ID A0A6G6WEH5_9ACTN Unreviewed; 480 AA. AC A0A6G6WEH5; DT 12-AUG-2020, integrated into UniProtKB/TrEMBL. DT 12-AUG-2020, sequence version 1. DT 19-JAN-2022, entry version 7. 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; Actinobacteria; Propionibacteriales; Nocardioidaceae; OC 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|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 --------------------------------------------------------------------------- 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 KEGG; nano:G5V58_13010; -. DR UniPathway; UPA00193; -. DR UniPathway; UPA00288; UER01023. DR Proteomes; UP000502996; Chromosome. 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; 2. 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: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="SHMT" FT /evidence="ECO:0000259|Pfam:PF00464" FT DOMAIN 156..428 FT /note="SHMT" FT /evidence="ECO:0000259|Pfam:PF00464" FT REGION 167..169 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 46 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 66 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 68 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 75 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 76 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 163 FT /note="Substrate; via carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 218 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 246 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 274 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 281 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 305 FT /note="Pyridoxal phosphate; via amide nitrogen and carbonyl FT oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 405 FT /note="Pyridoxal phosphate" 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 //