ID A0A257AC01_9CREN Unreviewed; 416 AA. AC A0A257AC01; DT 22-NOV-2017, integrated into UniProtKB/TrEMBL. DT 22-NOV-2017, sequence version 1. DT 14-DEC-2022, entry version 21. 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; Thermofilales; Thermofilaceae; OC Thermofilum. OX NCBI_TaxID=2012526 {ECO:0000313|EMBL:OYT61950.1, ECO:0000313|Proteomes:UP000243135}; RN [1] {ECO:0000313|EMBL:OYT61950.1, ECO:0000313|Proteomes:UP000243135} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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 hydrocarbon RT 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. Also CC exhibits a pteridine-independent aldolase activity toward beta- CC hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol CC mechanism. {ECO:0000256|HAMAP-Rule:MF_00051}. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|ARBA:ARBA00001933, CC ECO:0000256|HAMAP-Rule:MF_00051, ECO:0000256|PIRSR:PIRSR000412-50}; CC -!- PATHWAY: Amino-acid biosynthesis; glycine biosynthesis; glycine from L- CC 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|ARBA:ARBA00006376, CC ECO:0000256|HAMAP-Rule:MF_00051}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00051}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {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 AlphaFoldDB; A0A257AC01; -. DR UniPathway; UPA00288; UER01023. DR Proteomes; UP000243135; Unassembled WGS sequence. 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:0032259; P:methylation; IEA:UniProtKB-KW. 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; IPR015421; PyrdxlP-dep_Trfase_major. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small. DR InterPro; IPR001085; Ser_HO-MeTrfase. DR InterPro; IPR039429; SHMT-like_dom. DR PANTHER; PTHR11680; SERINE HYDROXYMETHYLTRANSFERASE; 1. DR Pfam; PF00464; SHMT; 1. DR PIRSF; PIRSF000412; SHMT; 1. DR SUPFAM; SSF53383; PLP-dependent transferases; 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|ARBA:ARBA00022898, ECO:0000256|HAMAP- KW Rule:MF_00051}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00051}. FT DOMAIN 17..383 FT /note="SHMT" FT /evidence="ECO:0000259|Pfam:PF00464" FT BINDING 117 FT /ligand="(6S)-5,6,7,8-tetrahydrofolate" FT /ligand_id="ChEBI:CHEBI:57453" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 121..123 FT /ligand="(6S)-5,6,7,8-tetrahydrofolate" FT /ligand_id="ChEBI:CHEBI:57453" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 242 FT /ligand="(6S)-5,6,7,8-tetrahydrofolate" FT /ligand_id="ChEBI:CHEBI:57453" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT SITE 226 FT /note="Plays an important role in substrate specificity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT MOD_RES 227 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="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 //