ID A4EWE4_9RHOB Unreviewed; 413 AA.
AC A4EWE4;
DT 17-APR-2007, integrated into UniProtKB/TrEMBL.
DT 17-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Serine hydroxymethyltransferase {ECO:0000313|EMBL:EBA15897.1};
GN ORFNames=RSK20926_04777 {ECO:0000313|EMBL:EBA15897.1};
OS Roseobacter sp. SK209-2-6.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseobacter.
OX NCBI_TaxID=388739 {ECO:0000313|EMBL:EBA15897.1, ECO:0000313|Proteomes:UP000005964};
RN [1] {ECO:0000313|EMBL:EBA15897.1, ECO:0000313|Proteomes:UP000005964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK209-2-6 {ECO:0000313|EMBL:EBA15897.1,
RC ECO:0000313|Proteomes:UP000005964};
RA Ward B., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUN-2006) 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:EBA15897.1}.
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DR EMBL; AAYC01000008; EBA15897.1; -; Genomic_DNA.
DR AlphaFoldDB; A4EWE4; -.
DR eggNOG; COG0112; Bacteria.
DR Proteomes; UP000005964; 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:EBA15897.1};
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000412-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000005964};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EBA15897.1}.
FT DOMAIN 13..376
FT /note="Serine hydroxymethyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF00464"
FT MOD_RES 227
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000412-50"
SQ SEQUENCE 413 AA; 42969 MW; 5CF64986122A2DD9 CRC64;
MEAAQAAARI EALVQENTQI HDHQCFNLNP ATNVMNPAAE AILARGLGSR PSLGYPGDKY
EMGLEAIEEI EVMAAELSAQ VFGAGFAEIR VASGAMANLY GFMALTKPGD CIIAPPAAIG
GHVTHHGEGC AGLYGLETHP APVNADGYSV DLEALRALAH KLQPKLITIG GSLNVLPHPV
AEVRAIADEV GAKVLFDAAH QCGVIAGGAW ANPLAEGAHL MTMSTYKSLG GPAGGLIVTN
EAEIAERLDK IAFPGMTANF DAAKSAALAL TMLDWLEYGA DYTRAMIELA IALADELEKQ
GLPIFKAGGQ ATASHQFALE AACFGGGQAA SKRLRQAGFL ACGIGLPIDP VSGDMNGLRI
GTPELVRRGV TPEHAPVLAG LIADGLKGNA LQDVAKRTAA LRAEFQGFHY VRK
//
