SynDB Home Page
SynDB Home Page

blue bulletSynDB protein details  

Parse error: syntax error, unexpected T_VARIABLE in /home/kongl/syndb/www/sdb_nats.php on line 52
0THNSL_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
DescriptionThreonine synthase-like 1.
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Shikimate kinase () catalyzes the fifth step in the biosynthesis of aromatic amino acids from chorismate(the so-called shikimate pathway) . The enzyme catalyzes the following reaction:ATP + shikimate = ADP + shikimate-3-phosphateThe protein is found in bacteria (gene aroK or aroL).lants and fungi (whereit is part of a multifunctional enzyme that catalyses five consecutive steps in this pathway). In 1994.he 3Dstructure of shikimate kinase was predicted to be very close to that of adenylate kinase.uggesting a functionalsimilarity as well as an evolutionary relationship . This prediction has since been confirmedexperimentally. The protein is reported to possess an alpha/beta fold.onsisting of a central sheet of fiveparallel beta-strands flanked by alpha-helices. Such a topology is very similar to that of adenylate kinase.
  IPR000623:Shikimate kinase
Pyridoxal-5-phosphate-dependent enzymes (B6 enzymes) catalyze manifold reactions in the metabolism of amino acids. Most of these enzymes can be assigned to one of three different families of homologous proteins.he alpha.eta and gamma families. The alpha and gamma family might be distantly related with one another.ut are clearly not homologous with the beta family. The beta family includes L- and D-serine dehydratase.hreonine dehydratase.he beta subunit of tryptophan synthase.hreonine synthase and cysteine synthase. These enzymes catalyze beta-replacement or beta-elimination reactions .Comparison of sequences from eukaryotic.rchebacterial.nd eubacterial species indicates that the functional specialization of most B6 enzymes has occurred already in the universal ancestor cell. The cofactor pyridoxal-5-phosphate must have emerged very early in biological evolution; conceivably.rganic cofactors and metal ions were the first biological catalysts . The 3Dstructure of the beta-subunit of tryptophan synthase has been solved. Thesubunit has two domains that are approximately the same size and similar toeach other in folding pattern. Each has a core containing a four-strandedparallel beta-sheet with three helices on its inner side and one on the outerside. The cofactor is bound at the interface between the domains .
  IPR001926:Pyridoxal-5'-phosphate-dependent enzyme, beta subunit
Threonine synthase () is involved in threonine biosynthesis. It catalyses the conversion of O-phospho-L-homoserine and water into L-threonine and orthophosphate.sing pyridoxal phosphate as a cofactor. The pyridoxal-phosphate binding site is a Lys (K) residue. The enzyme is distantly related to the serine/threonine dehydratases which are also pyridoxal-phosphate dependent enzymes .
  IPR004450:Threonine synthase
SequencesProtein: THNSL_HUMAN (743 aa)
mRNA: NM_024838
Local Annotation
Synapse Ontology
transport of vesicles in the presynaptic neuron
sdb:0017 Mobilization: synapsins, CAM kinase I  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 12 residues, 25345592-25345627Exon2: 57 residues, 25350676-25350843Exon3: 784 residues, 25352110-25354458Exon4: 2 residues, -Jump to THNSL_HUMAN  
Tune and view alternative isoforms