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InterPro: IPR001303 Class II aldolase/adducin, N-terminal
Protein matches
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UniProtKB Matches: 3596 proteins |
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Accession
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IPR001303 Aldolase_II/adducin_N |
Type
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Domain |
Signatures
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InterPro Relationships
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Children
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IPR013447 Rhamnulose-1-phosphate aldolase
IPR017714 Methylthioribulose-1-phosphate dehydratase
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Found in
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IPR004661 L-ribulose-5-phosphate 4-epimerase
IPR004782 L-fucose phosphate aldolase
IPR013454 Bifunctional rhamnulose-1-phosphate aldolase/alcohol dehydrogenase
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GO Term annotation
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Function
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GO:0046872 metal ion binding
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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 alpha/beta/alpha domain found in class II aldolases and adducin, usually at the N terminus. These proteins form part of a family that includes: rhamnulose-1-phosphate aldolase (EC:4.1.2.19), L-fuculose phosphate aldolase (EC:4.1.2.17) [1, 2] that is involved in the third step in fucose metabolism, L-ribulose- 5-phosphate 4-epimerase (EC:5.1.3.4) involved in the third step of L-arabinose catabolism, a probable sugar isomerase SgbE, hypothetical proteins and the metazoan adducins which have not been ascribed any enzymatic function but which play a role in cell membrane cytoskeleton organisation.
Adducins are members of the Ig superfamily and encode cell surface sialoglycoproteins expressed by cytokine-activated endothelium. This type I membrane protein mediates leukocyte-endothelial cell adhesion and signal transduction, and may play a role in the development of artherosclerosis and rheumatoid arthritis. Adducin is a cell-membrane skeletal protein that was first purified from human erythrocytes and subsequently isolated from bovine brain membranes. Isoforms of this protein have been detected in lung, kidney, testes and liver. Erythrocyte adducin is a 200kDa heterodimer protein, composed of alpha and beta subunits, present at about 30,000 copies per cell. It binds with high affinity to Ca(2+)/calmodulin and is a substrate for protein kinases A and C. Both alpha-adducin and beta-adducin show alternative splicing. Thus, there may be several different heterodimeric or homodimeric forms of adducin, each with a different functional specificity. It is thought to play a role in assembly of the spectrin-actin lattice that underlies the plasma membrane [3]. Missense mutations in both the alpha- and beta-adducin genes that alter amino acids that are normally phosphorylated have been associated with the regulation of blood pressure in the Milan hypertensive strain (MHS) of rats. Gamma adducin was isolated from human foetal brain [4]. It shows a high degree of similarity to the alpha and beta adducins.
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Structural links
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Database links
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Publications
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1.
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Dreyer MK, Schulz GE.
The spatial structure of the class II L-fuculose-1-phosphate aldolase from Escherichia coli.
J. Mol. Biol. 231 549-53 1993
[PubMed: 8515438]
http://dx.doi.org/10.1006/jmbi.1993.1307
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2.
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Dreyer MK, Schulz GE.
Catalytic mechanism of the metal-dependent fuculose aldolase from Escherichia coli as derived from the structure.
J. Mol. Biol. 259 458-66 1996
[PubMed: 8676381]
http://dx.doi.org/10.1006/jmbi.1996.0332
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3.
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Rabinovich PM, Beburov MIu, Linevich ZK, Stepanov AI.
[Amplification of the riboflavin operon genes of Bacillus subtilis in Escherichia coli cells]
Genetika 14 1696-1705 1978
[PubMed: 102560]
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4.
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Katagiri T, Ozaki K, Fujiwara T, Shimizu F, Kawai A, Okuno S, Suzuki M, Nakamura Y, Takahashi E, Hirai Y.
Cloning, expression and chromosome mapping of adducin-like 70 (ADDL), a human cDNA highly homologous to human erythrocyte adducin.
Cytogenet. Cell Genet. 74 90-5 1996
[PubMed: 8893809]
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Additional Reading
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Grueninger D, Treiber N, Ziegler MO, Koetter JW, Schulze MS, Schulz GE.
Designed protein-protein association.
Science 319 2008 206-9
[PubMed: 18187656]
http://dx.doi.org/10.1126/science.1150421
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Grueninger D, Schulz GE.
Antenna domain mobility and enzymatic reaction of L-rhamnulose-1-phosphate aldolase.
Biochemistry 47 2008 607-14
[PubMed: 18085797]
http://dx.doi.org/10.1021/bi7012799
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Kroemer M, Schulz GE.
The structure of L-rhamnulose-1-phosphate aldolase (class II) solved by low-resolution SIR phasing and 20-fold NCS averaging.
Acta Crystallogr. D Biol. Crystallogr. 58 2002 824-32
[PubMed: 11976494]
http://dx.doi.org/10.1107/S0907444902004614
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Luo Y, Samuel J, Mosimann SC, Lee JE, Tanner ME, Strynadka NC.
The structure of L-ribulose-5-phosphate 4-epimerase: an aldolase-like platform for epimerization.
Biochemistry 40 2001 14763-71
[PubMed: 11732895]
http://dx.doi.org/10.1021/bi0112513
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Kroemer M, Merkel I, Schulz GE.
Structure and catalytic mechanism of L-rhamnulose-1-phosphate aldolase.
Biochemistry 42 2003 10560-8
[PubMed: 12962479]
http://dx.doi.org/10.1021/bi0349266
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InterPro 23.1
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