ID   A0A223ERS7_9BACI        Unreviewed;       412 AA.
AC   A0A223ERS7;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   05-JUN-2019, entry version 3.
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
RT   thermocatenulatus 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
CC       carrier. This reaction serves as the major source of one-carbon
CC       groups required for the biosynthesis of purines, thymidylate,
CC       methionine, and other important biomolecules. Also exhibits THF-
CC       independent aldolase activity toward beta-hydroxyamino acids,
CC       producing glycine and aldehydes, via a retro-aldol mechanism.
CC       {ECO:0000256|HAMAP-Rule:MF_00051}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine +
CC         H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine;
CC         Xref=Rhea:RHEA:15481, ChEBI:CHEBI:15377, ChEBI:CHEBI:15636,
CC         ChEBI:CHEBI:33384, ChEBI:CHEBI:57305, ChEBI:CHEBI:57453;
CC         EC=2.1.2.1; Evidence={ECO:0000256|HAMAP-Rule:MF_00051};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00051,
CC         ECO:0000256|PIRSR:PIRSR000412-50};
CC   -!- PATHWAY: Amino-acid biosynthesis; glycine biosynthesis; glycine
CC       from L-serine: step 1/1. {ECO:0000256|HAMAP-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|HAMAP-
CC       Rule:MF_00051}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of 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   BioCyc; GCF_002243665:GT3921_RS02180-MONOMER; -.
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: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   Complete proteome {ECO:0000313|Proteomes:UP000214728};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00051};
KW   Methyltransferase {ECO:0000313|EMBL:ASS97956.1};
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|HAMAP-Rule:MF_00051,
KW   ECO:0000313|EMBL:ASS97956.1}.
FT   DOMAIN        5    380       SHMT. {ECO:0000259|Pfam:PF00464}.
FT   REGION      121    123       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   REGION      349    351       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   COILED      386    412       {ECO:0000256|SAM:Coils}.
FT   BINDING      31     31       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING      51     51       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING      53     53       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00051}.
FT   BINDING      60     60       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00051}.
FT   BINDING      61     61       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     117    117       Substrate; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00051}.
FT   BINDING     172    172       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     200    200       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     225    225       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     232    232       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     257    257       Pyridoxal phosphate; via amide nitrogen
FT                                and carbonyl oxygen. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     357    357       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00051}.
FT   MOD_RES     226    226       N6-(pyridoxal phosphate)lysine.
FT                                {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
//