ID A0A6G6WEH5_9ACTN Unreviewed; 480 AA. AC A0A6G6WEH5; DT 12-AUG-2020, integrated into UniProtKB/TrEMBL. DT 12-AUG-2020, sequence version 1. DT 29-MAY-2024, entry version 15. 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=G5V58_13010 {ECO:0000313|EMBL:QIG43557.1}; OS Nocardioides anomalus. OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales; OC Nocardioidaceae; Nocardioides. OX NCBI_TaxID=2712223 {ECO:0000313|EMBL:QIG43557.1, ECO:0000313|Proteomes:UP000502996}; RN [1] {ECO:0000313|EMBL:QIG43557.1, ECO:0000313|Proteomes:UP000502996} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R-3366 {ECO:0000313|EMBL:QIG43557.1, RC ECO:0000313|Proteomes:UP000502996}; RA Im W.-T.; RT "Full genome sequence of Nocardioides sp. R-3366."; RL Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases. 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|HAMAP-Rule:MF_00051}. CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. CC {ECO:0000256|HAMAP-Rule:MF_00051}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP- CC 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 --------------------------------------------------------------------------- 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; CP049257; QIG43557.1; -; Genomic_DNA. DR AlphaFoldDB; A0A6G6WEH5; -. DR KEGG; nano:G5V58_13010; -. DR UniPathway; UPA00193; -. DR UniPathway; UPA00288; UER01023. DR Proteomes; UP000502996; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0050897; F:cobalt ion binding; IEA:TreeGrafter. 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:0070905; F:serine binding; IEA:TreeGrafter. DR GO; GO:0008270; F:zinc ion binding; IEA:TreeGrafter. DR GO; GO:0046655; P:folic acid metabolic process; IEA:TreeGrafter. DR GO; GO:0019264; P:glycine biosynthetic process from serine; IEA:UniProtKB-UniRule. DR GO; GO:0006565; P:L-serine catabolic process; IEA:TreeGrafter. 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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1. DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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; SERINE HYDROXYMETHYLTRANSFERASE; 1. DR PANTHER; PTHR11680:SF28; SERINE HYDROXYMETHYLTRANSFERASE; 1. DR Pfam; PF00464; SHMT; 2. DR PIRSF; PIRSF000412; SHMT; 1. DR SUPFAM; SSF53383; PLP-dependent transferases; 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|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00051}; KW Methyltransferase {ECO:0000313|EMBL:QIG43557.1}; 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}; Reference proteome {ECO:0000313|Proteomes:UP000502996}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00051}. FT DOMAIN 22..122 FT /note="Serine hydroxymethyltransferase-like" FT /evidence="ECO:0000259|Pfam:PF00464" FT DOMAIN 156..428 FT /note="Serine hydroxymethyltransferase-like" FT /evidence="ECO:0000259|Pfam:PF00464" FT BINDING 163 FT /ligand="(6S)-5,6,7,8-tetrahydrofolate" FT /ligand_id="ChEBI:CHEBI:57453" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 167..169 FT /ligand="(6S)-5,6,7,8-tetrahydrofolate" FT /ligand_id="ChEBI:CHEBI:57453" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 289 FT /ligand="(6S)-5,6,7,8-tetrahydrofolate" FT /ligand_id="ChEBI:CHEBI:57453" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT SITE 274 FT /note="Plays an important role in substrate specificity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT MOD_RES 275 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051, FT ECO:0000256|PIRSR:PIRSR000412-50" SQ SEQUENCE 480 AA; 51472 MW; 992E6B686076FEBB CRC64; MADVDALISS AYQQILEVIG SVEPRIADAT RQELVDQRAS LKLIASENYA SPAVLLTMGT WFSDKYAEGT VGHRFYAGCQ NVDTVESLAA EHARELFGAP YAYAQPHSGI DANLVAFWSI LAHRVEGPWL EKAGAKNVND LTDEDWETLR HELGNQRLLG MSLDAGGHLT HGFRPNISGK MFHQQQYGTD PATGLLDYDQ VAAKAREFKP LILVAGYSAY PRRVDFAKMR EIADEVGATL MVDMAHFAGL VAGKVFTGDE DPVPHAHVVT TTTHKSLRGP RGGLVLAQEE FASSVDRGCP MVLGGPLSHM MAAKAVALAE ARQDSFRTYA QNIANNAQSL AEGFLKRGAT LVTGGTDNHL VLLDVSSFGL TGRQAESALL DAGVVTNRNS VPADPNGAWY TSGIRLGTPA LTTRGFGHDE FDTVAQLIVQ VLQNTQPGTT KDGAASKASY VLADGVADKV KDASSELLDK HPLYPGLTLD //