| IED ID | IndEnz0002003971 |
| Enzyme Type ID | protease003971 |
| Protein Name |
Serine hydroxymethyltransferase 4 AtSHMT4 EC 2.1.2.1 Glycine hydroxymethyltransferase 4 Serine methylase 4 |
| Gene Name | SHM4 SHMT4 At4g13930 dl3005c FCAALL.160 |
| Organism | Arabidopsis thaliana (Mouse-ear cress) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids malvids Brassicales Brassicaceae Camelineae Arabidopsis Arabidopsis thaliana (Mouse-ear cress) |
| Enzyme Sequence | MEPVSSWGNTSLVSVDPEIHDLIEKEKRRQCRGIELIASENFTSFAVIEALGSALTNKYSEGIPGNRYYGGNEFIDEIENLCRSRALEAFHCDPAAWGVNVQPYSGSPANFAAYTALLQPHDRIMGLDLPSGGHLTHGYYTSGGKKISATSIYFESLPYKVNFTTGYIDYDKLEEKALDFRPKLLICGGSAYPRDWDYARFRAIADKVGALLLCDMAHISGLVAAQEAANPFEYCDVVTTTTHKSLRGPRAGMIFYRKGPKPPKKGQPEGAVYDFEDKINFAVFPALQGGPHNHQIGALAVALKQANTPGFKVYAKQVKANAVALGNYLMSKGYQIVTNGTENHLVLWDLRPLGLTGNKVEKLCDLCSITLNKNAVFGDSSALAPGGVRIGAPAMTSRGLVEKDFEQIGEFLSRAVTLTLDIQKTYGKLLKDFNKGLVNNKDLDQLKADVEKFSASYEMPGFLMSEMKYKD |
| Enzyme Length | 471 |
| Uniprot Accession Number | O23254 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by the antifolate drugs methotrexate and pemetrexed. {ECO:0000269|PubMed:31873125}. |
| Binding Site | BINDING 39; /note="L-serine"; /evidence="ECO:0000250|UniProtKB:Q94C74"; BINDING 39; /note="Pemetrexed"; /evidence="ECO:0000269|PubMed:31873125, ECO:0007744|PDB:6SMR"; BINDING 59; /note="Pemetrexed"; /evidence="ECO:0000269|PubMed:31873125, ECO:0007744|PDB:6SMR"; BINDING 61; /note="L-serine"; /evidence="ECO:0000250|UniProtKB:Q94C74"; BINDING 61; /note="Pemetrexed"; /evidence="ECO:0000269|PubMed:31873125, ECO:0007744|PDB:6SMR"; BINDING 69; /note="L-serine"; /evidence="ECO:0000250|UniProtKB:Q94C74"; BINDING 134; /note="Pemetrexed"; /evidence="ECO:0000269|PubMed:31873125, ECO:0007744|PDB:6SMR"; BINDING 190; /note="Pemetrexed"; /evidence="ECO:0000269|PubMed:31873125, ECO:0007744|PDB:6SMR"; BINDING 218; /note="L-serine"; /evidence="ECO:0000250|UniProtKB:Q94C74"; BINDING 218; /note="Pemetrexed"; /evidence="ECO:0000269|PubMed:31873125, ECO:0007744|PDB:6SMR"; BINDING 244; /note="L-serine"; /evidence="ECO:0000250|UniProtKB:Q94C74"; BINDING 290; /note="Pemetrexed; via amide nitrogen"; /evidence="ECO:0000269|PubMed:31873125, ECO:0007744|PDB:6SMR"; BINDING 373; /note="Methotrexate"; /evidence="ECO:0000269|PubMed:31873125, ECO:0007744|PDB:6SMR"; BINDING 389; /note="L-serine"; /evidence="ECO:0000250|UniProtKB:Q94C74"; BINDING 389; /note="Pemetrexed"; /evidence="ECO:0000269|PubMed:31873125, ECO:0007744|PDB:6SMR" |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine; Xref=Rhea:RHEA:15481, ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, ChEBI:CHEBI:33384, ChEBI:CHEBI:57305, ChEBI:CHEBI:57453; EC=2.1.2.1; Evidence={ECO:0000269|PubMed:31873125}; |
| DNA Binding | |
| EC Number | 2.1.2.1 |
| Enzyme Function | FUNCTION: Catalyzes the interconversion of serine and glycine with the conversion of tetrahydrofolate (THF) into 5,10-methylene-THF. {ECO:0000269|PubMed:31873125}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. {ECO:0000305}. |
| nucleotide Binding | |
| Features | Beta strand (15); Binding site (15); Chain (1); Helix (27); Modified residue (2); Region (1); Sequence conflict (4); Turn (3) |
| Keywords | 3D-structure;Acetylation;Cytoplasm;One-carbon metabolism;Pyridoxal phosphate;Reference proteome;Transferase |
| Interact With | Q9SB51 |
| Induction | INDUCTION: Circadian-regulation. {ECO:0000269|PubMed:10806255}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. |
| Modified Residue | MOD_RES 1; /note=N-acetylmethionine; /evidence=ECO:0007744|PubMed:22223895; MOD_RES 244; /note=N6-(pyridoxal phosphate)lysine; /evidence=ECO:0000250 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 6SMR; |
| Mapped Pubmed ID | 12644654; 15276459; 15911562; 15971193; 16242667; 16247729; 16307804; 16336779; 16502469; 16679420; 16798886; 16951055; 17227551; 17432890; 17644812; 18650403; 20118269; 21378116; 23281391; 23800877; 28627464; |
| Motif | |
| Gene Encoded By | |
| Mass | 51,718 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.56 mM for L-serine (at pH 6.5 and 30 degrees Celsius) {ECO:0000269|PubMed:31873125}; KM=0.54 mM for L-serine (at pH 7.0 and 30 degrees Celsius) {ECO:0000269|PubMed:31873125}; KM=0.30 mM for L-serine (at pH 8.0 and 30 degrees Celsius) {ECO:0000269|PubMed:31873125}; KM=0.24 mM for L-serine (at pH 8.5 and 30 degrees Celsius) {ECO:0000269|PubMed:31873125}; KM=0.20 mM for L-serine (at pH 9.5 and 30 degrees Celsius) {ECO:0000269|PubMed:31873125}; KM=7.87 uM for (6S)-5,6,7,8-tetrahydrofolate (at pH 6.5 and 30 degrees Celsius) {ECO:0000269|PubMed:31873125}; KM=14.97 uM for (6S)-5,6,7,8-tetrahydrofolate (at pH 7.0 and 30 degrees Celsius) {ECO:0000269|PubMed:31873125}; KM=23.83 uM for (6S)-5,6,7,8-tetrahydrofolate (at pH 8.0 and 30 degrees Celsius) {ECO:0000269|PubMed:31873125}; KM=33.75 uM for (6S)-5,6,7,8-tetrahydrofolate (at pH 8.5 and 30 degrees Celsius) {ECO:0000269|PubMed:31873125}; KM=49.24 uM for (6S)-5,6,7,8-tetrahydrofolate (at pH 9.5 and 30 degrees Celsius) {ECO:0000269|PubMed:31873125}; |
| Metal Binding | |
| Rhea ID | RHEA:15481 |
| Cross Reference Brenda |