{PDOC52061}
{PS52061; DAHPS_I}
{PS52062; DAHPS_II}
{BEGIN}
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* DAHPS class-I and -II core TIM-barrel domains profiles *
**********************************************************

Despite their  different  biosynthetic roles in microorganisms and plants, the
enzymes 3-deoxy-D-arabino-heptulosonate-7-phosphate  synthase  (DAHPS)  and 3-
deoxy-D-manno-octulosonate-8-phosphate synthase  (KDOPS)  possess  significant
mechanistic and structural similarities. DAHPS catalyzes the first step in the
biosynthesis of  the  aromatic amino acids as well as other aromatic compounds
of primary   and   secondary   metabolism,   the  aldol-like  condensation  of
phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) with the formation
of DAHP and phosphate. KDOPS catalyses the first step in the biosynthesis of a
variety of  cell  surface  components, an analogous condensation of PEP and D-
arabinose-5-phosphate (A5P),  which  is  one carbon atom longer than E4P, with
the formation  of KDOP and phosphate. DAHPS and KDOPS are unusual in that they
both cleave  the  C-O,  not the O-P, bond of PEP. Members of both enzymes were
divided into two distinct main families (defined as class-I and class-II). The
class-I family is found mostly in prokaryotic and archaeal organisms. However,
some eukaryotic   examples   have  been  identified,  e.g.,  in  Saccharomyces
cerevisiae and  Neurospora  crassa.  This type of DAHPS can be further divided
into subfamilies  Ialpha  and  Ibeta.  KDOPSs  have been assigned to the Ibeta
subfamily. The  class-II,  defined  as "plant-like" DAHPS, consists of enzymes
from higher  plants  together  with a group of microbial enzymes that function
mainly in pathways of secondary metabolism [1,2,3,4,5].

Although there  is  no  significant  sequence  similarity between the class-II
DAHPSs and  the  class-I DAHPSs and KDOPSs, they share a characteristic (beta/
alpha)8 TIM-barrel  fold  in  which  the  eight parallel beta-strands are each
followed by   alpha-helices,   and   similar  active  site  architecture  (see
<PDB:1OFQ>, <PDB:1ZCO>, <PDB:1D9E>) and <PDB:2B7O>) [1,2,3,4,5].

We developed  two  profiles  for the DAHPS core TIM-barrel domain, one for the
class-I and one for the class-II.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Last update: April 2025 / First entry.

[ 1] Shumilin I.A., Bauerle R., Wu J., Woodard R.W., Kretsinger R.H.
     "Crystal structure of the reaction complex of
     3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Thermotoga
     maritima  refines the catalytic mechanism and indicates a new
     mechanism of allosteric  regulation."
     J. Mol. Biol. 341:455-466(2004).
     PubMed=15276836; DOI=10.1016/j.jmb.2004.05.077
[ 2] Wagner T., Kretsinger R.H., Bauerle R., Tolbert W.D.
     "3-Deoxy-D-manno-octulosonate-8-phosphate synthase from Escherichia
     coli. Model of  binding of phosphoenolpyruvate and
     D-arabinose-5-phosphate."
     J. Mol. Biol. 301:233-238(2000).
     PubMed=10926505; DOI=10.1006/jmbi.2000.3956
[ 3] Wu J., Woodard R.W.
     "New insights into the evolutionary links relating to the
     3-deoxy-D-arabino-heptulosonate 7-phosphate synthase subfamilies."
     J. Biol. Chem. 281:4042-4048(2006).
     PubMed=16339761; DOI=10.1074/jbc.M512223200
[ 4] Bhattacharya S., Kumar P.
     "An insilico approach to structural elucidation of
     3-deoxy-D-arabino-heptulosonate  7-phosphate synthase from Arabidopsis
     thaliana: hints for herbicide design."
     Phytochemistry 73:7-14(2012).
     PubMed=22000723; DOI=10.1016/j.phytochem.2011.09.005
[ 5] Schofield L.R., Anderson B.F., Patchett M.L., Norris G.E.,
     Jameson G.B., Parker E.J.
     "Substrate ambiguity and crystal structure of Pyrococcus furiosus
     3-deoxy-D-arabino-heptulosonate-7-phosphate synthase: an ancestral
     3-deoxyald-2-ulosonate-phosphate synthase?"
     Biochemistry 44:11950-11962(2005).
     PubMed=16142893; DOI=10.1021/bi050577z

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