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Database: UniProt
Entry: A0A0B9AND2_BRELN
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ID   A0A0B9AND2_BRELN        Unreviewed;       453 AA.
AC   A0A0B9AND2;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 40.
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=AE0388_2922 {ECO:0000313|EMBL:KHS50850.1};
OS   Brevibacterium linens.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Brevibacteriaceae;
OC   Brevibacterium.
OX   NCBI_TaxID=1703 {ECO:0000313|EMBL:KHS50850.1, ECO:0000313|Proteomes:UP000031488};
RN   [1] {ECO:0000313|EMBL:KHS50850.1, ECO:0000313|Proteomes:UP000031488}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AE038-8 {ECO:0000313|EMBL:KHS50850.1,
RC   ECO:0000313|Proteomes:UP000031488};
RA   Maizel D., Utturkar S.M., Brown S.D., Ferrero M., Rosen B.P.;
RT   "Draft Genome Sequence of Brevibacterium linens AE038-8.";
RL   Submitted (NOV-2014) 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|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|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:KHS50850.1}.
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DR   EMBL; JTJZ01000022; KHS50850.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B9AND2; -.
DR   PATRIC; fig|1703.6.peg.2870; -.
DR   OMA; GWLCDVL; -.
DR   OrthoDB; 9803846at2; -.
DR   UniPathway; UPA00193; -.
DR   UniPathway; UPA00288; UER01023.
DR   Proteomes; UP000031488; 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:UniProtKB-UniPathway.
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; IPR019798; Ser_HO-MeTrfase_PLP_BS.
DR   InterPro; IPR039429; SHMT-like_dom.
DR   PANTHER; PTHR11680; SERINE HYDROXYMETHYLTRANSFERASE; 1.
DR   PANTHER; PTHR11680:SF28; SERINE HYDROXYMETHYLTRANSFERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00464; SHMT; 1.
DR   PIRSF; PIRSF000412; SHMT; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00096; SHMT; 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:KHS50850.1};
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}; Reference proteome {ECO:0000313|Proteomes:UP000031488};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00051}.
FT   DOMAIN          28..409
FT                   /note="Serine hydroxymethyltransferase-like"
FT                   /evidence="ECO:0000259|Pfam:PF00464"
FT   BINDING         140
FT                   /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57453"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   BINDING         144..146
FT                   /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57453"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   SITE            248
FT                   /note="Plays an important role in substrate specificity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051"
FT   MOD_RES         249
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00051,
FT                   ECO:0000256|PIRSR:PIRSR000412-50"
SQ   SEQUENCE   453 AA;  48017 MW;  35848DAFB3F9C6FB CRC64;
     MTEQLAHPAD VAEAFPGREP VELNTSIAEL DPQIAGFIDA ELARQREGLE MIASENHTAS
     AVMEAQGSVL TNKYAEGYPG RRYYGGCEHV DEIERIAIDR VKALFGAAYA NVQPHSGAQA
     NASVMHALIR PGDTVLGLNL AHGGHLTHGM KINFSGRLYS IVPYGLDPET GRVDMAEVER
     LAHENQPKLI VAGWSAYTRR LDFAEFRRIA DAVGAYLMVD MAHFAGLVAA GLHPSPVPHA
     HVVSSTTHKT LGGPRGGIIL TNDADIAKKI NSAVFPGQQG GPLEHVIAGK AVAFGLAATD
     TFVDKQKRTL AGAGELARRL TEDDVAERGI SVLTGGTDVH LVLVDLRNST LDGAQAEDLL
     AQIGITVNRN AVPDDPRPPM VTSGLRIGTP ALASRGFGSE AFAEAADIIA EVLKAGTDES
     GASPEIIAEL SERVTRLAND HPLYPTLTEI GAR
//
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