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-JUL-2010, entry version 61. DE RecName: Full=Serine hydroxymethyltransferase; DE Short=Serine methylase; DE Short=SHMT; DE EC=2.1.2.1; GN Name=glyA; OrderedLocusNames=BH3765; OS Bacillus halodurans. OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=86665; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-125 / C-125 / DSM 18197 / FERM 7344 / JCM 9153; RX MEDLINE=20512582; 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: Interconversion of serine and glycine. 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 -!- SUBUNIT: Homotetramer (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; -. DR SMR; Q9K6G4; 1-404. DR EnsemblBacteria; EBBACT00000051832; EBBACP00000050471; EBBACG00000051823. DR GeneID; 894524; -. DR GenomeReviews; BA000004_GR; BH3765. DR KEGG; bha:BH3765; -. DR NMPDR; fig|272558.1.peg.3765; -. DR HOGENOM; HBG301263; -. DR OMA; GRAYVTC; -. DR PhylomeDB; Q9K6G4; -. DR ProtClustDB; PRK00011; -. DR BioCyc; BHAL272558:BH3765-MONOMER; -. DR BRENDA; 2.1.2.1; 191865. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IEA:EC. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0006544; P:glycine metabolic process; IEA:InterPro. DR GO; GO:0006563; P:L-serine metabolic process; IEA:InterPro. DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW. DR HAMAP; MF_00051_B; SHMT_B; 1; -. DR InterPro; IPR015424; PyrdxlP-dep_Trfase_major_dom. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR001085; Ser_HO-MeTrfase. DR InterPro; IPR019798; Ser_HO-MeTrfase_PLP_BS. DR Gene3D; G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1. DR PANTHER; PTHR11680; Gly_HO-Metrfase; 1. DR Pfam; PF00464; SHMT; 1. DR PIRSF; PIRSF000412; SHMT; 1. DR SUPFAM; SSF53383; PyrdxlP-dep_Trfase_major; 1. DR PROSITE; PS00096; SHMT; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; One-carbon metabolism; KW Pyridoxal phosphate; Transferase. FT CHAIN 1 413 Serine hydroxymethyltransferase. FT /FTId=PRO_0000113529. 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 //