ID M1ZXK6_CLOBO Unreviewed; 192 AA.
AC M1ZXK6;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Serine hydroxymethyltransferase {ECO:0000313|EMBL:EKN42189.1};
DE EC=2.1.2.1 {ECO:0000313|EMBL:EKN42189.1};
DE Flags: Fragment;
GN Name=glyA {ECO:0000313|EMBL:EKN42189.1};
GN ORFNames=CFSAN001627_08397 {ECO:0000313|EMBL:EKN42189.1};
OS Clostridium botulinum CFSAN001627.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1232189 {ECO:0000313|EMBL:EKN42189.1, ECO:0000313|Proteomes:UP000011944};
RN [1] {ECO:0000313|EMBL:EKN42189.1, ECO:0000313|Proteomes:UP000011944}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFSAN001627 {ECO:0000313|EMBL:EKN42189.1,
RC ECO:0000313|Proteomes:UP000011944};
RA Strain E.A., Brown E., Allard M.W., Gonzalez-Escalona N., Timme R.;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EKN42189.1, ECO:0000313|Proteomes:UP000011944}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFSAN001627 {ECO:0000313|EMBL:EKN42189.1,
RC ECO:0000313|Proteomes:UP000011944};
RA Timme R.E., Allard M., Luo Y., Strain E., Gonzalez-Escalona N., Brown E.;
RT "Diversity in Clostridium botulinum.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
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:EKN42189.1}.
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DR EMBL; AMXI01000482; EKN42189.1; -; Genomic_DNA.
DR AlphaFoldDB; M1ZXK6; -.
DR PATRIC; fig|1232189.3.peg.1342; -.
DR Proteomes; UP000011944; Unassembled WGS sequence.
DR GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IEA:UniProtKB-EC.
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 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 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:EKN42189.1};
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EKN42189.1}.
FT DOMAIN 2..183
FT /note="Serine hydroxymethyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF00464"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EKN42189.1"
SQ SEQUENCE 192 AA; 21448 MW; 29C2B7ACB4F406F8 CRC64;
ETIDYDQLKK IALENRPKMI VSGASAYPRI IDFEKIREIC DEIDAYMMVD MAHIAGLVAT
GLHPSPVPYA DFVTTTTHKT LRGPRGGAIL CKEKYAKAVD KAIFPGIQGG PLMHTIAAKA
VCFGEALRED YKEYMKQVVK NTKVLGEELK NYGFRLISGG TDNHLLLIDL TNKNITGKDA
EKTFRFSRNY CE
//