GLYA_ECOLI
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 03-AUG-2022, entry version 140.
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, ECO:0000303|PubMed:6300791};
GN OrderedLocusNames=b2551, JW2535;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; 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=5,10-methenyltetrahydrofolate + H2O = (6S)-5-formyl-5,6,7,8-
CC tetrahydrofolate + H(+); Xref=Rhea:RHEA:34767, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57455, ChEBI:CHEBI:57457;
CC Evidence={ECO:0000269|PubMed:10858298, 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}.
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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 SWISS-2DPAGE; P0A825; -.
DR jPOST; P0A825; -.
DR PaxDb; P0A825; -.
DR PRIDE; P0A825; -.
DR EnsemblBacteria; AAC75604; AAC75604; b2551.
DR EnsemblBacteria; BAA16459; BAA16459; BAA16459.
DR GeneID; 66673561; -.
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; SHPAGLI; -.
DR PhylomeDB; P0A825; -.
DR BioCyc; EcoCyc:GLYOHMETRANS-MON; -.
DR BioCyc; MetaCyc:GLYOHMETRANS-MON; -.
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: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; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 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; PTHR11680; 1.
DR Pfam; PF00464; SHMT; 1.
DR PIRSF; PIRSF000412; SHMT; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00096; SHMT; 1.
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 non-
FT 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
