ID GLYA_NEIG1 Reviewed; 416 AA. AC Q5F8C0; DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 24-JUL-2024, entry version 111. 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}; OrderedLocusNames=NGO0866; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae; OC Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=10417653; DOI=10.1046/j.1365-2958.1999.01514.x; RA Zhu P., Morelli G., Achtman M.; RT "The opcA and (psi)opcB regions in Neisseria: genes, pseudogenes, RT deletions, insertion elements and DNA islands."; RL Mol. Microbiol. 33:635-650(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AJ242839; CAB45001.1; -; Genomic_DNA. DR EMBL; AE004969; AAW89567.1; -; Genomic_DNA. DR RefSeq; WP_010951137.1; NC_002946.2. DR RefSeq; YP_207979.1; NC_002946.2. DR AlphaFoldDB; Q5F8C0; -. DR SMR; Q5F8C0; -. DR STRING; 242231.NGO_0866; -. DR KEGG; ngo:NGO_0866; -. DR PATRIC; fig|242231.10.peg.1022; -. DR HOGENOM; CLU_022477_2_1_4; -. DR UniPathway; UPA00193; -. DR UniPathway; UPA00288; UER01023. DR Proteomes; UP000000535; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0050897; F:cobalt ion binding; 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:0070905; F:serine binding; IEA:TreeGrafter. DR GO; GO:0008270; F:zinc ion binding; IEA:TreeGrafter. DR GO; GO:0046655; P:folic acid metabolic process; IEA:TreeGrafter. DR GO; GO:0019264; P:glycine biosynthetic process from serine; IEA:UniProtKB-UniRule. DR GO; GO:0006565; P:L-serine catabolic process; IEA:TreeGrafter. DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway. 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; IPR049943; Ser_HO-MeTrfase-like. 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. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Cytoplasm; One-carbon metabolism; KW Pyridoxal phosphate; Reference proteome; Transferase. FT CHAIN 1..416 FT /note="Serine hydroxymethyltransferase" FT /id="PRO_0000113620" 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 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 416 AA; 44990 MW; F53A0C9274D00219 CRC64; MFSKSVTLAQ YDPDLAAAIA QEDRRQQDHV ELIASENYVS CAVMEAQGSQ LTNKYAEGYP AKRYYGGCEY VDIVEQLAID RVKELFGAAY ANVQPHSGSQ ANQAVYASVL KPGDTILGMS LAHGGHLTHG ASVNISGKLY NAVTYGLDEN EVLDYAEVER LALEHKPKMI VAGASAYALQ IDWAKFREIA DKVGAYLFVD MAHYAGLVAG GEYPNPVPFC DFVTTTTHKT LRGPRGGVIL CRDNTHEKAL NSSIFPSLQG GPLMHVIAAK AVAFKEALQP EFKQYAKQVK INAAVMAEEL VKRGLRIVSG RTESHVFLVD LQPMKITGKA AEAALGKAHI TVNKNAIPND PEKPFVTSGI RIGSAAMTTR GFNETDARVL SNLVADVLAN PEDEANLAKV RGQVTALCDK YPVYGT //