ID A0A422QVY2_9RHOB Unreviewed; 431 AA. AC A0A422QVY2; DT 08-MAY-2019, integrated into UniProtKB/TrEMBL. DT 08-MAY-2019, sequence version 1. DT 03-MAY-2023, entry version 12. 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 ECO:0000313|EMBL:RNF34104.1}; GN ORFNames=A7A09_011835 {ECO:0000313|EMBL:RNF34104.1}; OS Methylarcula marina. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales; OC Paracoccaceae; Methylarcula. OX NCBI_TaxID=72022 {ECO:0000313|EMBL:RNF34104.1, ECO:0000313|Proteomes:UP000238137}; RN [1] {ECO:0000313|EMBL:RNF34104.1, ECO:0000313|Proteomes:UP000238137} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VKM B-2159 {ECO:0000313|EMBL:RNF34104.1, RC ECO:0000313|Proteomes:UP000238137}; RA Shmareva M.N., Doronina N.V., Vasilenko O.V., Tarlachkov S.V., RA Trotsenko Y.A.; RT "Reclassification of Methylarcula marina and Methylarcula terricola as RT Paracoccus methylarcula sp.nov., comb.nov. and Paracoccus terricola RT comb.nov."; RL Submitted (MAY-2018) 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|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:RNF34104.1}. 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; PXNQ02000007; RNF34104.1; -; Genomic_DNA. DR AlphaFoldDB; A0A422QVY2; -. DR OrthoDB; 9803846at2; -. DR UniPathway; UPA00193; -. DR UniPathway; UPA00288; UER01023. DR Proteomes; UP000238137; 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; 3.90.1150.10; 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, MITOCHONDRIAL; 1. DR Pfam; PF00464; SHMT; 1. 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|HAMAP-Rule:MF_00051}; KW Methyltransferase {ECO:0000313|EMBL:RNF34104.1}; 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:UP000238137}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00051}. FT DOMAIN 16..392 FT /note="Serine hydroxymethyltransferase-like" FT /evidence="ECO:0000259|Pfam:PF00464" FT BINDING 128 FT /ligand="(6S)-5,6,7,8-tetrahydrofolate" FT /ligand_id="ChEBI:CHEBI:57453" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 132..134 FT /ligand="(6S)-5,6,7,8-tetrahydrofolate" FT /ligand_id="ChEBI:CHEBI:57453" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT SITE 236 FT /note="Plays an important role in substrate specificity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT MOD_RES 237 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051, FT ECO:0000256|PIRSR:PIRSR000412-50" SQ SEQUENCE 431 AA; 46099 MW; 6C464F96EC2A8555 CRC64; MNAPTRDDGF FTEALTSRDP EIAAAIGKEL GRQRDEIELI ASENIVSKAV LEAQGTVLTN KYAEGYPGKR YYGGCQYVDI VENLAIERAK ELFDCEFANV QPNSGSQMNQ AVFLALLKPG DTFMGLDLNS GGHLTHGSPV NMSGKWFNVL SYGVRQQDQL LDMEAIAEAA RQHKPKLILA GGTAYSRIWD WAAFRKIADE VGAYLMVDMA HIAGLVAGGQ HPSPLPHAHV VTTTTHKSLR GPRGGMVLTN DADIAKKINS AVFPGLQGGP LMHVIAAKAV AFGEALEPGF KDYAAQVVTN ARAMADELMK GGIDIVSGGT DNHLCLADLR PKGVTGKATE AALGRAHITC NKNGVPFDPE KPFVTSGIRL GAPAGTTRGF GEAEFRQIAR WIVEVVDGLA ANGEEGNSAT EDKVRAEVAE LCARFPLYPD L //