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 13-NOV-2013, entry version 87. DE RecName: Full=Serine hydroxymethyltransferase; DE Short=SHMT; DE Short=Serine methylase; DE EC=2.1.2.1; GN Name=glyA; OrderedLocusNames=BH3765; OS Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM OS 9153 / C-125). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. 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., RA Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., RA Horikoshi K.; RT "Complete genome sequence of the alkaliphilic bacterium Bacillus RT halodurans 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 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 (By CC similarity). CC -!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + glycine + CC H(2)O = tetrahydrofolate + L-serine. CC -!- COFACTOR: Pyridoxal phosphate (By similarity). CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. CC -!- PATHWAY: Amino-acid biosynthesis; glycine biosynthesis; glycine CC from L-serine: step 1/1. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the SHMT family. 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; NP_244632.1; NC_002570.2. DR ProteinModelPortal; Q9K6G4; -. DR SMR; Q9K6G4; 1-404. DR STRING; 272558.BH3765; -. DR EnsemblBacteria; BAB07484; BAB07484; BAB07484. DR GeneID; 894524; -. DR KEGG; bha:BH3765; -. DR PATRIC; 18944840; VBIBacHal18977_3918. DR eggNOG; COG0112; -. DR HOGENOM; HOG000239405; -. DR KO; K00600; -. DR OMA; MLIDLRN; -. DR OrthoDB; EOG6Z0QB2; -. DR ProtClustDB; PRK00011; -. DR BioCyc; BHAL272558:GJC5-3868-MONOMER; -. 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-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 1 413 Serine hydroxymethyltransferase. FT /FTId=PRO_0000113529. FT REGION 121 123 Substrate binding (By similarity). FT REGION 349 351 Substrate binding (By similarity). FT BINDING 31 31 Pyridoxal phosphate (By similarity). FT BINDING 51 51 Pyridoxal phosphate (By similarity). FT BINDING 53 53 Substrate (By similarity). FT BINDING 60 60 Substrate (By similarity). FT BINDING 61 61 Pyridoxal phosphate (By similarity). FT BINDING 117 117 Substrate; via carbonyl oxygen (By FT similarity). FT BINDING 172 172 Pyridoxal phosphate (By similarity). FT BINDING 200 200 Pyridoxal phosphate (By similarity). FT BINDING 225 225 Pyridoxal phosphate (By similarity). FT BINDING 232 232 Pyridoxal phosphate (By similarity). FT BINDING 257 257 Pyridoxal phosphate; via amide nitrogen FT and carbonyl oxygen (By similarity). FT BINDING 357 357 Pyridoxal phosphate (By similarity). FT MOD_RES 226 226 N6-(pyridoxal phosphate)lysine (By FT similarity). 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 //