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 27-MAY-2015, entry version 63. 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=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., RA Koonin E.V., Pavlov A., Pavlova N., Karamychev V., Polouchine N., RA Shakhova V., Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., RA Goodstein D.M., Hawkins T., Plengvidhya V., Welker D., Hughes J., RA Goh Y., Benson A., Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., RA Smeianov V., Wechter W., Barabote R., Lorca G., Altermann E., RA Barrangou R., Ganesan B., Xie Y., Rawsthorne H., Tamir D., Parker C., RA Breidt F., Broadbent J.R., Hutkins R., O'Sullivan D., Steele J., RA Unlu G., Saier M.H. Jr., Klaenhammer T., Richardson P., Kozyavkin S., RA 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 CC carrier. This reaction serves as the major source of one-carbon CC groups required for the biosynthesis of purines, thymidylate, CC methionine, and other important biomolecules. Also exhibits THF- CC independent aldolase activity toward beta-hydroxyamino acids, CC producing glycine and aldehydes, via a retro-aldol mechanism. CC {ECO:0000255|HAMAP-Rule:MF_00051}. CC -!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + glycine + CC H(2)O = tetrahydrofolate + L-serine. {ECO:0000255|HAMAP- CC 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 CC from L-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 RefSeq; YP_820241.1; NC_008532.1. DR ProteinModelPortal; Q03L77; -. DR SMR; Q03L77; 12-411. DR STRING; 322159.STER_0796; -. DR PRIDE; Q03L77; -. DR EnsemblBacteria; ABJ66045; ABJ66045; STER_0796. DR KEGG; ste:STER_0796; -. DR PATRIC; 19798857; VBIStrThe129203_0781. DR eggNOG; COG0112; -. DR HOGENOM; HOG000239404; -. DR KO; K00600; -. DR OMA; AAWANVQ; -. DR OrthoDB; EOG6Z0QB2; -. DR BioCyc; STHE322159:GJ9F-796-MONOMER; -. DR UniPathway; UPA00193; -. DR UniPathway; UPA00288; UER01023. DR Proteomes; UP000000772; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-HAMAP. DR GO; GO:0019264; P:glycine biosynthetic process from serine; IEA:UniProtKB-HAMAP. DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway. 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; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR InterPro; IPR001085; Ser_HO-MeTrfase. DR InterPro; IPR019798; Ser_HO-MeTrfase_PLP_BS. 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; Complete proteome; Cytoplasm; KW One-carbon metabolism; Pyridoxal phosphate; Transferase. FT CHAIN 1 416 Serine hydroxymethyltransferase. FT /FTId=PRO_1000006335. FT REGION 125 127 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT REGION 355 357 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 35 35 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 55 55 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 57 57 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 64 64 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 65 65 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 99 99 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 121 121 Substrate; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00051}. FT BINDING 176 176 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 204 204 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 229 229 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 236 236 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 262 262 Pyridoxal phosphate; via amide nitrogen FT and carbonyl oxygen. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT BINDING 363 363 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00051}. FT MOD_RES 230 230 N6-(pyridoxal phosphate)lysine. FT {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 //