ID   GLYA_METS3              Reviewed;         422 AA.
AC   A5UMW4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=Msm_1337;
OS   Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX   NCBI_TaxID=420247;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35061 / DSM 861 / OCM 144 / PS;
RX   PubMed=17563350; DOI=10.1073/pnas.0704189104;
RA   Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., Henrissat B.,
RA   Fulton R., Latreille P., Kim K., Wilson R.K., Gordon J.I.;
RT   "Genomic and metabolic adaptations of Methanobrevibacter smithii to the
RT   human gut.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007).
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; CP000678; ABQ87542.1; -; Genomic_DNA.
DR   RefSeq; WP_004036282.1; NC_009515.1.
DR   AlphaFoldDB; A5UMW4; -.
DR   SMR; A5UMW4; -.
DR   STRING; 420247.Msm_1337; -.
DR   EnsemblBacteria; ABQ87542; ABQ87542; Msm_1337.
DR   GeneID; 5217162; -.
DR   KEGG; msi:Msm_1337; -.
DR   PATRIC; fig|420247.28.peg.1332; -.
DR   eggNOG; arCOG00070; Archaea.
DR   HOGENOM; CLU_022477_2_1_2; -.
DR   OMA; SHPAGLI; -.
DR   UniPathway; UPA00288; UER01023.
DR   Proteomes; UP000001992; 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; Transferase.
FT   CHAIN           1..422
FT                   /note="Serine hydroxymethyltransferase"
FT                   /id="PRO_0000369970"
FT   BINDING         121..123
FT                   /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57453"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT   BINDING         245
FT                   /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57453"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT   SITE            226
FT                   /note="Plays an important role in substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT   MOD_RES         227
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
SQ   SEQUENCE   422 AA;  46862 MW;  0990B581436A6DBB CRC64;
     MTDYQNEVLE FERIMKEHTN YMRNSINLIA SENITSSDVT EAVASDLAHR YAEGQSHERL
     YEGCQYIDEI EDRVIDLSKK LFNVDYANVQ PISGVTANLA AFFGYSDYGD KLMALDVPYG
     GHISHAKVSA AGIAGLKTIS HPFDKDIMNI DIDAMNKKIL EEKPKIVLFG GSLFLFPHPV
     KEAREAADEV GAKIMYDAAH VLGLIAGGQF QQPIAEGADL MMGSTHKSFP GPQGGIILSH
     KENKEVIDNA VFPGVVSNHH LHHLAGLGIA SAEMLEFGQD YAKQIVKNSK ALAQSLYERG
     FDVLCEELGF TESHQLAINV SNIRSASDIA HDLANNDVIL NKNLLPGDNV DDSDNPSGLR
     IGTQEITRRG LKEKEMDEVA EFIKRVAVDK ENIKDEVREF MDQYTTVHYS FSQNEGYRFH
     KL