ID   GLYA_METST              Reviewed;         422 AA.
AC   Q2NEA8;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 94.
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.- {ECO:0000255|HAMAP-Rule:MF_00051};
GN   Name=glyA {ECO:0000255|HAMAP-Rule:MF_00051}; OrderedLocusNames=Msp_1475;
OS   Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 /
OS   MCB-3).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX   NCBI_TaxID=339860;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3;
RX   PubMed=16385054; DOI=10.1128/jb.188.2.642-658.2006;
RA   Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., Hedderich R.,
RA   Gottschalk G., Thauer R.K.;
RT   "The genome sequence of Methanosphaera stadtmanae reveals why this human
RT   intestinal archaeon is restricted to methanol and H2 for methane formation
RT   and ATP synthesis.";
RL   J. Bacteriol. 188:642-658(2006).
CC   -!- FUNCTION: Catalyzes the reversible interconversion of serine and
CC       glycine with tetrahydromethanopterin (H4MPT) serving as the one-carbon
CC       carrier. Also exhibits a pteridine-independent aldolase activity toward
CC       beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-
CC       aldol mechanism. {ECO:0000255|HAMAP-Rule:MF_00051}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5,10-methylenetetrahydromethanopterin + glycine + H2O =
CC         5,6,7,8-tetrahydromethanopterin + L-serine; Xref=Rhea:RHEA:47104,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57305,
CC         ChEBI:CHEBI:57818, ChEBI:CHEBI:58103; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00051};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={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; CP000102; ABC57845.1; -; Genomic_DNA.
DR   RefSeq; WP_011407044.1; NC_007681.1.
DR   AlphaFoldDB; Q2NEA8; -.
DR   SMR; Q2NEA8; -.
DR   STRING; 339860.Msp_1475; -.
DR   EnsemblBacteria; ABC57845; ABC57845; Msp_1475.
DR   GeneID; 41326048; -.
DR   KEGG; mst:Msp_1475; -.
DR   eggNOG; arCOG00070; Archaea.
DR   HOGENOM; CLU_022477_2_1_2; -.
DR   OMA; SHPAGLI; -.
DR   OrthoDB; 22518at2157; -.
DR   UniPathway; UPA00288; UER01023.
DR   Proteomes; UP000001931; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0019264; P:glycine biosynthetic process from serine; IEA:UniProtKB-UniRule.
DR   GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:InterPro.
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; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
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; Cytoplasm; One-carbon metabolism;
KW   Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..422
FT                   /note="Serine hydroxymethyltransferase"
FT                   /id="PRO_0000235054"
FT   BINDING         120..122
FT                   /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57453"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT   BINDING         241
FT                   /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57453"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT   SITE            225
FT                   /note="Plays an important role in substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT   MOD_RES         226
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
SQ   SEQUENCE   422 AA;  46447 MW;  A741596C970F2876 CRC64;
     MSNLEQAERI KNLTKDHHNW MKNSLNLIAS ENITSRAVRE AVASDLSHRY AEGLPGERLY
     EGCDYIDAIE EETIALSKKL YDAEHVNVQP TSGVVANLAS FFALTKPGDL LMSINVPEGG
     HISHASVSAA GIRGLKISSV PMDDSIMNVD IDKTLSKIRE KEPKAIVLGG SLFLFPQPVS
     EVADVAKEVG AKIIYDAAHV LGLIAGKRFQ DPVKEGADIV TGSTHKTFPG PQGGIILCKE
     EIGRKVDNCV FPGVVSNHHL HHMAALGVAT AEMLEFGKDY ANQTISNAKA LAQALYERGF
     NVLCEDQGFT ESHQVAMDVA KLGDVSKMAK TLQYNNIILN KNLLPWDDVN DSDNPSGIRM
     GTQELTHRGF KEDEMDQVAE FIKQVVMDKK DVKEDVTEFM QDYTTVHYAF DEGCEGYDYI
     EF