ID GLYA_ECOLI Reviewed; 417 AA. AC P0A825; P00477; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 27-MAR-2024, entry version 148. DE RecName: Full=Serine hydroxymethyltransferase {ECO:0000255|HAMAP-Rule:MF_00051, ECO:0000303|PubMed:6300791}; DE Short=SHMT {ECO:0000255|HAMAP-Rule:MF_00051, ECO:0000303|PubMed:6300791}; DE Short=Serine methylase {ECO:0000255|HAMAP-Rule:MF_00051}; DE EC=2.1.2.1 {ECO:0000255|HAMAP-Rule:MF_00051, ECO:0000269|PubMed:10858298, ECO:0000269|PubMed:12773539, ECO:0000269|PubMed:1517215, ECO:0000269|PubMed:19883126, ECO:0000269|PubMed:7925461}; GN Name=glyA {ECO:0000255|HAMAP-Rule:MF_00051, GN ECO:0000303|PubMed:6300791}; OrderedLocusNames=b2551, JW2535; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=K12; RX PubMed=6300791; DOI=10.1093/nar/11.7.2065; RA Plamann M.D., Stauffer L.T., Urbanowski M.L., Stauffer G.V.; RT "Complete nucleotide sequence of the E. coli glyA gene."; RL Nucleic Acids Res. 11:2065-2075(1983). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=9205837; DOI=10.1093/dnares/4.2.91; RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S., RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.; RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of RT its sequence features."; RL DNA Res. 4:91-113(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [5] RP PROTEIN SEQUENCE OF 1-19. RC STRAIN=K12 / EMG2; RX PubMed=9298646; DOI=10.1002/elps.1150180807; RA Link A.J., Robison K., Church G.M.; RT "Comparing the predicted and observed properties of proteins encoded in the RT genome of Escherichia coli K-12."; RL Electrophoresis 18:1259-1313(1997). RN [6] RP PROTEIN SEQUENCE OF 1-17. RC STRAIN=K12; RX PubMed=2034230; DOI=10.1007/bf00273586; RA Vasudevan S.G., Armarego W.L.F., Shaw D.C., Lilley P.E., Dixon N.E., RA Poole R.K.; RT "Isolation and nucleotide sequence of the hmp gene that encodes a RT haemoglobin-like protein in Escherichia coli K-12."; RL Mol. Gen. Genet. 226:49-58(1991). RN [7] RP PROTEIN SEQUENCE OF 1-11. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RA Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J., Frutiger S., RA Paquet N., Wilkins M., Appel R.D., Bairoch A., Hochstrasser D.F.; RL Submitted (SEP-1994) to UniProtKB. RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7. RX PubMed=6190704; DOI=10.1016/0378-1119(83)90059-8; RA Plamann M.D., Stauffer G.V.; RT "Characterization of the Escherichia coli gene for serine RT hydroxymethyltransferase."; RL Gene 22:9-18(1983). RN [9] RP PROTEIN SEQUENCE OF 1-3 AND 415-417, FUNCTION, CATALYTIC ACTIVITY, RP COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT. RX PubMed=3891721; DOI=10.1128/jb.163.1.1-7.1985; RA Schirch V., Hopkins S., Villar E., Angelaccio S.; RT "Serine hydroxymethyltransferase from Escherichia coli: purification and RT properties."; RL J. Bacteriol. 163:1-7(1985). RN [10] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=2201683; DOI=10.1016/s0021-9258(18)77290-6; RA Stover P., Schirch V.; RT "Serine hydroxymethyltransferase catalyzes the hydrolysis of 5,10- RT methenyltetrahydrofolate to 5-formyltetrahydrofolate."; RL J. Biol. Chem. 265:14227-14233(1990). RN [11] RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND RP MUTAGENESIS OF HIS-228. RX PubMed=1517215; DOI=10.1016/s0021-9258(19)37096-6; RA Stover P., Zamora M., Shostak K., Gautam-Basak M., Schirch V.; RT "Escherichia coli serine hydroxymethyltransferase. The role of histidine RT 228 in determining reaction specificity."; RL J. Biol. Chem. 267:17679-17687(1992). RN [12] RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ARG-363 AND ARG-372. RX PubMed=7925461; DOI=10.1111/j.1432-1033.1994.00395.x; RA Delle Fratte S., Iurescia S., Angelaccio S., Bossa F., Schirch V.; RT "The function of arginine 363 as the substrate carboxyl-binding site in RT Escherichia coli serine hydroxymethyltransferase."; RL Eur. J. Biochem. 225:395-401(1994). RN [13] RP IDENTIFICATION BY 2D-GEL. RX PubMed=9298644; DOI=10.1002/elps.1150180805; RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.; RT "Escherichia coli proteome analysis using the gene-protein database."; RL Electrophoresis 18:1243-1251(1997). RN [14] RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF RP PRO-214; PRO-216; PRO-218; PRO-258 AND PRO-264. RX PubMed=12773539; DOI=10.1074/jbc.m303779200; RA Fu T.F., Boja E.S., Safo M.K., Schirch V.; RT "Role of proline residues in the folding of serine RT hydroxymethyltransferase."; RL J. Biol. Chem. 278:31088-31094(2003). RN [15] RP INDUCTION. RX PubMed=12624214; DOI=10.1099/mic.0.25841-0; RA Chirwa N.T., Herrington M.B.; RT "CsgD, a regulator of curli and cellulose synthesis, also regulates serine RT hydroxymethyltransferase synthesis in Escherichia coli K-12."; RL Microbiology 149:525-535(2003). RN [16] RP COFACTOR, AND REACTION MECHANISM. RX PubMed=17341210; DOI=10.1042/bj20061681; RA Malerba F., Bellelli A., Giorgi A., Bossa F., Contestabile R.; RT "The mechanism of addition of pyridoxal 5'-phosphate to Escherichia coli RT apo-serine hydroxymethyltransferase."; RL Biochem. J. 404:477-485(2007). RN [17] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-54; LYS-250; LYS-285; LYS-354 AND RP LYS-375, AND IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076; RX PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200; RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., RA Grishin N.V., Zhao Y.; RT "Lysine acetylation is a highly abundant and evolutionarily conserved RT modification in Escherichia coli."; RL Mol. Cell. Proteomics 8:215-225(2009). RN [18] RP MUTAGENESIS OF LEU-85 AND LEU-276, AND SUBUNIT. RX PubMed=19019081; DOI=10.1111/j.1742-4658.2008.06761.x; RA Florio R., Chiaraluce R., Consalvi V., Paiardini A., Catacchio B., RA Bossa F., Contestabile R.; RT "The role of evolutionarily conserved hydrophobic contacts in the RT quaternary structure stability of Escherichia coli serine RT hydroxymethyltransferase."; RL FEBS J. 276:132-143(2009). RN [19] RP SUCCINYLATION AT LYS-62; LYS-242; LYS-250; LYS-277; LYS-293; LYS-331; RP LYS-346 AND LYS-354. RC STRAIN=K12; RX PubMed=21151122; DOI=10.1038/nchembio.495; RA Zhang Z., Tan M., Xie Z., Dai L., Chen Y., Zhao Y.; RT "Identification of lysine succinylation as a new post-translational RT modification."; RL Nat. Chem. Biol. 7:58-63(2011). RN [20] {ECO:0007744|PDB:1EQB} RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF MUTANT PHE-65 IN COMPLEX WITH RP PYRIDOXYL-GLYCINE-PHOSPHATE AND 5-FORMYLTETRAHYDROFOLATE, FUNCTION, RP CATALYTIC ACTIVITY, COFACTOR, AND MUTAGENESIS OF TYR-65. RX PubMed=10858298; DOI=10.1021/bi000032z; RA Contestabile R., Angelaccio S., Bossa F., Wright H.T., Scarsdale N., RA Kazanina G., Schirch V.; RT "Role of tyrosine 65 in the mechanism of serine hydroxymethyltransferase."; RL Biochemistry 39:7492-7500(2000). RN [21] {ECO:0007744|PDB:1DFO} RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH RP PYRIDOXYL-GLYCINE-PHOSPHATE AND 5-FORMYLTETRAHYDROFOLATE, AND SUBUNIT. RX PubMed=10656824; DOI=10.1006/jmbi.1999.3453; RA Scarsdale J.N., Radaev S., Kazanina G., Schirch V., Wright H.T.; RT "Crystal structure at 2.4-A resolution of E. coli serine RT hydroxymethyltransferase in complex with glycine substrate and 5-formyl RT tetrahydrofolate."; RL J. Mol. Biol. 296:155-168(2000). RN [22] {ECO:0007744|PDB:3G8M} RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF MUTANT PHE-55 IN COMPLEX WITH RP PYRIDOXAL PHOSPHATE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF TYR-55 AND ARG-235. RX PubMed=19883126; DOI=10.1021/bi901568b; RA Vivoli M., Angelucci F., Ilari A., Morea V., Angelaccio S., di Salvo M.L., RA Contestabile R.; RT "Role of a conserved active site cation-pi interaction in Escherichia coli RT serine hydroxymethyltransferase."; RL Biochemistry 48:12034-12046(2009). CC -!- FUNCTION: Catalyzes the reversible interconversion of serine and CC glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. CC This reaction serves as the major source of one-carbon groups required CC for the biosynthesis of purines, thymidylate, methionine, and other CC important biomolecules (PubMed:3891721, PubMed:1517215, PubMed:7925461, CC PubMed:10858298, PubMed:19883126). Also exhibits THF-independent CC aldolase activity toward beta-hydroxyamino acids, producing glycine and CC aldehydes, via a retro-aldol mechanism. Thus, is able to catalyze the CC cleavage of allothreonine and 3-phenylserine (PubMed:3891721, CC PubMed:1517215, PubMed:10858298, PubMed:19883126). Also catalyzes the CC irreversible conversion of 5,10-methenyltetrahydrofolate to 5- CC formyltetrahydrofolate (PubMed:2201683, PubMed:10858298). CC {ECO:0000269|PubMed:10858298, ECO:0000269|PubMed:1517215, CC ECO:0000269|PubMed:19883126, ECO:0000269|PubMed:2201683, CC ECO:0000269|PubMed:3891721, ECO:0000269|PubMed:7925461}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = CC (6S)-5,6,7,8-tetrahydrofolate + L-serine; Xref=Rhea:RHEA:15481, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, ChEBI:CHEBI:33384, CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57453; EC=2.1.2.1; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00051, CC ECO:0000269|PubMed:10858298, ECO:0000269|PubMed:12773539, CC ECO:0000269|PubMed:1517215, ECO:0000269|PubMed:19883126, CC ECO:0000269|PubMed:3891721, ECO:0000269|PubMed:7925461}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-allo-threonine = acetaldehyde + glycine; CC Xref=Rhea:RHEA:26209, ChEBI:CHEBI:15343, ChEBI:CHEBI:57305, CC ChEBI:CHEBI:58585; Evidence={ECO:0000269|PubMed:10858298, CC ECO:0000269|PubMed:1517215, ECO:0000269|PubMed:19883126, CC ECO:0000269|PubMed:3891721}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(6R)-5,10-methenyltetrahydrofolate + H2O = (6S)-5- CC formyl-5,6,7,8-tetrahydrofolate + H(+); Xref=Rhea:RHEA:34767, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57455, CC ChEBI:CHEBI:57457; Evidence={ECO:0000269|PubMed:10858298, CC ECO:0000269|PubMed:2201683}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00051, CC ECO:0000269|PubMed:10858298, ECO:0000269|PubMed:1517215, CC ECO:0000269|PubMed:17341210, ECO:0000269|PubMed:19883126, CC ECO:0000269|PubMed:3891721}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=800 uM for L-serine {ECO:0000269|PubMed:3891721}; CC KM=140 uM for serine {ECO:0000269|PubMed:19883126}; CC KM=300 uM for serine {ECO:0000269|PubMed:12773539, CC ECO:0000269|PubMed:1517215}; CC KM=80 uM for tetrahydrofolate {ECO:0000269|PubMed:3891721}; CC KM=7 uM for tetrahydrofolate {ECO:0000269|PubMed:19883126}; CC KM=15 uM for tetrahydrofolate {ECO:0000269|PubMed:12773539}; CC KM=1500 uM for L-allothreonine {ECO:0000269|PubMed:19883126, CC ECO:0000269|PubMed:3891721}; CC KM=1000 uM for L-allothreonine {ECO:0000269|PubMed:1517215}; CC Note=kcat is 10.7 sec(-1) with L-serine as substrate. kcat is 0.5 CC sec(-1) with L-allothreonine as substrate. CC {ECO:0000269|PubMed:1517215}; CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. CC {ECO:0000255|HAMAP-Rule:MF_00051}. CC -!- PATHWAY: Amino-acid biosynthesis; glycine biosynthesis; glycine from L- CC serine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00051, ECO:0000305}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00051, CC ECO:0000269|PubMed:10656824, ECO:0000269|PubMed:10858298, CC ECO:0000269|PubMed:19019081, ECO:0000269|PubMed:19883126, CC ECO:0000269|PubMed:3891721}. CC -!- INTERACTION: CC P0A825; P0A825: glyA; NbExp=5; IntAct=EBI-909080, EBI-909080; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00051, CC ECO:0000305}. CC -!- INDUCTION: By CsgD. {ECO:0000269|PubMed:12624214}. CC -!- SIMILARITY: Belongs to the SHMT family. {ECO:0000255|HAMAP- CC Rule:MF_00051, ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; V00283; CAA23547.1; -; Genomic_DNA. DR EMBL; U00096; AAC75604.1; -; Genomic_DNA. DR EMBL; AP009048; BAA16459.1; -; Genomic_DNA. DR EMBL; J01620; AAA23912.1; -; Genomic_DNA. DR PIR; A00559; XYECS. DR RefSeq; NP_417046.1; NC_000913.3. DR RefSeq; WP_000919159.1; NZ_STEB01000011.1. DR PDB; 1DFO; X-ray; 2.40 A; A/B/C/D=1-417. DR PDB; 1EQB; X-ray; 2.70 A; A/B/C/D=1-417. DR PDB; 3G8M; X-ray; 3.30 A; A=1-417. DR PDBsum; 1DFO; -. DR PDBsum; 1EQB; -. DR PDBsum; 3G8M; -. DR AlphaFoldDB; P0A825; -. DR SMR; P0A825; -. DR BioGRID; 4261314; 221. DR DIP; DIP-36205N; -. DR IntAct; P0A825; 8. DR MINT; P0A825; -. DR STRING; 511145.b2551; -. DR iPTMnet; P0A825; -. DR jPOST; P0A825; -. DR PaxDb; 511145-b2551; -. DR EnsemblBacteria; AAC75604; AAC75604; b2551. DR GeneID; 83579904; -. DR GeneID; 947022; -. DR KEGG; ecj:JW2535; -. DR KEGG; eco:b2551; -. DR PATRIC; fig|1411691.4.peg.4183; -. DR EchoBASE; EB0403; -. DR eggNOG; COG0112; Bacteria. DR HOGENOM; CLU_022477_2_1_6; -. DR InParanoid; P0A825; -. DR OMA; CQFANVQ; -. DR OrthoDB; 9803846at2; -. DR PhylomeDB; P0A825; -. DR BioCyc; EcoCyc:GLYOHMETRANS-MONOMER; -. DR BioCyc; MetaCyc:GLYOHMETRANS-MONOMER; -. DR BRENDA; 2.1.2.1; 2026. DR BRENDA; 4.1.2.48; 2026. DR SABIO-RK; P0A825; -. DR UniPathway; UPA00193; -. DR UniPathway; UPA00288; UER01023. DR EvolutionaryTrace; P0A825; -. DR PRO; PR:P0A825; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IDA:EcoCyc. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IDA:EcoCyc. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0008732; F:L-allo-threonine aldolase activity; IEA:RHEA. DR GO; GO:0042803; F:protein homodimerization activity; IDA:EcoCyc. DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:EcoCyc. DR GO; GO:0070905; F:serine binding; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IDA:EcoliWiki. DR GO; GO:0046655; P:folic acid metabolic process; IBA:GO_Central. DR GO; GO:0019264; P:glycine biosynthetic process from serine; IDA:EcoCyc. DR GO; GO:0006546; P:glycine catabolic process; IMP:EcoCyc. DR GO; GO:0006564; P:L-serine biosynthetic process; IGI:EcoliWiki. DR GO; GO:0006565; P:L-serine catabolic process; IDA:EcoCyc. DR GO; GO:0006730; P:one-carbon metabolic process; IBA:GO_Central. DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway. DR GO; GO:0046653; P:tetrahydrofolate metabolic process; IBA:GO_Central. DR CDD; cd00378; SHMT; 1. DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1. DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1. DR HAMAP; MF_00051; SHMT; 1. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small. DR InterPro; IPR001085; Ser_HO-MeTrfase. DR InterPro; IPR019798; Ser_HO-MeTrfase_PLP_BS. DR InterPro; IPR039429; SHMT-like_dom. DR PANTHER; PTHR11680; SERINE HYDROXYMETHYLTRANSFERASE; 1. DR PANTHER; PTHR11680:SF50; SERINE HYDROXYMETHYLTRANSFERASE; 1. DR Pfam; PF00464; SHMT; 1. DR PIRSF; PIRSF000412; SHMT; 1. DR SUPFAM; SSF53383; PLP-dependent transferases; 1. DR PROSITE; PS00096; SHMT; 1. DR SWISS-2DPAGE; P0A825; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Amino-acid biosynthesis; Cytoplasm; KW Direct protein sequencing; One-carbon metabolism; Pyridoxal phosphate; KW Reference proteome; Transferase. FT CHAIN 1..417 FT /note="Serine hydroxymethyltransferase" FT /id="PRO_0000113573" FT BINDING 35 FT /ligand="glycine" FT /ligand_id="ChEBI:CHEBI:57305" FT /evidence="ECO:0000305|PubMed:10656824, FT ECO:0000305|PubMed:10858298, ECO:0007744|PDB:1DFO, FT ECO:0007744|PDB:1EQB" FT BINDING 55 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000305|PubMed:10656824, FT ECO:0000305|PubMed:10858298, ECO:0007744|PDB:1DFO, FT ECO:0007744|PDB:1EQB" FT BINDING 65 FT /ligand="glycine" FT /ligand_id="ChEBI:CHEBI:57305" FT /evidence="ECO:0000305|PubMed:10656824, FT ECO:0007744|PDB:1DFO" FT BINDING 99 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000305|PubMed:10656824, FT ECO:0000305|PubMed:10858298, ECO:0007744|PDB:1DFO, FT ECO:0007744|PDB:1EQB" FT BINDING 121 FT /ligand="(6S)-5,6,7,8-tetrahydrofolate" FT /ligand_id="ChEBI:CHEBI:57453" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051, FT ECO:0000305|PubMed:10656824, ECO:0000305|PubMed:10858298, FT ECO:0007744|PDB:1DFO, ECO:0007744|PDB:1EQB" FT BINDING 125..127 FT /ligand="(6S)-5,6,7,8-tetrahydrofolate" FT /ligand_id="ChEBI:CHEBI:57453" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051, FT ECO:0000305|PubMed:10656824, ECO:0000305|PubMed:10858298, FT ECO:0007744|PDB:1DFO, ECO:0007744|PDB:1EQB" FT BINDING 175 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000305|PubMed:10656824, FT ECO:0000305|PubMed:10858298, ECO:0007744|PDB:1DFO, FT ECO:0007744|PDB:1EQB" FT BINDING 203 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000305|PubMed:10656824, FT ECO:0000305|PubMed:10858298, ECO:0007744|PDB:1DFO, FT ECO:0007744|PDB:1EQB" FT BINDING 228 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000269|PubMed:19883126, FT ECO:0007744|PDB:3G8M" FT BINDING 235 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000269|PubMed:19883126, FT ECO:0007744|PDB:3G8M" FT BINDING 246 FT /ligand="(6S)-5,6,7,8-tetrahydrofolate" FT /ligand_id="ChEBI:CHEBI:57453" FT /evidence="ECO:0000305|PubMed:10656824, FT ECO:0000305|PubMed:10858298, ECO:0007744|PDB:1DFO, FT ECO:0007744|PDB:1EQB" FT BINDING 263 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000305|PubMed:10656824, FT ECO:0000305|PubMed:10858298, ECO:0007744|PDB:1DFO, FT ECO:0007744|PDB:1EQB" FT BINDING 355..357 FT /ligand="(6S)-5,6,7,8-tetrahydrofolate" FT /ligand_id="ChEBI:CHEBI:57453" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051, FT ECO:0000305|PubMed:10656824, ECO:0000305|PubMed:10858298, FT ECO:0007744|PDB:1DFO, ECO:0007744|PDB:1EQB" FT BINDING 363 FT /ligand="glycine" FT /ligand_id="ChEBI:CHEBI:57305" FT /evidence="ECO:0000305|PubMed:10656824, FT ECO:0000305|PubMed:10858298, ECO:0007744|PDB:1DFO, FT ECO:0007744|PDB:1EQB" FT SITE 55 FT /note="Transaldimination and stability" FT SITE 228 FT /note="Plays an important role in substrate specificity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051, FT ECO:0000269|PubMed:1517215" FT SITE 235 FT /note="Transaldimination and stability" FT MOD_RES 54 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:18723842" FT MOD_RES 62 FT /note="N6-succinyllysine" FT /evidence="ECO:0000269|PubMed:21151122" FT MOD_RES 229 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051, FT ECO:0000269|PubMed:19883126, ECO:0007744|PDB:3G8M" FT MOD_RES 242 FT /note="N6-succinyllysine" FT /evidence="ECO:0000269|PubMed:21151122" FT MOD_RES 250 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000269|PubMed:18723842" FT MOD_RES 250 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000269|PubMed:21151122" FT MOD_RES 277 FT /note="N6-succinyllysine" FT /evidence="ECO:0000269|PubMed:21151122" FT MOD_RES 285 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:18723842" FT MOD_RES 293 FT /note="N6-succinyllysine" FT /evidence="ECO:0000269|PubMed:21151122" FT MOD_RES 331 FT /note="N6-succinyllysine" FT /evidence="ECO:0000269|PubMed:21151122" FT MOD_RES 346 FT /note="N6-succinyllysine" FT /evidence="ECO:0000269|PubMed:21151122" FT MOD_RES 354 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000269|PubMed:18723842" FT MOD_RES 354 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000269|PubMed:21151122" FT MOD_RES 375 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:18723842" FT MUTAGEN 55 FT /note="Y->F: 50 and 15-fold increase in the affinity for FT serine and tetrahydrofolate, respectively, and 4-fold FT decrease in the catalytic efficiency." FT /evidence="ECO:0000269|PubMed:19883126" FT MUTAGEN 65 FT /note="Y->F: Decrease in catalytic activity." FT /evidence="ECO:0000269|PubMed:10858298" FT MUTAGEN 85 FT /note="L->A: Alteration of the dimer-monomer equilibrium FT accompanied by minor changes in the catalytic properties FT and whitout any significant change of tertiary structure. FT In the monomeric state; when associated with A-276." FT /evidence="ECO:0000269|PubMed:19019081" FT MUTAGEN 214 FT /note="P->A: No significant difference in catalytic FT efficiency and affinity compared to the wild-type." FT /evidence="ECO:0000269|PubMed:12773539" FT MUTAGEN 214 FT /note="P->G: No significant difference in catalytic FT efficiency and affinity compared to the wild-type." FT /evidence="ECO:0000269|PubMed:12773539" FT MUTAGEN 216 FT /note="P->A: No significant difference in catalytic FT efficiency and affinity compared to the wild-type. FT Alteration in the folding rate." FT /evidence="ECO:0000269|PubMed:12773539" FT MUTAGEN 216 FT /note="P->G: Important decrease in affinity and catalytic FT efficiency. Severely compromised in folding into a FT catalytically competent enzyme." FT /evidence="ECO:0000269|PubMed:12773539" FT MUTAGEN 218 FT /note="P->A: No significant difference in catalytic FT efficiency and affinity compared to the wild-type." FT /evidence="ECO:0000269|PubMed:12773539" FT MUTAGEN 218 FT /note="P->G: No significant difference in catalytic FT efficiency and affinity compared to the wild-type." FT /evidence="ECO:0000269|PubMed:12773539" FT MUTAGEN 228 FT /note="H->D,N: Utilize substrates and substrate analogs FT more effectively for a variety of alternate FT non-physiological reactions." FT /evidence="ECO:0000269|PubMed:1517215" FT MUTAGEN 235 FT /note="R->K: 1500- and 20-fold increase in the affinity for FT serine and tetrahydrofolate, respectively, and 15-fold FT decrease in the catalytic efficiency." FT /evidence="ECO:0000269|PubMed:19883126" FT MUTAGEN 235 FT /note="R->L: 450- and 11-fold increase in the affinity for FT serine and tetrahydrofolate, respectively, and 60-fold FT decrease in the catalytic efficiency." FT /evidence="ECO:0000269|PubMed:19883126" FT MUTAGEN 235 FT /note="R->Q: 900- and 17-fold increase in the affinity for FT serine and tetrahydrofolate, respectively, and 30-fold FT decrease in the catalytic efficiency." FT /evidence="ECO:0000269|PubMed:19883126" FT MUTAGEN 258 FT /note="P->A: Important decrease in affinity and catalytic FT efficiency. Reduced thermal stability." FT /evidence="ECO:0000269|PubMed:12773539" FT MUTAGEN 258 FT /note="P->G: Important decrease in affinity and catalytic FT efficiency." FT /evidence="ECO:0000269|PubMed:12773539" FT MUTAGEN 264 FT /note="P->A: Important decrease in affinity and catalytic FT efficiency." FT /evidence="ECO:0000269|PubMed:12773539" FT MUTAGEN 264 FT /note="P->G: Important decrease in affinity and catalytic FT efficiency." FT /evidence="ECO:0000269|PubMed:12773539" FT MUTAGEN 276 FT /note="L->A: Alteration of the dimer-monomer equilibrium FT accompanied by minor changes in the catalytic properties FT and whitout any significant change of tertiary structure. FT In the monomeric state; when associated with A-85." FT /evidence="ECO:0000269|PubMed:19019081" FT MUTAGEN 363 FT /note="R->A: It does not bind serine and glycine and shows FT no activity with serine as the substrate." FT /evidence="ECO:0000269|PubMed:7925461" FT MUTAGEN 363 FT /note="R->K: Exhibits only 0.03% of the catalytic activity FT of the wild-type and a 15-fold reduction in affinity for FT glycine and serine." FT /evidence="ECO:0000269|PubMed:7925461" FT MUTAGEN 372 FT /note="R->A: No significant difference compared to the FT wild-type." FT /evidence="ECO:0000269|PubMed:7925461" FT MUTAGEN 372 FT /note="R->K: No significant difference compared to the FT wild-type." FT /evidence="ECO:0000269|PubMed:7925461" FT HELIX 8..11 FT /evidence="ECO:0007829|PDB:1DFO" FT HELIX 13..28 FT /evidence="ECO:0007829|PDB:1DFO" FT STRAND 29..31 FT /evidence="ECO:0007829|PDB:1DFO" FT HELIX 41..47 FT /evidence="ECO:0007829|PDB:1DFO" FT HELIX 50..53 FT /evidence="ECO:0007829|PDB:1DFO" FT STRAND 62..66 FT /evidence="ECO:0007829|PDB:1DFO" FT HELIX 69..86 FT /evidence="ECO:0007829|PDB:1DFO" FT STRAND 89..92 FT /evidence="ECO:0007829|PDB:1DFO" FT HELIX 98..109 FT /evidence="ECO:0007829|PDB:1DFO" FT STRAND 115..119 FT /evidence="ECO:0007829|PDB:1DFO" FT TURN 121..124 FT /evidence="ECO:0007829|PDB:1DFO" FT HELIX 127..129 FT /evidence="ECO:0007829|PDB:1DFO" FT HELIX 135..139 FT /evidence="ECO:0007829|PDB:1DFO" FT STRAND 140..145 FT /evidence="ECO:0007829|PDB:1DFO" FT STRAND 149..152 FT /evidence="ECO:0007829|PDB:1DFO" FT HELIX 155..165 FT /evidence="ECO:0007829|PDB:1DFO" FT STRAND 168..173 FT /evidence="ECO:0007829|PDB:1DFO" FT HELIX 183..192 FT /evidence="ECO:0007829|PDB:1DFO" FT STRAND 196..200 FT /evidence="ECO:0007829|PDB:1DFO" FT TURN 202..204 FT /evidence="ECO:0007829|PDB:1DFO" FT HELIX 205..209 FT /evidence="ECO:0007829|PDB:1DFO" FT TURN 217..219 FT /evidence="ECO:0007829|PDB:1DFO" FT STRAND 220..229 FT /evidence="ECO:0007829|PDB:1DFO" FT STRAND 237..243 FT /evidence="ECO:0007829|PDB:1DFO" FT HELIX 246..256 FT /evidence="ECO:0007829|PDB:1DFO" FT TURN 257..260 FT /evidence="ECO:0007829|PDB:1DFO" FT HELIX 266..278 FT /evidence="ECO:0007829|PDB:1DFO" FT HELIX 282..304 FT /evidence="ECO:0007829|PDB:1DFO" FT HELIX 310..312 FT /evidence="ECO:0007829|PDB:1DFO" FT STRAND 315..322 FT /evidence="ECO:0007829|PDB:1DFO" FT HELIX 324..326 FT /evidence="ECO:0007829|PDB:1DFO" FT HELIX 330..339 FT /evidence="ECO:0007829|PDB:1DFO" FT TURN 356..358 FT /evidence="ECO:0007829|PDB:1DFO" FT STRAND 360..365 FT /evidence="ECO:0007829|PDB:1DFO" FT HELIX 367..371 FT /evidence="ECO:0007829|PDB:1DFO" FT HELIX 376..391 FT /evidence="ECO:0007829|PDB:1DFO" FT TURN 392..394 FT /evidence="ECO:0007829|PDB:1DFO" FT HELIX 396..412 FT /evidence="ECO:0007829|PDB:1DFO" FT STRAND 415..417 FT /evidence="ECO:0007829|PDB:1DFO" SQ SEQUENCE 417 AA; 45317 MW; 13E5558E99938539 CRC64; MLKREMNIAD YDAELWQAME QEKVRQEEHI ELIASENYTS PRVMQAQGSQ LTNKYAEGYP GKRYYGGCEY VDIVEQLAID RAKELFGADY ANVQPHSGSQ ANFAVYTALL EPGDTVLGMN LAHGGHLTHG SPVNFSGKLY NIVPYGIDAT GHIDYADLEK QAKEHKPKMI IGGFSAYSGV VDWAKMREIA DSIGAYLFVD MAHVAGLVAA GVYPNPVPHA HVVTTTTHKT LAGPRGGLIL AKGGSEELYK KLNSAVFPGG QGGPLMHVIA GKAVALKEAM EPEFKTYQQQ VAKNAKAMVE VFLERGYKVV SGGTDNHLFL VDLVDKNLTG KEADAALGRA NITVNKNSVP NDPKSPFVTS GIRVGTPAIT RRGFKEAEAK ELAGWMCDVL DSINDEAVIE RIKGKVLDIC ARYPVYA //