Enzymes
UniProtKB help_outline | 7 proteins |
Enzyme class help_outline |
|
GO Molecular Function help_outline |
|
Reaction participants Show >> << Hide
-
Namehelp_outline
trans-4-hydroxy-L-prolyl-[protein]
Identifier
RHEA-COMP:12408
Reactive part
help_outline
- Name help_outline trans-4-hydroxy-L-proline residue Identifier CHEBI:61965 Charge 0 Formula C5H7NO2 SMILEShelp_outline [C@H]1(C[C@@H](O)CN1*)C(*)=O 2D coordinates Mol file for the small molecule Search links Involved in 6 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline UDP-β-L-arabinofuranose Identifier CHEBI:61463 Charge -2 Formula C14H20N2O16P2 InChIKeyhelp_outline QGNZSCRNMXQWNR-IAZOVDBXSA-L SMILEShelp_outline OC[C@@H]1O[C@H](OP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)n2ccc(=O)[nH]c2=O)[C@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 3 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,431 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
-
Namehelp_outline
O-(β-L-arabinofuranosyl)-trans-4-hydroxy-L-prolyl-[protein]
Identifier
RHEA-COMP:12409
Reactive part
help_outline
- Name help_outline O-(β-L-arabinofuranosyl)-trans-4-hydroxy-L-proline residue Identifier CHEBI:131610 Charge 0 Formula C10H15NO6 SMILEShelp_outline [C@H]1(C[C@@H](O[C@H]2O[C@H]([C@@H]([C@H]2O)O)CO)CN1*)C(*)=O 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline UDP Identifier CHEBI:58223 Charge -3 Formula C9H11N2O12P2 InChIKeyhelp_outline XCCTYIAWTASOJW-XVFCMESISA-K SMILEShelp_outline O[C@@H]1[C@@H](COP([O-])(=O)OP([O-])([O-])=O)O[C@H]([C@@H]1O)n1ccc(=O)[nH]c1=O 2D coordinates Mol file for the small molecule Search links Involved in 576 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:49472 | RHEA:49473 | RHEA:49474 | RHEA:49475 | |
---|---|---|---|---|
Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
UniProtKB help_outline |
|
|||
EC numbers help_outline | ||||
Gene Ontology help_outline | ||||
MetaCyc help_outline |
Publications
-
Identification of three hydroxyproline O-arabinosyltransferases in Arabidopsis thaliana.
Ogawa-Ohnishi M., Matsushita W., Matsubayashi Y.
Hydroxyproline (Hyp) O-arabinosylation is a post-translational modification that is prominent in extracellular glycoproteins in plants. Hyp O-arabinosylation is generally found in these glycoproteins in the form of linear oligoarabinoside chains and has a key role in their function by contributing ... >> More
Hydroxyproline (Hyp) O-arabinosylation is a post-translational modification that is prominent in extracellular glycoproteins in plants. Hyp O-arabinosylation is generally found in these glycoproteins in the form of linear oligoarabinoside chains and has a key role in their function by contributing to conformational stability. However, Hyp O-arabinosyltransferase (HPAT), a key enzyme that catalyzes the transfer of the L-arabinose to the hydroxyl group of Hyp residues, has remained undiscovered. Here, we purified and identified Arabidopsis HPAT as a Golgi-localized transmembrane protein that is structurally similar to the glycosyltransferase GT8 family. Loss-of-function mutations in HPAT-encoding genes cause pleiotropic phenotypes that include enhanced hypocotyl elongation, defects in cell wall thickening, early flowering, early senescence and impaired pollen tube growth. Our results indicate essential roles of Hyp O-arabinosylation in both vegetative and reproductive growth in plants. << Less
-
Hydroxyproline O-arabinosyltransferase mutants oppositely alter tip growth in Arabidopsis thaliana and Physcomitrella patens.
MacAlister C.A., Ortiz-Ramirez C., Becker J.D., Feijo J.A., Lippman Z.B.
Hydroxyproline O-arabinosyltransferases (HPATs) are members of a small, deeply conserved family of plant-specific glycosyltransferases that add arabinose sugars to diverse proteins including cell wall-associated extensins and small signaling peptides. Recent genetic studies in flowering plants sug ... >> More
Hydroxyproline O-arabinosyltransferases (HPATs) are members of a small, deeply conserved family of plant-specific glycosyltransferases that add arabinose sugars to diverse proteins including cell wall-associated extensins and small signaling peptides. Recent genetic studies in flowering plants suggest that different HPAT homologs have been co-opted to function in diverse species-specific developmental contexts. However, nothing is known about the roles of HPATs in basal plants. We show that complete loss of HPAT function in Arabidopsis thaliana and the moss Physcomitrella patens results in a shared defect in gametophytic tip cell growth. Arabidopsis hpat1/2/3 triple knockout mutants suffer from a strong male sterility defect as a consequence of pollen tubes that fail to fully elongate following pollination. Knocking out the two HPAT genes of Physcomitrella results in larger multicellular filamentous networks due to increased elongation of protonemal tip cells. Physcomitrella hpat mutants lack cell-wall associated hydroxyproline arabinosides and can be rescued with exogenous cellulose, while global expression profiling shows that cell wall-associated genes are severely misexpressed, implicating a defect in cell wall formation during tip growth. Our findings point to a major role for HPATs in influencing cell elongation during tip growth in plants. << Less