ID A0A3A6NDG1_9DELT Unreviewed; 418 AA. AC A0A3A6NDG1; DT 05-DEC-2018, integrated into UniProtKB/TrEMBL. DT 05-DEC-2018, sequence version 1. DT 10-APR-2019, entry version 4. 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=C4531_18200 {ECO:0000313|EMBL:RJX24868.1}; OS Desulfurivibrio sp. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales; OC Desulfobulbaceae; Desulfurivibrio. OX NCBI_TaxID=2093369 {ECO:0000313|EMBL:RJX24868.1}; RN [1] {ECO:0000313|EMBL:RJX24868.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SURF_16 {ECO:0000313|EMBL:RJX24868.1}; RX PubMed=28644444; DOI=10.1038/ismej.2017.94; RA Momper L., Jungbluth S.P., Lee M.D., Amend J.P.; RT "Energy and carbon metabolisms in a deep terrestrial subsurface fluid RT microbial community."; RL ISME J. 11:2319-2333(2017). RN [2] {ECO:0000313|EMBL:RJX24868.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SURF_16 {ECO:0000313|EMBL:RJX24868.1}; RA Keele B.F.; RL Submitted (MAR-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 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: 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:RJX24868.1}. 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; QZKJ01000118; RJX24868.1; -; Genomic_DNA. DR UniPathway; UPA00193; -. DR UniPathway; UPA00288; UER01023. 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 Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00051}; KW Methyltransferase {ECO:0000313|EMBL:RJX24868.1}; 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, KW ECO:0000313|EMBL:RJX24868.1}. FT DOMAIN 4 380 SHMT. {ECO:0000259|Pfam:PF00464}. FT REGION 121 123 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT REGION 349 351 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 31 31 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 51 51 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 53 53 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00051}. FT BINDING 60 60 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00051}. FT BINDING 61 61 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 95 95 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 117 117 Substrate; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_00051}. FT BINDING 172 172 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 200 200 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 225 225 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 232 232 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 257 257 Pyridoxal phosphate; via amide nitrogen FT and carbonyl oxygen. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 357 357 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT MOD_RES 226 226 N6-(pyridoxal phosphate)lysine. FT {ECO:0000256|HAMAP-Rule:MF_00051, FT ECO:0000256|PIRSR:PIRSR000412-50}. SQ SEQUENCE 418 AA; 46040 MW; 2271670565082752 CRC64; MSALKQTDPA VYRAIRYELE RQTNQLELIA SENIVSMAVL EAQGSIFTNK YAEGYPSKRY YGGCEYADEI ESLAIDRAKE IFGAEYANVQ PHSGSQANMA VYFASLKPGD KVLGMDLAHG GHLTHGSGVN FSGQLYDFVS YGVRQDTGQI DMEAVERIAL AERPKMIVAG ASAYPRLIDF AAFRHIADKI DALFMVDMAH IAGLVAAGVH PSPVPHAHFV TTTTHKTMRG PRGGMILAKG EFDKRLNSKI FPGIQGGPLV HVIAAKAVSF KEAMTEEFRI YQEQVVKNAR ALAENLQQFS FRLVSGGTDN HLMLVDLTNK DITGKLAEEV LEDAGLTVNK NAIPFDTQSR FVTSGIRIGT PSVTTRGLQE PEMAKIAEWI NRAISNRDNK ETLAAIRLEV RMLCDQFPLY PDLVRDDD //