ID G3C904_PINPS Unreviewed; 470 AA.
AC G3C904;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Serine hydroxymethyltransferase {ECO:0000256|RuleBase:RU000585};
DE EC=2.1.2.1 {ECO:0000256|RuleBase:RU000585};
GN Name=cshmt {ECO:0000313|EMBL:CCC55430.1};
OS Pinus pinaster (Maritime pine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC Pinus subgen. Pinus.
OX NCBI_TaxID=71647 {ECO:0000313|EMBL:CCC55430.1};
RN [1] {ECO:0000313|EMBL:CCC55430.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Differentiating xylem {ECO:0000313|EMBL:CCC55430.1};
RA Canton F.;
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CCC55430.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Differentiating xylem {ECO:0000313|EMBL:CCC55430.1};
RA Pacheco-Villalobos D., Diaz-Moreno S.M., Canas R.A., Said E.-.S., Osuna D.,
RA Van Kerckhoven S.H.E., Bautista R., Claros M.G., Canovas F.M., Canton F.R.;
RT "Comparative transcriptome analysis of compression and opposite wood
RT formation in maritime pine by suppression subtractive hybridization coupled
RT with microarray.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Interconversion of serine and glycine.
CC {ECO:0000256|RuleBase:RU000585}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O =
CC (6S)-5,6,7,8-tetrahydrofolate + L-serine; Xref=Rhea:RHEA:15481,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57453; EC=2.1.2.1;
CC Evidence={ECO:0000256|RuleBase:RU000585};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR000412-50, ECO:0000256|RuleBase:RU000585};
CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC {ECO:0000256|ARBA:ARBA00004777, ECO:0000256|RuleBase:RU000585}.
CC -!- SIMILARITY: Belongs to the SHMT family. {ECO:0000256|ARBA:ARBA00006376,
CC ECO:0000256|RuleBase:RU000585}.
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DR EMBL; HE574564; CCC55430.1; -; mRNA.
DR AlphaFoldDB; G3C904; -.
DR UniPathway; UPA00193; -.
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:UniProtKB-UniPathway.
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 HAMAP; MF_00051; SHMT; 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:SF35; SERINE HYDROXYMETHYLTRANSFERASE, CYTOSOLIC; 1.
DR Pfam; PF00464; SHMT; 1.
DR PIRSF; PIRSF000412; SHMT; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00096; SHMT; 1.
PE 2: Evidence at transcript level;
KW Methyltransferase {ECO:0000313|EMBL:CCC55430.1};
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563,
KW ECO:0000256|RuleBase:RU000585};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000412-50};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000585}.
FT DOMAIN 12..411
FT /note="Serine hydroxymethyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF00464"
FT MOD_RES 244
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000412-50"
SQ SEQUENCE 470 AA; 51729 MW; FFBAEF2F9094A413 CRC64;
MDPVNVWGNT PLKVVDEEIF DLIEKEKRRQ CRGIELIASE NFTSLAVIEA LGTPLTNKYS
EGMPGNRYYG GNEYIDLIEN LCRSRALQAF HLDSEKWGVN VQPYSGSPAN FAAYTALLNP
HDRIMGLDLP SGGHLTHGYY TSGGKKISAT SIYFESLPYK VSQETGFIDY DKLEEKALDF
RPKLIICGGS AYPRDWDYAR FRSIADKCGA MLLCDMAHIS GLVAAQEAGN PFDYCDLVTT
TTHKSLRGPR AGMIFYRKGP KPPKKGQPEG ALNDYEDRVN FSVFPSLQGG PHNHQIAALA
VALKQVMTPG FKAYAKQVKA NAVAVGNYLM SKGYKLVTSG TENHLVLWDL RPIGLTGNKV
EKVCDLCNIT INKNAVYGDS SALSPGGVRI GTPAMTSRGL KEADFEQIGE FLHQSIIITL
AIQSEHGKLL KDFNKGLAGN KDIENLKAQV EKFSAQFDMP GFDVATMKFQ
//
