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Database: UniProt
Entry: A0A257GMM1_9RHOB
LinkDB: A0A257GMM1_9RHOB
Original site: A0A257GMM1_9RHOB 
ID   A0A257GMM1_9RHOB        Unreviewed;       439 AA.
AC   A0A257GMM1;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Serine hydroxymethyltransferase {ECO:0000313|EMBL:OYU39608.1};
GN   ORFNames=CFE33_09550 {ECO:0000313|EMBL:OYU39608.1};
OS   Pseudorhodobacter sp. PARRP1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Pseudorhodobacter.
OX   NCBI_TaxID=2015560 {ECO:0000313|EMBL:OYU39608.1, ECO:0000313|Proteomes:UP000215760};
RN   [1] {ECO:0000313|EMBL:OYU39608.1, ECO:0000313|Proteomes:UP000215760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PARRP1 {ECO:0000313|EMBL:OYU39608.1};
RA   Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA   Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT   "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT   formosa and its bacterial cohort.";
RL   Submitted (JUN-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         ECO:0000256|PIRSR:PIRSR000412-50};
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:OYU39608.1}.
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DR   EMBL; NKIU01000003; OYU39608.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A257GMM1; -.
DR   Proteomes; UP000215760; 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   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:SF28; SERINE HYDROXYMETHYLTRANSFERASE; 1.
DR   Pfam; PF00464; SHMT; 1.
DR   PIRSF; PIRSF000412; SHMT; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000313|EMBL:OYU39608.1};
KW   One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000412-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000215760};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OYU39608.1}.
FT   DOMAIN          53..407
FT                   /note="Serine hydroxymethyltransferase-like"
FT                   /evidence="ECO:0000259|Pfam:PF00464"
FT   MOD_RES         253
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000412-50"
SQ   SEQUENCE   439 AA;  45867 MW;  815E4DC2EFB6DE30 CRC64;
     MPHLSPRPWV PAACESLIQR IAADTTAPSP QVADRIEALV QANTQIHDLD CFNLNPATNI
     MNPRAEAVLA RGLGSRPSLG YPGDKYEMGL EAIEEIEVIA AELAAEIFQA KYAEIRVGSG
     ALANLYGFMA LTKPGDVIIA PPATIGGHVT HHAGGCAGLY GLITHPAPIN ADGYTVDLEQ
     LRALAHNVKP KLITVGGSLN LFPHPVAEIR AIADEVGAKV LFDAAHQCGI IAGGVWANPL
     HEGAHLMTMS TYKSLGGPAG GLIVTNDAEI AERLDHIAYP GMTANFDAAK SAALALSLLD
     WRDFGASYAR AMVDLAQALA RELGALGLPI FAAGKGSTQS HQFAIEAAGF GGGQTASKSL
     RKSGFLACGI GLPIAALAND LNGLRIGTPE LVRRGVTPAD APALARLIAE SLRSNDPEGI
     APRTAALRKD FQGLHYMHP
//
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