ID A0A075RA07_BRELA Unreviewed; 417 AA. AC A0A075RA07; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 29-APR-2015, entry version 6. 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=BRLA_c044450 {ECO:0000313|EMBL:AIG28709.1}; OS Brevibacillus laterosporus LMG 15441. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; OC Brevibacillus. OX NCBI_TaxID=1042163 {ECO:0000313|EMBL:AIG28709.1, ECO:0000313|Proteomes:UP000005850}; RN [1] {ECO:0000313|EMBL:AIG28709.1, ECO:0000313|Proteomes:UP000005850} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LMG 15441 {ECO:0000313|EMBL:AIG28709.1}; RX PubMed=21914864; DOI=10.1128/JB.05696-11; RA Djukic M., Poehlein A., Thurmer A., Daniel R.; RT "Genome sequence of Brevibacillus laterosporus LMG 15441, a pathogen RT of invertebrates."; RL J. Bacteriol. 193:5535-5536(2011). 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 --------------------------------------------------------------------------- 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; CP007806; AIG28709.1; -; Genomic_DNA. DR ProteinModelPortal; A0A075RA07; -. DR EnsemblBacteria; AIG28709; AIG28709; BRLA_c044450. DR UniPathway; UPA00193; -. DR UniPathway; UPA00288; UER01023. DR Proteomes; UP000005850; Chromosome. 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:UP000005850}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00051}; KW Methyltransferase {ECO:0000313|EMBL:AIG28709.1}; 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:UP000005850}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00051, KW ECO:0000313|EMBL:AIG28709.1}. FT BINDING 33 33 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 53 53 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 55 55 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00051}. FT BINDING 62 62 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00051}. FT BINDING 63 63 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 119 119 Substrate; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_00051}. FT BINDING 174 174 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 202 202 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 227 227 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 234 234 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 259 259 Pyridoxal phosphate; via amide nitrogen FT and carbonyl oxygen. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT BINDING 359 359 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00051}. FT MOD_RES 228 228 N6-(pyridoxal phosphate)lysine. FT {ECO:0000256|HAMAP-Rule:MF_00051, FT ECO:0000256|PIRSR:PIRSR000412-50}. SQ SEQUENCE 417 AA; 45593 MW; 1E1E82C7C716D901 CRC64; MMFDILKEKD PQITEAIRLE LGRQRDKIEL IASENFVSRT VMEAMGTVLT NKYAEGYPGR RYYGGCEYVD IAENIARDRV KEIFGAEHAN VQPHSGAQAN MAVYFTILQP GDTVLGMNLS HGGHLTHGSS VNFSGTLYNF VEYGVDEETH LINYEIVREK ALEHKPKLIV AGASAYPREI DFAKFREIAD EIGAYLMVDM AHIAGLVAAG LHQNPVPHAH FVTSTTHKTL RGPRGGLILC KEEFAKAIDK SVFPGIQGGP LMHVIAAKAV AFGEALQPEF KEYSQRVVNN ARAFAAALQA EGLQLVSGGT DNHLVLVDVR NLELTGKVAE HLLDEVGITT NKNTIPFDPA SPFVTSGVRM GTPAVTSRGF DEEAMKEVAG IIALTLKNPE DQAKHAEARE RVAALNKKFP LYEGLSI //