ID A0A2D6WNW7_9BACT Unreviewed; 418 AA. AC A0A2D6WNW7; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 11-DEC-2019, entry version 9. 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=CML08_03030 {ECO:0000313|EMBL:MAH40359.1}; OS Puniceicoccaceae bacterium. OC Bacteria; Verrucomicrobia; Opitutae; Puniceicoccales; Puniceicoccaceae. OX NCBI_TaxID=2026784 {ECO:0000313|EMBL:MAH40359.1, ECO:0000313|Proteomes:UP000226557}; RN [1] {ECO:0000313|Proteomes:UP000226557} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Tully B.J., Graham E.D., Heidelberg J.F.; RT "The Reconstruction of 2,631 Draft Metagenome-Assembled Genomes from the RT Global Oceans."; RL Submitted (SEP-2017) 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|HAMAP-Rule:MF_00051, CC 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|HAMAP- CC 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:MAH40359.1}. 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; NZEM01000048; MAH40359.1; -; Genomic_DNA. DR UniPathway; UPA00193; -. DR UniPathway; UPA00288; UER01023. DR Proteomes; UP000226557; 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; IPR015422; PyrdxlP-dep_Trfase_dom1. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major. 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:MAH40359.1}; KW One-carbon metabolism {ECO:0000256|HAMAP-Rule:MF_00051}; KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00051, KW ECO:0000256|PIRSR:PIRSR000412-50}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00051, ECO:0000313|EMBL:MAH40359.1}. FT DOMAIN 9..387 FT /note="SHMT" FT /evidence="ECO:0000259|Pfam:PF00464" FT REGION 126..128 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT REGION 356..358 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 36 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 56 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 58 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 65 FT /note="Substrate" 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 100 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 122 FT /note="Substrate; via carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 177 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 205 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 230 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 237 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 262 FT /note="Pyridoxal phosphate; via amide nitrogen and carbonyl FT oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 364 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT MOD_RES 231 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051, FT ECO:0000256|PIRSR:PIRSR000412-50" SQ SEQUENCE 418 AA; 45097 MW; EDCB295AF0C975D3 CRC64; MNPLNDTALD QLDPEIAQLI AREKARQQSH IELIASENFT YPAIMEAQGS ILTNKYAEGY PNKRYYGGCD FVDSIETIAI ERAKALFRAD HANVQPHAGS QANAAVYLSV LKPGDKILTM NLSDGGHLTH GHPMNFSGIY HEVVHYGVSI ENGLIDYDAI AESAEREQPK MITVGASAYS RVIDFKRMSE IARSVGAYLL ADIAHIAGLV AAGVHPSPVP YADFVTTTTH KTLRGPRGGL ILCKTDHAKK IDSAVFPGTQ GGPLMHVIAA KATCFKEANT DAFKTYQKQV ASNANTLANA LLEAGHNIVS GGTENHLFMI DLRKKYPQLT GKRAQIALDQ AHITANKNTV PGETRSPFQT SGIRIGTPAV TSRGFVEADM LKVAKAINLV LDSADNETTN AEAKSIALAL CSQYPLPY //