ID A0A4Q3Y5E0_9RHOB Unreviewed; 431 AA. AC A0A4Q3Y5E0; DT 31-JUL-2019, integrated into UniProtKB/TrEMBL. DT 31-JUL-2019, sequence version 1. DT 16-OCT-2019, entry version 3. 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=EU803_16070 {ECO:0000313|EMBL:RYG89669.1}; OS Loktanella sp. IMCC34160. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Loktanella. OX NCBI_TaxID=2510646 {ECO:0000313|EMBL:RYG89669.1, ECO:0000313|Proteomes:UP000294096}; RN [1] {ECO:0000313|EMBL:RYG89669.1, ECO:0000313|Proteomes:UP000294096} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IMCC34160 {ECO:0000313|EMBL:RYG89669.1, RC ECO:0000313|Proteomes:UP000294096}; RA Jang H.-J.; RT "Loktanella sp IMCC34160, Genome."; RL Submitted (FEB-2019) 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: CC Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + CC H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine; CC Xref=Rhea:RHEA:15481, ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, CC ChEBI:CHEBI:33384, ChEBI:CHEBI:57305, ChEBI:CHEBI:57453; CC EC=2.1.2.1; 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 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: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-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:RYG89669.1}. 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; SELP01000007; RYG89669.1; -; Genomic_DNA. DR UniPathway; UPA00193; -. DR UniPathway; UPA00288; UER01023. DR Proteomes; UP000294096; 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: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 Complete proteome {ECO:0000313|Proteomes:UP000294096}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00051}; KW Methyltransferase {ECO:0000313|EMBL:RYG89669.1}; 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 Reference proteome {ECO:0000313|Proteomes:UP000294096}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00051, KW ECO:0000313|EMBL:RYG89669.1}. FT DOMAIN 16 392 SHMT. {ECO:0000259|Pfam:PF00464}. FT REGION 132 134 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 42 42 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 62 62 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 64 64 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00051}. FT BINDING 71 71 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00051}. FT BINDING 72 72 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 106 106 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 128 128 Substrate; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_00051}. FT BINDING 183 183 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 211 211 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 236 236 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 243 243 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 269 269 Pyridoxal phosphate; via amide nitrogen FT and carbonyl oxygen. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 369 369 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT MOD_RES 237 237 N6-(pyridoxal phosphate)lysine. FT {ECO:0000256|HAMAP-Rule:MF_00051, FT ECO:0000256|PIRSR:PIRSR000412-50}. SQ SEQUENCE 431 AA; 46083 MW; BAD35E7E607BFBB6 CRC64; MNATTRDSGF FTESLSSRDP ELFGAITGEL GRQRHEIELI ASENIVSAAV MEAQGSVMTN KYAEGYPGRR YYGGCEFVDV AENLAIERSC QLFDCAFANV QPNSGSQANQ GVFQALLTPG DTILGMSLDA GGHLTHGAKP NQSGKWFNAV QYGVRQQDSQ IDYDQIAALA TEHQPKMIIA GGSAIPRIID FARMREIADS VGAYLMVDMA HFAGLVAAGL YPSPFPHAHV ATTTTHKTLR GPRGGAIFTN DEDIAKKVNS AIFPGIQGGP LMHVIAAKAV AFGEALRPEF KLYQEQVVKN AKALADQLMK GGLDIVTGGT DSHVMLVDLR PKGVKGNATE KALGRANITT NKNGIPFDPE KPTVTSGIRL GTPAGTTRGF TEAEFRQIAD WIVEVVDGLA ANGEEGNAEI EAKVKAEVEA LCETFPLYPN L //