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Database: UniProt
Entry: A0A259F3H3_9PROT
LinkDB: A0A259F3H3_9PROT
Original site: A0A259F3H3_9PROT 
ID   A0A259F3H3_9PROT        Unreviewed;       109 AA.
AC   A0A259F3H3;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Serine hydroxymethyltransferase {ECO:0000313|EMBL:OZA33085.1};
DE   Flags: Fragment;
GN   Name=glyA {ECO:0000313|EMBL:OZA33085.1};
GN   ORFNames=B7X82_10085 {ECO:0000313|EMBL:OZA33085.1};
OS   Hydrogenophilales bacterium 17-64-65.
OC   Bacteria; Pseudomonadota; Hydrogenophilia; Hydrogenophilales.
OX   NCBI_TaxID=1970528 {ECO:0000313|EMBL:OZA33085.1, ECO:0000313|Proteomes:UP000216509};
RN   [1] {ECO:0000313|EMBL:OZA33085.1, ECO:0000313|Proteomes:UP000216509}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17-64-65 {ECO:0000313|EMBL:OZA33085.1};
RA   Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA   Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT   "Lifting the veil on microbial sulfur biogeochemistry in mining
RT   wastewaters.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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:OZA33085.1}.
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DR   EMBL; NCIQ01000014; OZA33085.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A259F3H3; -.
DR   Proteomes; UP000216509; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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   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; IPR039429; SHMT-like_dom.
DR   PANTHER; PTHR11680; SERINE HYDROXYMETHYLTRANSFERASE; 1.
DR   PANTHER; PTHR11680:SF50; SERINE HYDROXYMETHYLTRANSFERASE; 1.
DR   Pfam; PF00464; SHMT; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000313|EMBL:OZA33085.1};
KW   One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OZA33085.1}.
FT   DOMAIN          8..108
FT                   /note="Serine hydroxymethyltransferase-like"
FT                   /evidence="ECO:0000259|Pfam:PF00464"
FT   NON_TER         109
FT                   /evidence="ECO:0000313|EMBL:OZA33085.1"
SQ   SEQUENCE   109 AA;  12137 MW;  47F65D29309AE671 CRC64;
     MFNRQDTLAK TDPDLWAAIQ KEDQRQQDHI ELIASENYTS PAVMEAQGSQ LTNKYAEGYP
     GKRYYGGCEY VDIVEQLAID RVKALFGAEA ANVQPNSGSQ ANQAVFMAF
//
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