ID A1R450_PAEAT Unreviewed; 430 AA. AC A1R450; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 24-JUL-2024, entry version 138. 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 ECO:0000313|EMBL:ABM08285.1}; GN OrderedLocusNames=AAur_1227 {ECO:0000313|EMBL:ABM08285.1}; OS Paenarthrobacter aurescens (strain TC1). OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae; OC Paenarthrobacter. OX NCBI_TaxID=290340 {ECO:0000313|EMBL:ABM08285.1, ECO:0000313|Proteomes:UP000000637}; RN [1] {ECO:0000313|EMBL:ABM08285.1, ECO:0000313|Proteomes:UP000000637} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TC1 {ECO:0000313|EMBL:ABM08285.1, RC ECO:0000313|Proteomes:UP000000637}; RX PubMed=17194220; DOI=10.1371/journal.pgen.0020214; RA Mongodin E.F., Shapir N., Daugherty S.C., DeBoy R.T., Emerson J.B., RA Shvartzbeyn A., Radune D., Vamathevan J., Riggs F., Grinberg V., Khouri H., RA Wackett L.P., Nelson K.E., Sadowsky M.J.; RT "Secrets of soil survival revealed by the genome sequence of Arthrobacter RT aurescens TC1."; RL PLoS Genet. 2:2094-2106(2006). 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|ARBA:ARBA00011738, ECO:0000256|HAMAP- CC 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; CP000474; ABM08285.1; -; Genomic_DNA. DR AlphaFoldDB; A1R450; -. DR SMR; A1R450; -. DR STRING; 290340.AAur_1227; -. DR KEGG; aau:AAur_1227; -. DR eggNOG; COG0112; Bacteria. DR HOGENOM; CLU_022477_2_1_11; -. DR UniPathway; UPA00193; -. DR UniPathway; UPA00288; UER01023. DR Proteomes; UP000000637; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0050897; F:cobalt ion binding; IEA:TreeGrafter. 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:0070905; F:serine binding; IEA:TreeGrafter. DR GO; GO:0008270; F:zinc ion binding; IEA:TreeGrafter. DR GO; GO:0046655; P:folic acid metabolic process; IEA:TreeGrafter. DR GO; GO:0019264; P:glycine biosynthetic process from serine; IEA:UniProtKB-UniRule. DR GO; GO:0006565; P:L-serine catabolic process; IEA:TreeGrafter. 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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1. DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1. DR HAMAP; MF_00051; SHMT; 1. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small. DR InterPro; IPR001085; Ser_HO-MeTrfase. DR InterPro; IPR049943; Ser_HO-MeTrfase-like. DR InterPro; IPR019798; Ser_HO-MeTrfase_PLP_BS. DR InterPro; IPR039429; SHMT-like_dom. DR PANTHER; PTHR11680; SERINE HYDROXYMETHYLTRANSFERASE; 1. DR PANTHER; PTHR11680:SF28; SERINE HYDROXYMETHYLTRANSFERASE; 1. DR Pfam; PF00464; SHMT; 1. DR PIRSF; PIRSF000412; SHMT; 1. DR SUPFAM; SSF53383; PLP-dependent transferases; 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|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00051}; KW Methyltransferase {ECO:0000313|EMBL:ABM08285.1}; KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563, ECO:0000256|HAMAP- KW 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 14..395 FT /note="Serine hydroxymethyltransferase-like" FT /evidence="ECO:0000259|Pfam:PF00464" FT BINDING 127 FT /ligand="(6S)-5,6,7,8-tetrahydrofolate" FT /ligand_id="ChEBI:CHEBI:57453" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 131..133 FT /ligand="(6S)-5,6,7,8-tetrahydrofolate" FT /ligand_id="ChEBI:CHEBI:57453" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT SITE 235 FT /note="Plays an important role in substrate specificity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT MOD_RES 236 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051, FT ECO:0000256|PIRSR:PIRSR000412-50" SQ SEQUENCE 430 AA; 46054 MW; C477D9DDA44314E8 CRC64; MTTTTSASVS NQSLADLDPE IAAVLNQELG RQRGTLEMIA SENFAPRAVM EAQGSVLTNK YAEGYPGRRY YGGCEYVDVA EQLAIDRVKE LFGAEYANVQ PHSGAQANAA ALSAMITPGD KILGLSLAHG GHLTHGMKLN FSGKLYNVAA YQVEEDNFRI DMDKLREQAI AEKPQVIIAG WSAYPRHLDF AAFRSIADEV GALLWTDMAH FAGLVAAGLH PSPVPHSDVV TSTVHKTLAG PRSGVILGKQ EWAKKLNSSV FPGQQGGPLM HVIAAKAVAF KIAGGEEFKE RQERVLEGAR IIADRLNQSD VAEAGVSVLT GGTDVHLVLV DLRNSQLDGQ QAEDLLHSVG ITVNRNAVPF DPRPPMVTSG LRIGTPALAT RGFGATEFTE VAEIIATALK AGSSADVESL QARVDKLAAD FPLYPQHEQW //