ID   A0A223ERS7_9BACI        Unreviewed;       412 AA.
AC   A0A223ERS7;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   07-OCT-2020, entry version 7.
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=2.1.2.1 {ECO:0000256|HAMAP-Rule:MF_00051};
GN   Name=glyA {ECO:0000256|HAMAP-Rule:MF_00051};
GN   ORFNames=GT3921_02115 {ECO:0000313|EMBL:ASS97956.1};
OS   Geobacillus thermocatenulatus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   Geobacillus thermoleovorans group.
OX   NCBI_TaxID=33938 {ECO:0000313|EMBL:ASS97956.1, ECO:0000313|Proteomes:UP000214728};
RN   [1] {ECO:0000313|EMBL:ASS97956.1, ECO:0000313|Proteomes:UP000214728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 3921 {ECO:0000313|EMBL:ASS97956.1,
RC   ECO:0000313|Proteomes:UP000214728};
RA   Lee Y.-J., Park M.-K., Yi H., Bahn Y.-S., Kim J.F., Lee D.-W.;
RT   "The whole genome sequencing and assembly of Geobacillus thermocatenulatus
RT   KCTC 3921 strain.";
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible interconversion of serine and
CC       glycine with tetrahydrofolate (THF) serving as the one-carbon carrier.
CC       This reaction serves as the major source of one-carbon groups required
CC       for the biosynthesis of purines, thymidylate, methionine, and other
CC       important biomolecules. Also exhibits THF-independent aldolase activity
CC       toward beta-hydroxyamino acids, producing glycine and aldehydes, via a
CC       retro-aldol mechanism. {ECO:0000256|HAMAP-Rule:MF_00051}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O =
CC         (6S)-5,6,7,8-tetrahydrofolate + L-serine; Xref=Rhea:RHEA:15481,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, ChEBI:CHEBI:33384,
CC         ChEBI:CHEBI:57305, ChEBI:CHEBI:57453; EC=2.1.2.1;
CC         Evidence={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|ARBA:ARBA00004697, ECO:0000256|HAMAP-
CC       Rule:MF_00051}.
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC       {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}.
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DR   EMBL; CP018058; ASS97956.1; -; Genomic_DNA.
DR   RefSeq; WP_015376066.1; NZ_NEWK01000001.1.
DR   KEGG; gtm:GT3921_02115; -.
DR   KO; K00600; -.
DR   UniPathway; UPA00193; -.
DR   UniPathway; UPA00288; UER01023.
DR   Proteomes; UP000214728; Chromosome.
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:UniProtKB-UniPathway.
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; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
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 {ECO:0000256|HAMAP-Rule:MF_00051};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00051};
KW   Methyltransferase {ECO:0000313|EMBL:ASS97956.1};
KW   One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563, ECO:0000256|HAMAP-
KW   Rule:MF_00051};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW   Rule:MF_00051, ECO:0000256|PIRSR:PIRSR000412-50};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00051, ECO:0000313|EMBL:ASS97956.1}.
FT   DOMAIN          5..380
FT                   /note="SHMT"
FT                   /evidence="ECO:0000259|Pfam:PF00464"
FT   REGION          121..123
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   REGION          349..351
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   COILED          386..412
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         31
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   BINDING         51
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   BINDING         53
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   BINDING         60
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   BINDING         61
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   BINDING         117
FT                   /note="Substrate; via carbonyl oxygen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   BINDING         172
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   BINDING         200
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   BINDING         225
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   BINDING         232
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   BINDING         257
FT                   /note="Pyridoxal phosphate; via amide nitrogen and carbonyl
FT                   oxygen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   BINDING         357
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   MOD_RES         226
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051,
FT                   ECO:0000256|PIRSR:PIRSR000412-50"
SQ   SEQUENCE   412 AA;  45183 MW;  7DDD341901692C12 CRC64;
     MNYLPQQDPQ VFAAIEQERK RQHAKIELIA SENFVSRAVM EAQGSVLTNK YAEGYPGRRY
     YGGCEYVDIV EELARERAKQ LFGAEHANVQ PHSGAQANMA VYFTVLEHGD TVLGMNLSHG
     GHLTHGSPVN FSGIQYHFVE YGVDPKTHVI DYDDVREKAR LHRPKLIVAG ASAYPRIIDF
     AKFREIADEV GAYLMVDMAH IAGLVAAGVH PNPVPYAHFV TTTTHKTLRG PRGGMILCQE
     QFAKQIDKAI FPGIQGGPLM HVIAAKAVAL GEALQDDFKV YAKRVVENAK RLAAALQNEG
     FTLISGGTDN HLLLVDLRPQ QLTGKTAEKV LDEVGITVNK NTIPYDPESP FVTSGIRIGT
     AAVTTRGFGL EEMDEIAAII GLVLKNVGSE QALEEARQRV AALTEKFPLY QD
//