ID GLYA_PROM9 Reviewed; 423 AA. AC Q31CS4; DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 06-DEC-2005, sequence version 1. DT 02-SEP-2026, entry version 108. 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=PMT9312_0260; OS Prochlorococcus marinus (strain MIT 9312). OC Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Synechococcales; OC Prochlorococcaceae; Prochlorococcus. OX NCBI_TaxID=74546; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MIT 9312; RX PubMed=16556843; DOI=10.1126/science.1122050; RA Coleman M.L., Sullivan M.B., Martiny A.C., Steglich C., Barry K., RA Delong E.F., Chisholm S.W.; RT "Genomic islands and the ecology and evolution of Prochlorococcus."; RL Science 311:1768-1770(2006). 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; CP000111; ABB49321.1; -; Genomic_DNA. DR RefSeq; WP_011375823.1; NC_007577.1. DR AlphaFoldDB; Q31CS4; -. DR SMR; Q31CS4; -. DR STRING; 74546.PMT9312_0260; -. DR KEGG; pmi:PMT9312_0260; -. DR eggNOG; COG0112; Bacteria. DR HOGENOM; CLU_022477_2_1_3; -. DR OrthoDB; 9803846at2; -. DR UniPathway; UPA00193; -. DR UniPathway; UPA00288; UER01023. 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; Transferase. FT CHAIN 1..423 FT /note="Serine hydroxymethyltransferase" FT /id="PRO_0000234998" FT BINDING 120 FT /ligand="(6S)-5,6,7,8-tetrahydrofolate" FT /ligand_id="ChEBI:CHEBI:57453" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051" FT BINDING 124..126 FT /ligand="(6S)-5,6,7,8-tetrahydrofolate" FT /ligand_id="ChEBI:CHEBI:57453" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051" FT BINDING 245 FT /ligand="(6S)-5,6,7,8-tetrahydrofolate" FT /ligand_id="ChEBI:CHEBI:57453" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051" FT BINDING 353..355 FT /ligand="(6S)-5,6,7,8-tetrahydrofolate" FT /ligand_id="ChEBI:CHEBI:57453" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051" FT SITE 228 FT /note="Plays an important role in substrate specificity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051" FT MOD_RES 229 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051" SQ SEQUENCE 423 AA; 46016 MW; AAF63E243EE55A8E CRC64; MNILQNLKKS DPVISNFINS EKNRQETHLE LIASENFASI AVMQAQGSVL TNKYAEGLPQ KRYYGGCEFV DEIEELAIQR AKKLFNANWA NVQPHSGAQA NAAVFLSLLQ PGDTIMGMDL SHGGHLTHGS PVNMSGKWFN AVHYGVNKET SELNFDEIRE IALETKPKLI ICGYSAYPRT IDFESFRNIA DEVGAFLMAD IAHIAGLVAS KLHPNPLPYC DVVTTTTHKT LRGPRGGLIL CKDGEFGKKF DKSVFPGTQG GPLEHIIAAK AVAFGEALQP DFVNYSQQVI KNAKVLASTL ISRGIDIVSG GTDNHIVLLD LRSINMTGKI ADLLVSAVNI TANKNTVPFD PESPFVTSGL RLGTAALTTR GFNETAFAEV GEIIADRLLN PNDSVIESQC KDKVLALCNR FPLYEGKLEA SIK //