ID GLYA_STRTD Reviewed; 416 AA. AC Q03L77; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 14-NOV-2006, sequence version 1. DT 22-APR-2020, entry version 83. 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=STER_0796; OS Streptococcus thermophilus (strain ATCC BAA-491 / LMD-9). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=322159; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-491 / LMD-9; RX PubMed=17030793; DOI=10.1073/pnas.0607117103; RA Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V., RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V., RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M., RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A., RA Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W., RA Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y., RA Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R., RA O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T., RA Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.; RT "Comparative genomics of the lactic acid bacteria."; RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(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; CP000419; ABJ66045.1; -; Genomic_DNA. DR RefSeq; WP_011227085.1; NC_008532.1. DR SMR; Q03L77; -. DR PRIDE; Q03L77; -. DR EnsemblBacteria; ABJ66045; ABJ66045; STER_0796. DR KEGG; ste:STER_0796; -. DR HOGENOM; CLU_022477_2_1_9; -. DR KO; K00600; -. DR OMA; PLEHIIA; -. DR UniPathway; UPA00193; -. DR UniPathway; UPA00288; UER01023. 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; Transferase. FT CHAIN 1..416 FT /note="Serine hydroxymethyltransferase" FT /id="PRO_1000006335" FT REGION 125..127 FT /note="Substrate binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051" FT REGION 355..357 FT /note="Substrate binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051" FT BINDING 35 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051" FT BINDING 55 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051" FT BINDING 57 FT /note="Substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051" FT BINDING 64 FT /note="Substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051" FT BINDING 65 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051" FT BINDING 99 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051" FT BINDING 121 FT /note="Substrate; via carbonyl oxygen" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051" FT BINDING 176 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051" FT BINDING 204 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051" FT BINDING 229 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051" FT BINDING 236 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051" FT BINDING 262 FT /note="Pyridoxal phosphate; via amide nitrogen and carbonyl FT oxygen" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00051" FT BINDING 363 FT /note="Pyridoxal phosphate" 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 416 AA; 45086 MW; 2F6437A39A42094A CRC64; MIFDKEDYKA FDPELWNAID AEAERQQNNI ELIASENVVS KAVMAAQGTL LTNKYAEGYP GKRYYGGTAV IDVVETLAIE RAKKLFGAKF ANVQPHSGSQ ANAAVYMSLI QPGDTVMGMD LSAGGHLTHG APVSFSGKTY NFVSYNVDKE SELLDYDAIL AQAKEVRPKL IVAGASAYSR IIDFAKFREI ADAVGAYLMV DMAHIAGLVA SGHHPSPVPY AHVTTTTTHK TLRGPRGGLI LTDDEDIAKK LNSAVFPGLQ GGPLEHVIAA KAVALKEALD PAFKEYGENV IKNAAAMADV FNQHPDFRVI SGGTNNHLFL VDVTKVVENG KVAQNVLEEV NITLNKNSIP YEQLSPFKTS GIRVGSPAIT SRGMGEAESR QIAEWMVEAL ENHDKPEVLE RIRGDVKVLT DAFPLY //