ID A1R450_PAEAT Unreviewed; 430 AA. AC A1R450; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 13-FEB-2019, entry version 108. 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; 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., RA Khouri H., Wackett L.P., Nelson K.E., Sadowsky M.J.; RT "Secrets of soil survival revealed by the genome sequence of RT Arthrobacter 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 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 --------------------------------------------------------------------------- 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 ProteinModelPortal; A1R450; -. DR SMR; A1R450; -. DR STRING; 290340.AAur_1227; -. DR EnsemblBacteria; ABM08285; ABM08285; AAur_1227. DR KEGG; aau:AAur_1227; -. DR eggNOG; ENOG4105C65; Bacteria. DR eggNOG; COG0112; LUCA. DR HOGENOM; HOG000239404; -. DR KO; K00600; -. 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: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 Complete proteome {ECO:0000313|Proteomes:UP000000637}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00051}; KW Methyltransferase {ECO:0000313|EMBL:ABM08285.1}; 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:UP000000637}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00051, KW ECO:0000313|EMBL:ABM08285.1}. FT DOMAIN 14 395 SHMT. {ECO:0000259|Pfam:PF00464}. FT REGION 131 133 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT COILED 148 168 {ECO:0000256|SAM:Coils}. FT BINDING 41 41 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 61 61 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 63 63 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00051}. FT BINDING 70 70 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00051}. FT BINDING 71 71 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 127 127 Substrate; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_00051}. FT BINDING 182 182 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 210 210 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 235 235 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 242 242 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 267 267 Pyridoxal phosphate; via amide nitrogen FT and carbonyl oxygen. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 372 372 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT MOD_RES 236 236 N6-(pyridoxal phosphate)lysine. FT {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 //