ID GLYA_BACHD Reviewed; 413 AA. AC Q9K6G4; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 02-DEC-2020, entry version 121. 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 Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 OS / C-125). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus. 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 SMR; Q9K6G4; -. DR STRING; 272558.10176389; -. DR EnsemblBacteria; BAB07484; BAB07484; BAB07484. DR KEGG; bha:BH3765; -. DR eggNOG; COG0112; Bacteria. DR HOGENOM; CLU_022477_2_1_9; -. DR OMA; PLEHIIA; -. DR OrthoDB; 861782at2; -. DR BioCyc; BHAL272558:G1G3A-3837-MONOMER; -. DR UniPathway; UPA00193; -. DR UniPathway; UPA00288; UER01023. DR Proteomes; UP000001258; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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:0019264; P:glycine biosynthetic process from serine; IEA:UniProtKB-UniRule. DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway. DR CDD; cd00378; SHMT; 1. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR HAMAP; MF_00051; SHMT; 1. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major. DR InterPro; IPR001085; Ser_HO-MeTrfase. DR InterPro; IPR019798; Ser_HO-MeTrfase_PLP_BS. DR InterPro; IPR039429; SHMT-like_dom. DR PANTHER; PTHR11680; PTHR11680; 1. DR Pfam; PF00464; SHMT; 1. DR PIRSF; PIRSF000412; SHMT; 1. DR SUPFAM; SSF53383; SSF53383; 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 REGION 121..123 FT /note="Substrate binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051" FT REGION 349..351 FT /note="Substrate binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051" FT BINDING 31 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051" FT BINDING 51 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051" FT BINDING 53 FT /note="Substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051" FT BINDING 60 FT /note="Substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051" FT BINDING 61 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051" FT BINDING 117 FT /note="Substrate; via carbonyl oxygen" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051" FT BINDING 172 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051" FT BINDING 200 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051" FT BINDING 225 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051" FT BINDING 232 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051" FT BINDING 257 FT /note="Pyridoxal phosphate; via amide nitrogen and carbonyl FT oxygen" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051" FT BINDING 357 FT /note="Pyridoxal phosphate" 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 //