ID M3FQ95_9ACTN Unreviewed; 412 AA. AC M3FQ95; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 01-MAY-2013, sequence version 1. DT 07-APR-2021, entry version 36. 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=SBD_3957 {ECO:0000313|EMBL:EMF54289.1}; OS Streptomyces bottropensis ATCC 25435. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1054862 {ECO:0000313|EMBL:EMF54289.1, ECO:0000313|Proteomes:UP000030760}; RN [1] {ECO:0000313|Proteomes:UP000030760} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25435 {ECO:0000313|Proteomes:UP000030760}; RX PubMed=23516178; RA Zhang H., Zhou W., Zhuang Y., Liang X., Liu T.; RT "Draft Genome Sequence of Streptomyces bottropensis ATCC 25435, a RT Bottromycin-Producing Actinomycete."; RL Genome Announc. Announc.1:E0001913-E0001913(2013). 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 --------------------------------------------------------------------------- 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; KB405078; EMF54289.1; -; Genomic_DNA. DR RefSeq; WP_005480264.1; NZ_KB911581.1. DR EnsemblBacteria; EMF54289; EMF54289; SBD_3957. DR UniPathway; UPA00193; -. DR UniPathway; UPA00288; UER01023. DR Proteomes; UP000030760; 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: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; IPR039429; SHMT-like_dom. DR PANTHER; PTHR11680; PTHR11680; 1. DR Pfam; PF00464; SHMT; 1. DR PIRSF; PIRSF000412; SHMT; 1. DR SUPFAM; SSF53383; SSF53383; 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 One-carbon metabolism {ECO:0000256|HAMAP-Rule:MF_00051}; KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP- KW Rule:MF_00051}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00051}. FT DOMAIN 13..381 FT /note="SHMT" FT /evidence="ECO:0000259|Pfam:PF00464" FT REGION 129..131 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 59 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 61 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 103 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 125 FT /note="Substrate; via carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 208 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 233 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 240 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 265 FT /note="Pyridoxal phosphate; via amide nitrogen and carbonyl FT oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 360 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT MOD_RES 234 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051, FT ECO:0000256|PIRSR:PIRSR000412-50" SQ SEQUENCE 412 AA; 43349 MW; 2559BCD9AEB4963D CRC64; MSVTPVLEAD VLRRQDPELA DVLLGEQDRQ ATTLQLVAAE NFTSPAVLAA LGSPLANKYA EGYPGARHHG GCEMVDVAER LAVERARSLF GAEHANVQSH SGSSAVLAAY AALLRPGDTV LAMGLHFGGH LTHGSPANFS GRWFDFVGYG VEAESGLIDR EQVRTLARTH RPKALVCGSI SYPRHIDYAF FREVADEVGA YLIVDAAHPI GLVAGGAAPN PVPYADIVCA TTHKVLRGPR GGMLLCGDEL AERVDRAVFP FTQGGAQMHT IAAKAVAFGE AATPAFTAYA HQVVANARVL ARGLAEEGLV VVTGGTDTHL LTVDPAPLGV DGRTARGRLA AAGMVLDCCA LPHDDARGLR LGTAALTTQG MGETEMARLA VLFAGALRDG GNGKRTREEV RELAGRFPPY PR //