ID   GLYA_ACIET              Reviewed;         414 AA.
AC   B9MAC8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   02-SEP-2026, entry version 86.
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=Dtpsy_2044;
OS   Acidovorax ebreus (strain TPSY) (Diaphorobacter sp. (strain TPSY)).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC   Burkholderiales; Comamonadaceae; Diaphorobacter.
OX   NCBI_TaxID=535289;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TPSY;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Coates J.D.;
RT   "Complete sequence of Diaphorobacter sp. TPSY.";
RL   Submitted (JAN-2009) 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; CP001392; ACM33500.1; -; Genomic_DNA.
DR   RefSeq; WP_011804931.1; NC_011992.1.
DR   AlphaFoldDB; B9MAC8; -.
DR   SMR; B9MAC8; -.
DR   KEGG; dia:Dtpsy_2044; -.
DR   eggNOG; COG0112; Bacteria.
DR   HOGENOM; CLU_022477_2_1_4; -.
DR   UniPathway; UPA00193; -.
DR   UniPathway; UPA00288; UER01023.
DR   Proteomes; UP000000450; 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..414
FT                   /note="Serine hydroxymethyltransferase"
FT                   /id="PRO_1000195444"
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   SITE            228
FT                   /note="Plays an important role in substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT   MOD_RES         229
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
SQ   SEQUENCE   414 AA;  45233 MW;  143BA06E78BBF18A CRC64;
     MYQRNILVEQ TDPEVWAAIQ AEDRRQEEHI ELIASENYAS PAVMAAQGSQ LTNKYAEGYP
     GKRYYGGCEN VDVIEQLAID RIKQLFGAEA ANVQPNSGSQ ANQAVLMAFL KPGDTILGMS
     LAEGGHLTHG MPLNMSGKWF NVVSYGLNDK EEIDYDALEA KAREHKPKLI IAGASAYALR
     IDFERFAKIA KEVGAIFWVD IAHYAGLVVA GEYPNPVPFA DVVTSTTHKS LRGPRGGIIL
     MKAEHEKAIN SAIFPGLQGG PLEHVIAAKA VAFKEALSPE FKQYQQQVTK NAKVFAETLI
     QRGLRIVSGR TESHVMLVDL RAKGITGKEA EAALGKAHIT INKNAIPNDP EKPMVTSGIR
     VGTPAITTRG FKEEETRLTA NLVADVLDNP HDEANLEAVR AKVHALTSRF PVYR
//