ID   GLYA_PICTO              Reviewed;         433 AA.
AC   Q6L1F6;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 105.
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=PTO0611;
OS   Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS   100828).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Picrophilaceae; Picrophilus.
OX   NCBI_TaxID=263820;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828;
RX   PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA   Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA   Schepers B., Dock C., Antranikian G., Liebl W.;
RT   "Genome sequence of Picrophilus torridus and its implications for life
RT   around pH 0.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
CC   -!- FUNCTION: Catalyzes the reversible interconversion of serine and
CC       glycine with a modified folate serving as the one-carbon carrier. Also
CC       exhibits a pteridine-independent aldolase activity toward beta-
CC       hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol
CC       mechanism. {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: 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; AE017261; AAT43196.1; -; Genomic_DNA.
DR   RefSeq; WP_011177412.1; NC_005877.1.
DR   AlphaFoldDB; Q6L1F6; -.
DR   SMR; Q6L1F6; -.
DR   STRING; 263820.PTO0611; -.
DR   EnsemblBacteria; AAT43196; AAT43196; PTO0611.
DR   GeneID; 2844844; -.
DR   KEGG; pto:PTO0611; -.
DR   PATRIC; fig|263820.9.peg.643; -.
DR   eggNOG; arCOG00070; Archaea.
DR   HOGENOM; CLU_022477_2_1_2; -.
DR   OMA; SHPAGLI; -.
DR   OrthoDB; 22518at2157; -.
DR   UniPathway; UPA00288; UER01023.
DR   Proteomes; UP000000438; 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..433
FT                   /note="Serine hydroxymethyltransferase"
FT                   /id="PRO_0000113718"
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            230
FT                   /note="Plays an important role in substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT   MOD_RES         231
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
SQ   SEQUENCE   433 AA;  48545 MW;  7667E9DD660C2278 CRC64;
     MLDNKKEYLK DAMFIRDMAM QHEQLFRESI PLIASENIMS PLAMEMLLTD LGFRYAEGLP
     HHRYYQGNEY VDVIEDKTTE LGKRLFNSKT FDPRPLSGTN ANMAVLYALT EPGDKISVPP
     LSGGGHISAA KFGAVGFRGL KTVQYPFDIN EMNIDIDGTI KTIKNERPKV CWFGQSVFLF
     PTPLKELQDA FNEVNARVVY DGAHVAGLIA GGEFQDPLRE GAEIITGSTH KTLPGPQHGM
     IIGNTDDDTW KKVQRGVFPG TLSNHHLNAM AALGVTLAEE LDFGRDYAKQ IVKNARHLGE
     KLYEFGFNVL GEKNGFTRSH TLAVDVSKNG GGRKVAENLE KSGIILNKNL LPWDDNKNSQ
     NPSGIRIGVQ EITRIGFMED DVTELAEILR DAVINEKPVN EIRRRALELK SRFNNIEYCY
     GNMKPYSYIK IFE