ID   GLYA_META3              Reviewed;         429 AA.
AC   A6UVV2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, 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.- {ECO:0000255|HAMAP-Rule:MF_00051};
GN   Name=glyA {ECO:0000255|HAMAP-Rule:MF_00051}; OrderedLocusNames=Maeo_1046;
OS   Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 /
OS   Nankai-3).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=419665;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3;
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A.,
RA   Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus aeolicus Nankai-3.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000743; ABR56624.1; -; Genomic_DNA.
DR   RefSeq; WP_011973756.1; NC_009635.1.
DR   AlphaFoldDB; A6UVV2; -.
DR   SMR; A6UVV2; -.
DR   STRING; 419665.Maeo_1046; -.
DR   EnsemblBacteria; ABR56624; ABR56624; Maeo_1046.
DR   GeneID; 5327142; -.
DR   KEGG; mae:Maeo_1046; -.
DR   eggNOG; arCOG00070; Archaea.
DR   HOGENOM; CLU_022477_2_1_2; -.
DR   OMA; SHPAGLI; -.
DR   OrthoDB; 22518at2157; -.
DR   UniPathway; UPA00288; UER01023.
DR   Proteomes; UP000001106; 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; IPR039429; SHMT-like_dom.
DR   PANTHER; PTHR11680; PTHR11680; 1.
DR   Pfam; PF00464; SHMT; 1.
DR   PIRSF; PIRSF000412; SHMT; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; One-carbon metabolism;
KW   Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..429
FT                   /note="Serine hydroxymethyltransferase"
FT                   /id="PRO_0000369971"
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   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   429 AA;  47669 MW;  ADA9E61DAA73917B CRC64;
     MNPSEVQQFV RETALKQHNW MRECIKLIAS ENITSIPVRE ACATDFMHRY AEGLPNNRLY
     QGCEYIDDIE NLCIELSEDI FKAEHANVQP TSGVVANLAV FFAEAKPGDK LMAMDVPNGG
     HISHWKVSAA GIRGLRASAH PFDAEEMNID VDKMVKQILE EKPRLVLFGG SLFPFPHPVK
     DAVDAANEVG ATIAYDGAHV LGLIAGGQFQ DPLREGAEYM MGSTHKTLFG TQGGVVLTEK
     KNAKKIDDKI FPGVVSNHHL HHKAGLAIAL AETKEFGEAY AKQVVKNAKA LGQALYERGC
     NVLCEHKGFT ESHQVILDIE KSECIEFSAR ELATMFEEAN IILNKNLLPW DDVSNSDNPS
     GIRLGSQECT RLGMKESEMD EIAEFMKRIA IDGEDIKKVK EDIVEFAKSY SEIHYAFEGG
     DAFKYLKFY