ID GLYA_HALH5 Reviewed; 413 AA. AC Q9K6G4; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 24-JUL-2024, entry version 132. 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=BH3765; OS Halalkalibacterium halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 OS / JCM 9153 / C-125) (Bacillus halodurans). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; OC Halalkalibacterium (ex Joshi et al. 2022). OX NCBI_TaxID=272558; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125; RX PubMed=11058132; DOI=10.1093/nar/28.21.4317; RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.; RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans RT and genomic sequence comparison with Bacillus subtilis."; RL Nucleic Acids Res. 28:4317-4331(2000). 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; BA000004; BAB07484.1; -; Genomic_DNA. DR PIR; E84120; E84120. DR RefSeq; WP_010899890.1; NC_002570.2. DR AlphaFoldDB; Q9K6G4; -. DR SMR; Q9K6G4; -. DR STRING; 272558.gene:10729678; -. DR KEGG; bha:BH3765; -. DR eggNOG; COG0112; Bacteria. DR HOGENOM; CLU_022477_2_1_9; -. DR OrthoDB; 9803846at2; -. DR UniPathway; UPA00193; -. DR UniPathway; UPA00288; UER01023. DR Proteomes; UP000001258; 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:SF28; 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..413 FT /note="Serine hydroxymethyltransferase" FT /id="PRO_0000113529" FT BINDING 117 FT /ligand="(6S)-5,6,7,8-tetrahydrofolate" FT /ligand_id="ChEBI:CHEBI:57453" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051" FT BINDING 121..123 FT /ligand="(6S)-5,6,7,8-tetrahydrofolate" FT /ligand_id="ChEBI:CHEBI:57453" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051" FT BINDING 241 FT /ligand="(6S)-5,6,7,8-tetrahydrofolate" FT /ligand_id="ChEBI:CHEBI:57453" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051" FT BINDING 349..351 FT /ligand="(6S)-5,6,7,8-tetrahydrofolate" FT /ligand_id="ChEBI:CHEBI:57453" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051" FT SITE 225 FT /note="Plays an important role in substrate specificity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051" FT MOD_RES 226 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051" SQ SEQUENCE 413 AA; 45233 MW; 1133BA2083E3B6BA CRC64; MSTLQSKDPK VFEAVQQELG RQRDKIELIA SENFVSEAVM EAQSSVLTNK YAEGYPGRRY YGGCEYVDIV EDLARDRAKE IFGGEHVNVQ PHSGAQANMA VYFTILEHGD TVLGMNLSHG GHLTHGSPVN FSGIQYNFVE YGVDKESQRI DYEEVRRLAK EHQPKMIVAG ASAYPREIDF AKFREIADEV GAYLMVDMAH IAGLVAAGLH QNPVPHSHFV TTTTHKTLRG PRGGMIICNE EFAKQIDKSI FPGIQGGPLM HVIAAKAVAF GEALQPEFKS YGEAIIRNAK RLGEKLTSEG IDLVSGGTDN HLLLLDLRSL GLTGKVAEKA LDDVGITTNK NTIPFDPESP FVTSGIRIGT AAVTSRGLDE EAMDEIGATI ALTLKNVDNE EKMNEARERV DALTAKFPMY PNL //