ID A0A0F5P5Y2_9SPHN Unreviewed; 438 AA. AC A0A0F5P5Y2; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 08-JUN-2016, entry version 7. 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:KKC23890.1}; GN ORFNames=WP12_22355 {ECO:0000313|EMBL:KKC23890.1}; OS Sphingomonas sp. SRS2. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingomonas. OX NCBI_TaxID=133190 {ECO:0000313|EMBL:KKC23890.1, ECO:0000313|Proteomes:UP000033680}; RN [1] {ECO:0000313|EMBL:KKC23890.1, ECO:0000313|Proteomes:UP000033680} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SRS2 {ECO:0000313|EMBL:KKC23890.1, RC ECO:0000313|Proteomes:UP000033680}; RA Nielsen T.K., Sorensen S.R., Hansen L.H.; RT "Draft genome sequence of isoproturon-mineralizing Sphingomonas sp. RT SRS2, isolated from an agricultural field in the United Kingdom."; RL Submitted (MAR-2015) 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: 5,10-methylenetetrahydrofolate + glycine + CC H(2)O = tetrahydrofolate + L-serine. {ECO:0000256|HAMAP- CC 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, ECO:0000256|RuleBase:RU004104}. 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:KKC23890.1}. 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; LARW01000157; KKC23890.1; -; Genomic_DNA. DR RefSeq; WP_046195857.1; NZ_LARW01000157.1. DR EnsemblBacteria; KKC23890; KKC23890; WP12_22355. DR Proteomes; UP000033680; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-HAMAP. DR GO; GO:0019264; P:glycine biosynthetic process from serine; IEA:UniProtKB-HAMAP. DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway. 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; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR InterPro; IPR001085; Ser_HO-MeTrfase. DR InterPro; IPR019798; Ser_HO-MeTrfase_PLP_BS. 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 Complete proteome {ECO:0000313|Proteomes:UP000033680}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00051}; KW Methyltransferase {ECO:0000313|EMBL:KKC23890.1}; 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:UP000033680}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00051, KW ECO:0000313|EMBL:KKC23890.1}. FT BINDING 49 49 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 69 69 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 71 71 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00051}. FT BINDING 78 78 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00051}. FT BINDING 79 79 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 135 135 Substrate; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_00051}. FT BINDING 190 190 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 218 218 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 243 243 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 250 250 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 276 276 Pyridoxal phosphate; via amide nitrogen FT and carbonyl oxygen. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 376 376 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT MOD_RES 244 244 N6-(pyridoxal phosphate)lysine. FT {ECO:0000256|HAMAP-Rule:MF_00051, FT ECO:0000256|PIRSR:PIRSR000412-50}. SQ SEQUENCE 438 AA; 46398 MW; 1EC9E5C1868D81F2 CRC64; MSSNPAANLS DVQPDGFFTR GLAQADPAVF GGLQAEVTRE KKQIELIASE NIVSKAVLEA QGSVFTNKYA EGYPGKRYYQ GCHPSDVVEQ LAIDRAKQLF GCGFVNVQPH SGAQANGAVM LALTKPGDTI MGLSLDAGGH LTHGARAAMS GKWYNAIQYG VRPDDHRIDF DQVEALAREH KPTLIITGGS AYPRHIDFAR FRAIADEVGA IFMVDMAHFA GLVAGGVHPT PFGHAHVVTT TTHKTLRGPR GGMIMTDDEA IAKKINSAVF PGLQGGPLMH VIAAKAVAFG EALQPDFKLY AAAVVENAKV LAARLKERGA DLVSGGTDTH LALVDLRPIG VTGRDADEAL ERAGITCNKN GVPNDPLPPV KTSGIRVGSP AGTTRGFGPA EFRDIADMIA DVLDGLAKNG PEGNGQTEAH VKERVEALCD RFPIYPEL //