ID GLYA_STRGC Reviewed; 420 AA. AC A8AXC8; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 23-OCT-2007, sequence version 1. DT 02-SEP-2026, entry version 107. 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=SGO_1151; OS Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 / OS DL1 / V288). OC Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=467705; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288; RX PubMed=17720781; DOI=10.1128/jb.01023-07; RA Vickerman M.M., Iobst S., Jesionowski A.M., Gill S.R.; RT "Genome-wide transcriptional changes in Streptococcus gordonii in response RT to competence signaling peptide."; RL J. Bacteriol. 189:7799-7807(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; CP000725; ABV09592.1; -; Genomic_DNA. DR RefSeq; WP_012000557.1; NC_009785.1. DR AlphaFoldDB; A8AXC8; -. DR SMR; A8AXC8; -. DR STRING; 467705.SGO_1151; -. DR KEGG; sgo:SGO_1151; -. DR eggNOG; COG0112; Bacteria. DR HOGENOM; CLU_022477_2_1_9; -. DR UniPathway; UPA00193; -. DR UniPathway; UPA00288; UER01023. DR Proteomes; UP000001131; 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 FunFam; 3.90.1150.10:FF:000072; 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..420 FT /note="Serine hydroxymethyltransferase" FT /id="PRO_1000074915" 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 420 AA; 45538 MW; CBE56555C05ACF93 CRC64; MIFDQEDYKA FDPEIWEAVA KEEERQQHNI ELIASENVVS KAVMAAQGSI LTNKYAEGYP GRRYYGGTDV VDVIESLAIE RAKEIFGAKF ANVQPHSGSQ ANCAAYMALI EPGDTVMGMD LSAGGHLTHG ASVSFSGQTY NFVSYSVDPE TELLDFDAIL KQAKEVQPKL IVAGASAYSH IIDFSKFREI ADAVGAKLMV DMAHIAGLVA AGLHPSPVPY ADITTTTTHK TLRGPRGGLI LTNDEDLAKK INSAIFPGIQ GGPLEHVIAA KAVAFKEVLD PAFKVYAQQI LDNAQAMAQV FRQHDKFRVI SDGTENHLFL VDVTKVVENG KVAQNLLDEV NITLNKNSIP YETLSPFKTS GIRIGTAAIA ARGFGVTESI KVAELIIKAL ENAENEAVLN QVRAEVRELT DAFPLYEGLN //