ID A0A2D6WNW7_9BACT Unreviewed; 418 AA. AC A0A2D6WNW7; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 23-MAY-2018, entry version 2. 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; OC Puniceicoccaceae. OX NCBI_TaxID=2026784 {ECO:0000313|EMBL:MAH40359.1, ECO:0000313|Proteomes:UP000226557}; RN [1] {ECO:0000313|EMBL:MAH40359.1, ECO:0000313|Proteomes:UP000226557} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ARS1008 {ECO:0000313|EMBL:MAH40359.1}; RA Tully B.J., Graham E.D., Heidelberg J.F.; RT "The Reconstruction of 2,631 Draft Metagenome-Assembled Genomes from RT the 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 CC carrier. This reaction serves as the major source of one-carbon CC groups required for the biosynthesis of purines, thymidylate, CC methionine, and other important biomolecules. Also exhibits THF- CC independent aldolase activity toward beta-hydroxyamino acids, CC producing glycine and aldehydes, via a retro-aldol mechanism. CC {ECO:0000256|HAMAP-Rule:MF_00051}. CC -!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + glycine + CC H(2)O = tetrahydrofolate + L-serine. {ECO:0000256|HAMAP- CC Rule:MF_00051}. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00051}; CC -!- PATHWAY: Amino-acid biosynthesis; glycine biosynthesis; glycine CC from L-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 CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 CDD; cd00378; SHMT; 1. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 2. 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 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 Complete proteome {ECO:0000313|Proteomes:UP000226557}; 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 Transferase {ECO:0000256|HAMAP-Rule:MF_00051, KW ECO:0000313|EMBL:MAH40359.1}. FT REGION 126 128 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT REGION 356 358 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 36 36 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 56 56 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 58 58 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00051}. FT BINDING 65 65 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00051}. FT BINDING 66 66 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 100 100 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 122 122 Substrate; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_00051}. FT BINDING 177 177 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 205 205 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 230 230 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 237 237 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 262 262 Pyridoxal phosphate; via amide nitrogen FT and carbonyl oxygen. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 364 364 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT MOD_RES 231 231 N6-(pyridoxal phosphate)lysine. FT {ECO:0000256|HAMAP-Rule:MF_00051}. 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 //