IPR003733 Thiamine monophosphate synthase
IPR006218 DAHP synthetase I/KDSA
IPR008867 Thiazole biosynthesis
IPR011060 Ribulose-phosphate binding barrel
IPR013132 N-acetylneuraminic acid synthase, N-terminal
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Found in
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IPR000111 Glycoside hydrolase, clan GH-D
IPR000652 Triosephosphate isomerase
IPR000741 Fructose-bisphosphate aldolase, class-I
IPR000771 Ketose-bisphosphate aldolase, class-II
IPR000887 KDPG/KHG aldolase
IPR001269 tRNA-dihydrouridine synthase
IPR001329 Glycoside hydrolase, family 56, allergen Api/Dol m 2
IPR001439 Glycoside hydrolase, family 56, sperm surface protein PH20
IPR001585 Transaldolase
IPR001731 Tetrapyrrole biosynthesis, porphobilinogen synthase
IPR001968 Glycoside hydrolase, family 56
IPR002241 Glycoside hydrolase, family 27
IPR002252 Glycoside hydrolase, family 36
IPR002638 Quinolinate phosphoribosyl transferase
IPR002684 Biotin synthase
IPR002915 Deoxyribose-phosphate aldolase/phospho-2-dehydro-3-deoxyheptonate aldolase
IPR003698 Lipoate synthase
IPR003830 (2R)-phospho-3-sulpholactate synthase, ComA
IPR004136 2-nitropropane dioxygenase, NPD
IPR004393 Nicotinate-nucleotide pyrophosphorylase
IPR004569 Pyridoxal phosphate (active vitamin B6) biosynthesis PdxJ
IPR004652 tRNA-dihydrouridine synthase, TIM-barrel, NifR3
IPR004653 tRNA-dihydrouridine synthase, TIM-barrel, YjbN
IPR004730 Transaldolase AB
IPR004731 Transaldolase C
IPR004732 Transaldolase subfamily
IPR005244 FO synthase, subunit 2-like
IPR005263 Dihydrodipicolinate synthase subfamily
IPR005264 N-acetylneuraminate lyase
IPR005270 tRNA-dihydrouridine synthase, TIM-barrel, NifR3-related
IPR005839 Methylthiotransferase
IPR005840 Ribosomal protein S12 methylthiotransferase RimO
IPR005911 Conserved hypothetical protein CHP01212
IPR005927 Tagatose 1,6-diphosphate aldolase, Gram-positive
IPR005991 IMP dehydrogenase related 1
IPR006215 Glycoside hydrolase, melibiase
IPR006242 Putative molybdenum utilization protein ModD
IPR006411 Fructose-bisphosphate aldolase, class II, yeast/E. coli subtype
IPR006412 Fructose-bisphosphate aldolase, class II, Calvin cycle subtype
IPR006463 tRNA-i(6)A37 modification enzyme MiaB
IPR006466 MiaB-like tRNA modifying enzyme, archaeal-type
IPR006467 MiaB-like tRNA modifying enzyme
IPR010210 Predicted phospho-2-dehydro-3-deoxyheptonate aldolase
IPR011288 Class II aldolase, tagatose bisphosphate
IPR011289 Fructose-1,6-bisphosphate aldolase, class II
IPR011343 Deoxyribose-phosphate aldolase
IPR011772 Magnesium-protoporphyrin IX monomethyl ester anaerobic oxidative cyclase
IPR011861 Transaldolase, Staphylococcus
IPR012220 Glutamate synthase, eukaryotic
IPR012691 2,4-dihydroxyhept-2-ene-1,7-dioic acid aldolase variant
IPR012726 Thiazole biosynthesis ThiH
IPR013483 Molybdenum cofactor biosynthesis protein A
IPR013485 Molybdenum cofactor biosynthesis protein A, archaea
IPR014634 Transaldolase, bacterial/plant type
IPR014651 Uncharacterised conserved protein, 2xCBS, MJ1404 type
IPR016426 Uncharacterised conserved protein UCP004698, CBS domain pair, MJ0100
IPR016427 Uncharacterised conserved protein UCP004699, CBS/ParB-like domains
IPR016436 Uncharacterised conserved protein UCP005063, CBS domain pair, MJ1232
IPR016486 Uncharacterised conserved protein UCP006591, CBS domain pair, MJ1004
IPR016779 Radical SAM enzyme, bacteria, predicted
IPR017291 Aldolase, YihT
IPR017430 Glycoside hydrolase, family 56, Hyaluronidase
IPR017569 Enoyl-(acyl-carrier-protein) reductase II, putative
IPR017655 5-dehydro-4-deoxyglucarate dehydratase
IPR017834 Hopanoid biosynthesis associated radical SAM protein HpnJ
IPR018155 Hyaluronidase
IPR019939 FO synthase, subunit 1
IPR019940 Complex F420, CofH
IPR020007 N-acetylneuraminate synthase
IPR020030 Pseudaminic acid biosynthesis, PseI
IPR020050 FO synthase, subunit 2
IPR020868 Bifunctional enzyme fae/hps
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Contains
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IPR000385 MoaA/nifB/pqqE, iron-sulphur binding, conserved site
IPR001295 Dihydroorotate dehydrogenase, conserved site
IPR002034 Alpha-isopropylmalate/homocitrate synthase, conserved site
IPR002932 Glutamate synthase, central-C
IPR006638 Elongator protein 3/MiaB/NifB
IPR006982 Glutamate synthase, central-N
IPR010722 Biotin/thiamin synthesis-associated protein
IPR015875 IMP dehydrogenase / GMP reductase, conserved site
IPR018089 Orotidine 5'-phosphate decarboxylase, active site
IPR018204 Tryptophan synthase, alpha chain, active site
IPR018225 Transaldolase, active site
IPR018508 3-dehydroquinate dehydratase, active site
IPR018517 tRNA-dihydrouridine synthase, conserved site
IPR020612 Methylthiotransferase, conserved site
IPR020624 Dihydrodipicolinate synthetase, conserved site
IPR020625 Dihydrodipicolinate synthetase, active site
IPR020861 Triosephosphate isomerase, active site
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GO Term annotation
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Process
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GO:0008152 metabolic process
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Function
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GO:0003824 catalytic activity
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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 the TIM beta/alpha barrel found in aldolase and in related proteins. This TIM barrel usually covers the entire protein structure. Proteins containing this TIM barrel domain include class I aldolases, class I DAHP synthases, class II fructose-bisphosphate aldolases (FBP aldolases), and 5-aminolaevulinate dehydratase (a hybrid of classes I and II aldolases) [1, 2, 3].
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Structural links
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SCOP:
b.85.1.1
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c.1.1.1
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c.1.10.1
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c.1.10.2
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c.1.10.3
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c.1.10.4
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c.1.10.5
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c.1.10.6
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c.1.17.1
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c.1.2.1
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c.1.2.2
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c.1.2.3
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c.1.2.4
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c.1.24.1
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c.1.27.1
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c.1.28.1
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c.1.28.3
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c.1.3.1
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c.1.31.1
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c.1.4.1
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c.1.5.1
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c.1.8.1
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c.1.8.13
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c.1.8.9
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c.4.1.1
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d.153.1.1
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d.37.1.1
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Publications
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1.
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Pan H, Smith DL.
Quaternary structure of aldolase leads to differences in its folding and unfolding intermediates.
Biochemistry 42 5713-21 2003
[PubMed: 12741828]
http://dx.doi.org/10.1021/bi027388q
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2.
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Erskine PT, Senior N, Awan S, Lambert R, Lewis G, Tickle IJ, Sarwar M, Spencer P, Thomas P, Warren MJ, Shoolingin-Jordan PM, Wood SP, Cooper JB.
X-ray structure of 5-aminolaevulinate dehydratase, a hybrid aldolase.
Nat. Struct. Biol. 4 1025-31 1997
[PubMed: 9406553]
http://dx.doi.org/10.1038/nsb1297-1025
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3.
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Heine A, Luz JG, Wong CH, Wilson IA.
Analysis of the class I aldolase binding site architecture based on the crystal structure of 2-deoxyribose-5-phosphate aldolase at 0.99A resolution.
J. Mol. Biol. 343 1019-34 2004
[PubMed: 15476818]
http://dx.doi.org/10.1016/j.jmb.2004.08.066
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Additional Reading
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Arakaki TL, Buckner FS, Gillespie JR, Malmquist NA, Phillips MA, Kalyuzhniy O, Luft JR, Detitta GT, Verlinde CL, Van Voorhis WC, Hol WG, Merritt EA.
Characterization of Trypanosoma brucei dihydroorotate dehydrogenase as a possible drug target; structural, kinetic and RNAi studies.
Mol. Microbiol. 68 2008 37-50
[PubMed: 18312275]
http://dx.doi.org/10.1111/j.1365-2958.2008.06131.x
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Murray MS, Holmes RP, Lowther WT.
Active site and loop 4 movements within human glycolate oxidase: implications for substrate specificity and drug design.
Biochemistry 47 2008 2439-49
[PubMed: 18215067]
http://dx.doi.org/10.1021/bi701710r
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Bello AM, Poduch E, Liu Y, Wei L, Crandall I, Wang X, Dyanand C, Kain KC, Pai EF, Kotra LP.
Structure-activity relationships of C6-uridine derivatives targeting plasmodia orotidine monophosphate decarboxylase.
J. Med. Chem. 51 2008 439-48
[PubMed: 18189347]
http://dx.doi.org/10.1021/jm7010673
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Kona F, Tao P, Martin P, Xu X, Gatti DL.
Electronic structure of the metal center in the Cd(2+), Zn(2+), and Cu(2+) substituted forms of KDO8P synthase: implications for catalysis.
Biochemistry 48 2009 3610-30
[PubMed: 19228070]
http://dx.doi.org/10.1021/bi801955h
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Sukumar N, Dewanti A, Merli A, Rossi GL, Mitra B, Mathews FS.
Structures of the G81A mutant form of the active chimera of (S)-mandelate dehydrogenase and its complex with two of its substrates.
Acta Crystallogr. D Biol. Crystallogr. 65 2009 543-52
[PubMed: 19465768]
http://dx.doi.org/10.1107/S0907444909010270
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