ID   A0A257AC01_9CREN        Unreviewed;       416 AA.
AC   A0A257AC01;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Serine hydroxymethyltransferase {ECO:0000256|HAMAP-Rule:MF_00051};
DE            Short=SHMT {ECO:0000256|HAMAP-Rule:MF_00051};
DE            Short=Serine methylase {ECO:0000256|HAMAP-Rule:MF_00051};
DE            EC=2.1.2.- {ECO:0000256|HAMAP-Rule:MF_00051};
GN   Name=glyA {ECO:0000256|HAMAP-Rule:MF_00051};
GN   ORFNames=B6U69_02640 {ECO:0000313|EMBL:OYT61950.1};
OS   Thermofilum sp. ex4484_15.
OC   Archaea; Thermoproteota; Thermoprotei; Thermofilales; Thermofilaceae;
OC   Thermofilum.
OX   NCBI_TaxID=2012526 {ECO:0000313|EMBL:OYT61950.1, ECO:0000313|Proteomes:UP000243135};
RN   [1] {ECO:0000313|EMBL:OYT61950.1, ECO:0000313|Proteomes:UP000243135}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ex4484_15 {ECO:0000313|EMBL:OYT61950.1};
RX   PubMed=28835260; DOI=.1186/s40168-017-0322-2;
RA   Dombrowski N., Seitz K.W., Teske A.P., Baker B.J.;
RT   "Genomic insights into potential interdependencies in microbial hydrocarbon
RT   and nutrient cycling in hydrothermal sediments.";
RL   Microbiome 5:106-106(2017).
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:0000256|HAMAP-Rule:MF_00051}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|HAMAP-Rule:MF_00051, ECO:0000256|PIRSR:PIRSR000412-50};
CC   -!- PATHWAY: Amino-acid biosynthesis; glycine biosynthesis; glycine from L-
CC       serine: step 1/1. {ECO:0000256|HAMAP-Rule:MF_00051}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00051}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00051}.
CC   -!- SIMILARITY: Belongs to the SHMT family. {ECO:0000256|ARBA:ARBA00006376,
CC       ECO:0000256|HAMAP-Rule:MF_00051}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00051}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OYT61950.1}.
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DR   EMBL; NJEH01000032; OYT61950.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A257AC01; -.
DR   UniPathway; UPA00288; UER01023.
DR   Proteomes; UP000243135; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
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:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:InterPro.
DR   CDD; cd00378; SHMT; 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; IPR039429; SHMT-like_dom.
DR   PANTHER; PTHR11680; SERINE HYDROXYMETHYLTRANSFERASE; 1.
DR   PANTHER; PTHR11680:SF28; SERINE HYDROXYMETHYLTRANSFERASE; 1.
DR   Pfam; PF00464; SHMT; 1.
DR   PIRSF; PIRSF000412; SHMT; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00051};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00051};
KW   Methyltransferase {ECO:0000313|EMBL:OYT61950.1};
KW   One-carbon metabolism {ECO:0000256|HAMAP-Rule:MF_00051};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00051,
KW   ECO:0000256|PIRSR:PIRSR000412-50};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00051}.
FT   DOMAIN          17..383
FT                   /note="Serine hydroxymethyltransferase-like"
FT                   /evidence="ECO:0000259|Pfam:PF00464"
FT   BINDING         117
FT                   /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57453"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   BINDING         121..123
FT                   /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57453"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   BINDING         242
FT                   /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57453"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   SITE            226
FT                   /note="Plays an important role in substrate specificity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   MOD_RES         227
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051,
FT                   ECO:0000256|PIRSR:PIRSR000412-50"
SQ   SEQUENCE   416 AA;  46290 MW;  EEBE3F35D042F65B CRC64;
     MELPGEALRI LKLNEAHNKW RREETVNLIA SENLTSPLVD SLYLSDAMHR YAEGLPFKRF
     YQGTKYIDEI EVLCEELMRK LFKAKYIDVR PISGTIANGA VFYALGKSGD TTCICPLPGG
     GHVSHSKYGI MGALGLKPLP LPFNVEEFNI DVEGASKLIK EVRPKFVVLG ASVILFPHPV
     KELGDAANEV GSKIIFDAAH VLGLIAGGKY PNPLSEGANV VTSSTHKTFP GPQGGVILTN
     EEEIYKKVKK VVFPVFVSNH HLHRLAATAM AAVEMLYFGE AYASQIIKNA KRLAECLYNR
     GFKVLGEKKG FTETHQVLLD VRELGGGTKV ALMLEKANII VNKNMLPWDR PEDIKNPSGI
     RIGVQEVTRI GMREGDMEVL AEYFYKVLIK REDPAKVAEE VREFRGKFKE LLYTFK
//