ID   GLYA_SHESH              Reviewed;         418 AA.
AC   A8FSQ9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   02-SEP-2026, entry version 102.
DE   RecName: Full=Serine hydroxymethyltransferase {ECO:0000255|HAMAP-Rule:MF_00051};
DE            Short=SHMT {ECO:0000255|HAMAP-Rule:MF_00051};
DE            Short=Serine methylase {ECO:0000255|HAMAP-Rule:MF_00051};
DE            EC=2.1.2.1 {ECO:0000255|HAMAP-Rule:MF_00051};
GN   Name=glyA {ECO:0000255|HAMAP-Rule:MF_00051};
GN   OrderedLocusNames=Ssed_1271;
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Alteromonadales; Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) 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 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:0000255|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:0000255|HAMAP-Rule:MF_00051};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00051};
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC       {ECO:0000255|HAMAP-Rule:MF_00051}.
CC   -!- PATHWAY: Amino-acid biosynthesis; glycine biosynthesis; glycine from L-
CC       serine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00051}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00051}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00051}.
CC   -!- SIMILARITY: Belongs to the SHMT family. {ECO:0000255|HAMAP-
CC       Rule:MF_00051}.
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DR   EMBL; CP000821; ABV35882.1; -; Genomic_DNA.
DR   RefSeq; WP_012141618.1; NC_009831.1.
DR   AlphaFoldDB; A8FSQ9; -.
DR   SMR; A8FSQ9; -.
DR   STRING; 425104.Ssed_1271; -.
DR   KEGG; sse:Ssed_1271; -.
DR   eggNOG; COG0112; Bacteria.
DR   HOGENOM; CLU_022477_2_1_6; -.
DR   OrthoDB; 9803846at2; -.
DR   UniPathway; UPA00193; -.
DR   UniPathway; UPA00288; UER01023.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006545; P:glycine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniRule.
DR   CDD; cd00378; SHMT; 1.
DR   FunFam; 3.40.640.10:FF:000001; Serine hydroxymethyltransferase; 1.
DR   FunFam; 3.90.1150.10:FF:000003; Serine hydroxymethyltransferase; 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   NCBIfam; NF000586; PRK00011.1; 1.
DR   PANTHER; PTHR11680; SERINE HYDROXYMETHYLTRANSFERASE; 1.
DR   PANTHER; PTHR11680:SF50; 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; Cytoplasm; One-carbon metabolism;
KW   Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..418
FT                   /note="Serine hydroxymethyltransferase"
FT                   /id="PRO_1000074910"
FT   BINDING         121
FT                   /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57453"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT   BINDING         125..127
FT                   /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57453"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT   BINDING         356..358
FT                   /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57453"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT   SITE            229
FT                   /note="Plays an important role in substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT   MOD_RES         230
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
SQ   SEQUENCE   418 AA;  45262 MW;  1B5180C2B523B598 CRC64;
     MLKKDMNIAD FDPQLFQAIA DETRRQEEHI ELIASENYTS PRVLEAQGSQ LTNKYAEGYP
     GKRYYGGCEH VDIAEELAIS RAKELFGATY ANVQPHSGSQ ANSAVFMALL QGGDTVLGMS
     LAHGGHLTHG SHVSFSGKLY NAVQYGIDEA TGKIDYAEVE RLAVEHKPKM IIAGFSAYSG
     IIDWGKFREI ADKVGAYLFV DMAHVAGLVA AGIYPNPLPH AHVVTTTTHK TLAGPRGGLI
     LSACDDEAIY KKLNSAVFPG GQGGPLMHVI AAKAVAFKEA LEPEFTAYQE QVVVNAKAMA
     KTFIERGYDV VSGGTDNHLF LLDLISKDIT GKDADAALGL ANITVNKNSV PNDPRSPFVT
     SGLRIGSPAI TRRGFKEEQS VELTNWMCDV LDDITDQGTI ERVKNQVLEL CARFPVYG
//