ID A0A257AC01_9CREN Unreviewed; 416 AA. AC A0A257AC01; DT 22-NOV-2017, integrated into UniProtKB/TrEMBL. DT 22-NOV-2017, sequence version 1. DT 12-SEP-2018, entry version 5. DE RecName: Full=Serine hydroxymethyltransferase {ECO:0000256|HAMAP-Rule:MF_00051}; DE Short=SHMT {ECO:0000256|HAMAP-Rule:MF_00051}; DE Short=Serine methylase {ECO:0000256|HAMAP-Rule:MF_00051}; DE EC=2.1.2.- {ECO:0000256|HAMAP-Rule:MF_00051}; GN Name=glyA {ECO:0000256|HAMAP-Rule:MF_00051}; GN ORFNames=B6U69_02640 {ECO:0000313|EMBL:OYT61950.1}; OS Thermofilum sp. ex4484_15. OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermofilaceae; OC Thermofilum. OX NCBI_TaxID=2012526 {ECO:0000313|EMBL:OYT61950.1}; RN [1] {ECO:0000313|EMBL:OYT61950.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Ex4484_15 {ECO:0000313|EMBL:OYT61950.1}; RX PubMed=28835260; DOI=.1186/s40168-017-0322-2; RA Dombrowski N., Seitz K.W., Teske A.P., Baker B.J.; RT "Genomic insights into potential interdependencies in microbial RT hydrocarbon and nutrient cycling in hydrothermal sediments."; RL Microbiome 5:106-106(2017). CC -!- FUNCTION: Catalyzes the reversible interconversion of serine and CC glycine with a modified folate serving as the one-carbon carrier. CC Also exhibits a pteridine-independent aldolase activity toward CC beta-hydroxyamino acids, producing glycine and aldehydes, via a CC retro-aldol mechanism. {ECO:0000256|HAMAP-Rule:MF_00051}. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00051}; CC -!- PATHWAY: Amino-acid biosynthesis; glycine biosynthesis; glycine CC from L-serine: step 1/1. {ECO:0000256|HAMAP-Rule:MF_00051}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00051}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00051}. CC -!- SIMILARITY: Belongs to the SHMT family. {ECO:0000256|HAMAP- CC Rule:MF_00051}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00051}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:OYT61950.1}. 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; NJEH01000032; OYT61950.1; -; Genomic_DNA. 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:0008168; F:methyltransferase activity; IEA:UniProtKB-KW. 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:InterPro. 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 PIRSF; PIRSF000412; SHMT; 1. DR SUPFAM; SSF53383; SSF53383; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00051}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00051}; KW Methyltransferase {ECO:0000313|EMBL:OYT61950.1}; KW One-carbon metabolism {ECO:0000256|HAMAP-Rule:MF_00051}; KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00051, KW ECO:0000256|PIRSR:PIRSR000412-50}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00051, KW ECO:0000313|EMBL:OYT61950.1}. FT BINDING 31 31 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 51 51 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 53 53 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00051}. FT BINDING 60 60 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00051}. FT BINDING 61 61 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 95 95 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 117 117 Substrate; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_00051}. FT BINDING 172 172 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 200 200 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 226 226 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 361 361 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT MOD_RES 227 227 N6-(pyridoxal phosphate)lysine. FT {ECO:0000256|HAMAP-Rule:MF_00051, FT ECO:0000256|PIRSR:PIRSR000412-50}. SQ SEQUENCE 416 AA; 46290 MW; EEBE3F35D042F65B CRC64; MELPGEALRI LKLNEAHNKW RREETVNLIA SENLTSPLVD SLYLSDAMHR YAEGLPFKRF YQGTKYIDEI EVLCEELMRK LFKAKYIDVR PISGTIANGA VFYALGKSGD TTCICPLPGG GHVSHSKYGI MGALGLKPLP LPFNVEEFNI DVEGASKLIK EVRPKFVVLG ASVILFPHPV KELGDAANEV GSKIIFDAAH VLGLIAGGKY PNPLSEGANV VTSSTHKTFP GPQGGVILTN EEEIYKKVKK VVFPVFVSNH HLHRLAATAM AAVEMLYFGE AYASQIIKNA KRLAECLYNR GFKVLGEKKG FTETHQVLLD VRELGGGTKV ALMLEKANII VNKNMLPWDR PEDIKNPSGI RIGVQEVTRI GMREGDMEVL AEYFYKVLIK REDPAKVAEE VREFRGKFKE LLYTFK //