SMART: Aldolase_II domain annotation

Aldolase_II Class II Aldolase and Adducin N-terminal domain

SMART accession number:	SM01007
Description:	This family includes class II aldolases and adducins which have not been ascribed any enzymatic function.
Interpro abstract (IPR001303):	This entry represents the alpha/beta/alpha domain found in class II aldolases and in adducin (usually at the N terminus of adducin). Proteins containing this domain include: rhamnulose-1-phosphate aldolase (EC 4.1.2.19), L-fuculose phosphate aldolase (EC 4.1.2.17) [(PUBMED:8515438), (PUBMED:8676381)] 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 and the metazoan adducins, which have not been ascribed any enzymatic function but which play a role in cell membrane cytoskeleton organisation [(PUBMED:1840603)].
GO function:	metal ion binding (GO:0046872)
Family alignment:	View or

There are 3346 Aldolase_II domains in 3336 proteins in SMART's nrdb database.

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Evolution (species in which this domain is found)
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This tree shows only several representative species. The complete taxonomic breakdown of all proteins with Aldolase_II domain is also avaliable.

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Go to specific node: Anopheles gambiae, Arabidopsis thaliana, Caenorhabditis elegans, Drosophila melanogaster, Homo sapiens, Mus musculus, Rattus norvegicus, Saccharomyces cerevisiae, Takifugu rubripes
Cellular role (predicted cellular role)
Cellular role: metabolism
Literature (relevant references for this domain)
Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Dreyer MK, Schulz GE
- Catalytic mechanism of the metal-dependent fuculose aldolase fromEscherichia coli as derived from the structure.
- J Mol Biol. 1996; 259: 458-66
- Display abstract
- The structure of L-fuculose-1-phosphate aldolase in a cubic crystal formhas been determined with and without the inhibitorphosphoglycolohydroxamate at 2.4 and 2.7 angstrom (1 angstrom = 0.1 nm)resolution, respectively. This inhibitor mimics the enediolate transitionstate of the substrate moiety dihydroxyacetone phosphate. The structuresshowed that dihydroxyacetone phosphate ligates the zinc ion of thismetal-dependent class II aldolase with its hydroxyl and keto oxygen atoms,shifting Glu73 away from the zinc coordination sphere to a non-polarenvironment. At this position Glu73 accepts a proton in the initialreaction step, producing the enediolate which is then stabilized by thezinc ion. The other substrate moiety L-lactaldehyde was modeled, becauseno binding structure is yet available.
- Dreyer MK, Schulz GE
- The spatial structure of the class II L-fuculose-1-phosphate aldolase fromEscherichia coli.
- J Mol Biol. 1993; 231: 549-53
- Display abstract
- The three-dimensional structure of L-fuculose-1-phosphate aldolase (FucA)from Escherichia coli was determined by X-ray crystallography at aresolution of 2.13 A. The enzyme is a homotetramer with an M(r) of 23,775per subunit. Since its activity depends on the presence of metal ions(Zn2+) the enzyme belongs to the class II aldolases. As expected fromamino acid sequence comparisons, this first structure of a class IIaldolase shows no similarity to the known structures of class I aldolases.It has some unusual features concerning the overall chain fold, thequaternary structure, and the co-ordination of the catalytically activezinc ion. A sequence comparison with the data bank indicated that themiddle domain of the enzyme L-ribulose-5-phosphate-4-epimerase ishomologous to FucA and may contain an active-center metal ion.
Structure (3D structures containing this domain)

3D Structures of Aldolase_II domains in PDB

PDB code	Main view	Title
1dzu		L-fuculose-1-phosphate aldolase from escherichia coli mutant t26a
1dzv		L-fuculose-1-phosphate aldolase from escherichia coli mutant y113f/y209f
1dzw		L-fuculose-1-phosphate aldolase from escherichia coli mutant f131a
1dzx		L-fuculose-1-phosphate aldolase from escherichia coli mutant r212a
1dzy		L-fuculose-1-phosphate aldolase from escherichia coli mutant e214a
1dzz		L-fuculose-1-phosphate aldolase from escherichia coli mutant y113f
1e46		L-fuculose 1-phosphate aldolase from escherichia coli mutant e73s
1e47		L-fuculose 1-phosphate aldolase from escherichia coli mutant e73q
1e48		L-fuculose 1-phosphate aldolase from escherichia coli mutant e73q/y113f/y209f
1e49		L-fuculose 1-phosphate aldolase from escherichia coli mutant n29l/s71a
1e4a		L-fuculose 1-phosphate aldolase from escherichia coli mutant del(27)
1e4b		L-fuculose 1-phosphate aldolase from escherichia coli mutant n29q
1e4c		L-fuculose 1-phosphate aldolase from escherichia coli mutant s71q
1fua		L-fuculose 1-phosphate aldolase crystal form t
1gt7		L-rhamnulose-1-phosphate aldolase from escherichia coli
1jdi		Crystal structure of l-ribulose-5-phosphate 4-epimerase
1k0w		Crystal structure of l-ribulose-5-phosphate 4-epimerase
1ojr		L-rhamnulose-1-phosphate aldolase from escherichia coli (mutant e192a)
1pvt		Crystal structure of sugar-phosphate aldolase from thermotoga maritima
2fk5		Crystal structure of l-fuculose-1-phosphate aldolase from thermus thermophilus hb8
2flf		Crystal structure of l-fuculose-1-phosphate aldolase from thermus thermophilus hb8
2fua		L-fuculose 1-phosphate aldolase crystal form t with cobalt
2irp		Crystal structure of the l-fuculose-1-phosphate aldolase (aq_1979) from aquifex aeolicus vf5
2opi		Crystal structure of l-fuculose-1-phosphate aldolase from bacteroides thetaiotaomicron
2uyu		L-rhamnulose-1-phosphate aldolase from escherichia coli ( mutant a88f-e192a)
2uyv		L-rhamnulose-1-phosphate aldolase from escherichia coli ( mutant q6y-e192a)
2v29		L-rhamnulose-1-phosphate aldolase from escherichia coli (mutant k15w)
2v2a		L-rhamnulose-1-phosphate aldolase from escherichia coli ( mutant e192a-k248g-r253a-e254a)
2v2b		L-rhamnulose-1-phosphate aldolase from escherichia coli ( mutant e117s-e192a-k248g-r253a-e254a)
2v9e		L-rhamnulose-1-phosphate aldolase from escherichia coli ( mutant e192a-k248w-a273s)
2v9f		L-rhamnulose-1-phosphate aldolase from escherichia coli ( mutant e192a-k248w-a273s)
2v9g		L-rhamnulose-1-phosphate aldolase from escherichia coli ( mutant q6y-l84w-e192a)
2v9i		L-rhamnulose-1-phosphate aldolase from escherichia coli ( mutant e192a-k248w-l274stop)
2v9l		L-rhamnulose-1-phosphate aldolase from escherichia coli ( mutant q6y-e192a)
2v9m		L-rhamnulose-1-phosphate aldolase from escherichia coli ( mutant a87m-t109f-e192a)
2v9n		L-rhamnulose-1-phosphate aldolase from escherichia coli ( mutant a88f-e192a)
2v9o		L-rhamnulose-1-phosphate aldolase from escherichia coli ( mutant a87m-t109f-e192a)
2z7b		Crystal structure of mesorhizobium loti 3-hydroxy-2- methylpyridine-4,5-dicarboxylate decarboxylase
3fua		L-fuculose-1-phosphate aldolase crystal form k
4fua		L-fuculose-1-phosphate aldolase complex with pgh

Links (links to other resources describing this domain)
PFAM Aldolase_II
INTERPRO IPR001303

PFAM	Aldolase_II
INTERPRO	IPR001303