ID A0A7C6DGY5_9FIRM Unreviewed; 414 AA. AC A0A7C6DGY5; DT 02-DEC-2020, integrated into UniProtKB/TrEMBL. DT 02-DEC-2020, sequence version 1. DT 03-AUG-2022, entry version 6. 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=2.1.2.1 {ECO:0000256|HAMAP-Rule:MF_00051}; GN Name=glyA {ECO:0000256|HAMAP-Rule:MF_00051}; GN ORFNames=GXZ81_04735 {ECO:0000313|EMBL:HHU04306.1}; OS Fastidiosipila sp. OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae; OC Fastidiosipila; unclassified Fastidiosipila. OX NCBI_TaxID=1938886 {ECO:0000313|EMBL:HHU04306.1, ECO:0000313|Proteomes:UP000579181}; RN [1] {ECO:0000313|EMBL:HHU04306.1, ECO:0000313|Proteomes:UP000579181} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AS08sgBPME_367 {ECO:0000313|EMBL:HHU04306.1}; RX PubMed=32123542; RA Campanaro S., Treu L., Rodriguez-R L.M., Kovalovszki A., Ziels R.M., RA Maus I., Zhu X., Kougias P.G., Basile A., Luo G., Schluter A., RA Konstantinidis K.T., Angelidaki I.; RT "New insights from the biogas microbiome by comprehensive genome-resolved RT metagenomics of nearly 1600 species originating from multiple anaerobic RT digesters."; RL Biotechnol. Biofuels 13:25-20(2020). CC -!- FUNCTION: Catalyzes the reversible interconversion of serine and CC glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. CC This reaction serves as the major source of one-carbon groups required CC for the biosynthesis of purines, thymidylate, methionine, and other CC important biomolecules. Also exhibits THF-independent aldolase activity CC toward beta-hydroxyamino acids, producing glycine and aldehydes, via a CC retro-aldol mechanism. {ECO:0000256|HAMAP-Rule:MF_00051}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = CC (6S)-5,6,7,8-tetrahydrofolate + L-serine; Xref=Rhea:RHEA:15481, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, ChEBI:CHEBI:33384, CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57453; EC=2.1.2.1; CC Evidence={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|ARBA:ARBA00004697, ECO:0000256|HAMAP- CC Rule:MF_00051}. CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. CC {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:HHU04306.1}. 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; DUQA01000087; HHU04306.1; -; Genomic_DNA. DR UniPathway; UPA00193; -. DR UniPathway; UPA00288; UER01023. DR Proteomes; UP000579181; 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:UniProtKB-UniPathway. 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; IPR019798; Ser_HO-MeTrfase_PLP_BS. DR InterPro; IPR039429; SHMT-like_dom. 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 {ECO:0000256|HAMAP-Rule:MF_00051}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00051}; KW Methyltransferase {ECO:0000313|EMBL:HHU04306.1}; KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563, ECO:0000256|HAMAP- KW 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 7..381 FT /note="SHMT" FT /evidence="ECO:0000259|Pfam:PF00464" FT REGION 123..125 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 33 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 53 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 55 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 62 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 63 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 119 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 174 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 202 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 227 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 234 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 359 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT MOD_RES 228 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051, FT ECO:0000256|PIRSR:PIRSR000412-50" SQ SEQUENCE 414 AA; 45610 MW; 702AD177686489E6 CRC64; MLYQHVKETD PKLYDSLICE LDRQQSKLEM IASENFVSKA VMEAAGSVLT NKYAEGYPGR RYYGGCEHVD VAEDLAIDRL KELFGAEYAN VQPHSGANAN TAVYFAMLEP GDTILGLDLD HGGHLTHGMR INFSGKYFHA EGYKVDKETE QIDYDVVRER ALEVKPKMII AGGSAYPRKI DFKKFREIAD EVGAYLMVDM AHIAGLIAAG LHENPVPYAD FVTSTTHKTL RGPRGGIILA KKEYAKKINS AVFPGLQGGP LMHVIAAKAV AFQEALQPSF KEYQQNVVNN AKTLGESLNK HGVNLVSGGT DTHLLLIDLR GTGCNGKVLQ ERLDDVNITT NKNTVPYETE SAMVTSGLRI GTPALTTRGF GKEEMELLGE LISLAIFKYD ESKDRIIEEV AALCEKFPLY ADLK //