ID A1R450_PAEAT Unreviewed; 430 AA. AC A1R450; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 10-FEB-2021, entry version 124. 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; Actinobacteria; Micrococcales; Micrococcaceae; 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|ARBA:ARBA00004697, ECO:0000256|HAMAP- CC 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; CP000474; ABM08285.1; -; Genomic_DNA. DR SMR; A1R450; -. DR STRING; 290340.AAur_1227; -. DR EnsemblBacteria; ABM08285; ABM08285; AAur_1227. DR KEGG; aau:AAur_1227; -. DR eggNOG; COG0112; Bacteria. DR HOGENOM; CLU_022477_2_1_11; -. DR OMA; PLEHIIA; -. DR UniPathway; UPA00193; -. DR UniPathway; UPA00288; UER01023. DR Proteomes; UP000000637; Chromosome. 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:0032259; P:methylation; IEA:UniProtKB-KW. 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 Coiled coil {ECO:0000256|SAM:Coils}; KW Cytoplasm {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, ECO:0000256|PIRSR:PIRSR000412-50}; KW Reference proteome {ECO:0000313|Proteomes:UP000000637}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00051, ECO:0000313|EMBL:ABM08285.1}. FT DOMAIN 14..395 FT /note="SHMT" FT /evidence="ECO:0000259|Pfam:PF00464" FT REGION 131..133 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT COILED 148..168 FT /evidence="ECO:0000256|SAM:Coils" FT BINDING 41 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 61 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 63 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 70 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 71 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 127 FT /note="Substrate; via carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 182 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 210 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 235 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 242 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 267 FT /note="Pyridoxal phosphate; via amide nitrogen and carbonyl FT oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00051" FT BINDING 372 FT /note="Pyridoxal phosphate" 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 //