ID GLYA_LACLM Reviewed; 415 AA. AC A2RIS0; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 06-MAR-2007, sequence version 1. DT 02-SEP-2026, entry version 102. DE RecName: Full=Serine hydroxymethyltransferase {ECO:0000255|HAMAP-Rule:MF_00051}; DE Short=SHMT {ECO:0000255|HAMAP-Rule:MF_00051}; DE Short=Serine methylase {ECO:0000255|HAMAP-Rule:MF_00051}; DE EC=2.1.2.1 {ECO:0000255|HAMAP-Rule:MF_00051}; GN Name=glyA {ECO:0000255|HAMAP-Rule:MF_00051}; GN OrderedLocusNames=llmg_0563; OS Lactococcus lactis subsp. cremoris (strain MG1363). OC Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Lactococcus; Lactococcus cremoris subsp. cremoris. OX NCBI_TaxID=416870; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MG1363; RX PubMed=17307855; DOI=10.1128/jb.01768-06; RA Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C., RA Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P., RA van Sinderen D., Kok J.; RT "The complete genome sequence of the lactic acid bacterial paradigm RT Lactococcus lactis subsp. cremoris MG1363."; RL J. Bacteriol. 189:3256-3270(2007). 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. Also exhibits THF-independent aldolase activity CC toward beta-hydroxyamino acids, producing glycine and aldehydes, via a CC retro-aldol mechanism. {ECO:0000255|HAMAP-Rule:MF_00051}. 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 -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00051}; 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}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00051}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00051}. CC -!- SIMILARITY: Belongs to the SHMT family. {ECO:0000255|HAMAP- CC Rule:MF_00051}. 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; AM406671; CAL97165.1; -; Genomic_DNA. DR RefSeq; WP_011834589.1; NC_009004.1. DR AlphaFoldDB; A2RIS0; -. DR SMR; A2RIS0; -. DR STRING; 416870.llmg_0563; -. DR PaxDb; 416870-llmg_0563; -. DR KEGG; llm:llmg_0563; -. DR eggNOG; COG0112; Bacteria. DR HOGENOM; CLU_022477_2_1_9; -. DR OrthoDB; 9803846at2; -. DR PhylomeDB; A2RIS0; -. DR UniPathway; UPA00193; -. DR UniPathway; UPA00288; UER01023. DR Proteomes; UP000000364; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule. DR GO; GO:0006545; P:glycine biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006563; P:L-serine metabolic process; IEA:UniProtKB-ARBA. DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniRule. DR CDD; cd00378; SHMT; 1. DR FunFam; 3.40.640.10:FF:000001; Serine hydroxymethyltransferase; 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; IPR049943; Ser_HO-MeTrfase-like. DR InterPro; IPR019798; Ser_HO-MeTrfase_PLP_BS. DR InterPro; IPR039429; SHMT-like_dom. DR NCBIfam; NF000586; PRK00011.1; 1. DR PANTHER; PTHR11680; SERINE HYDROXYMETHYLTRANSFERASE; 1. DR PANTHER; PTHR11680:SF35; SERINE HYDROXYMETHYLTRANSFERASE 1; 1. DR Pfam; PF00464; SHMT; 1. DR PIRSF; PIRSF000412; SHMT; 1. DR SUPFAM; SSF53383; PLP-dependent transferases; 1. DR PROSITE; PS00096; SHMT; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Cytoplasm; One-carbon metabolism; KW Pyridoxal phosphate; Reference proteome; Transferase. FT CHAIN 1..415 FT /note="Serine hydroxymethyltransferase" FT /id="PRO_1000006271" 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 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 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 SITE 229 FT /note="Plays an important role in substrate specificity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051" FT MOD_RES 230 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051" SQ SEQUENCE 415 AA; 44823 MW; 04963A7EA5124F9D CRC64; MIFDKEDFES FDPELWAAIH AEEIRQQQNI ELIASENIVS KAVMAAQGSV LTNKYAEGYP GKRYYGGTEA VDVVENLAID RAKELFGAKF ANVQPHSGSQ ANAAAYMALI QPGDTVLGMD LNAGGHLTHG ASVNFSGKTY HFVPYGVNPQ TELLDYEEIL KIAKEVQPKL IVAGASAYSR LIDFAKFRQI ADSVGAKLMV DMAHIAGLVA TGAHPNPLPY ADVVTTTTHK TLRGPRGGMI LTNDEVLAKK INSAIFPGTQ GGPLEHVIAA KAVAFKEALD PEFATYIEQV IKNTQAMADE FAKVDGLRLI AGGSDNHLLN LKVLDLGING KEAQDLLDSV HITLNKEAIP DETLSPFKTS GVRIGAAAIT SRGFKEAEAR KVAQLVSKAL VNHDNQEKLE EVRKSALELT HQFPL //