ID A0A0F9YPT1_9BACT Unreviewed; 341 AA.
AC A0A0F9YPT1;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Serine hydroxymethyltransferase {ECO:0000313|EMBL:KKP33378.1};
GN ORFNames=UR23_C0045G0004 {ECO:0000313|EMBL:KKP33378.1};
OS Candidatus Roizmanbacteria bacterium GW2011_GWA2_32_13.
OC Bacteria; Candidatus Roizmanbacteria.
OX NCBI_TaxID=1618475 {ECO:0000313|EMBL:KKP33378.1, ECO:0000313|Proteomes:UP000034349};
RN [1] {ECO:0000313|EMBL:KKP33378.1, ECO:0000313|Proteomes:UP000034349}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR000412-50};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the SHMT family.
CC {ECO:0000256|ARBA:ARBA00006376}.
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:KKP33378.1}.
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DR EMBL; LBOK01000045; KKP33378.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F9YPT1; -.
DR PATRIC; fig|1618475.3.peg.490; -.
DR Proteomes; UP000034349; Unassembled WGS sequence.
DR GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IEA:InterPro.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019264; P:glycine biosynthetic process from serine; IEA:InterPro.
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 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; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Methyltransferase {ECO:0000313|EMBL:KKP33378.1};
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000412-50};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KKP33378.1}.
FT DOMAIN 3..339
FT /note="Serine hydroxymethyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF00464"
FT MOD_RES 224
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000412-50"
SQ SEQUENCE 341 AA; 38077 MW; 3938424615205A92 CRC64;
MNQNLQSLLK KEEQRQKEFI NLIASENYPS DDVTRYSGNI LANKYAEGYP GRRYYPGLEI
IDEIENICQK EALKTFGLDS KEWHSNVQPY SGGVANAEIY LALLEFGDKI LGMNLTHGGH
LSHGHKANIS SRAYKAIAYG LNSKTNLIDY DEIERLAISE KPKLIIAGAS AYPREISFER
FGKIARKVKS YLLADISHIA GLIVGGEHSS PFPYADVVMT TTHKTLRGPR SAVIFCRKEL
ASKIDKAVFP GFQGGPHEHT IFAKAIAFQE AQTPQFKEYQ KQVVKNAKIL AEELKNKGFN
LVTGGTDNHL MLIDLKNKNI DGAEAQNILE KANILANRKR I
//
