ID A0A1J1HBV3_PLARL Unreviewed; 442 AA.
AC A0A1J1HBV3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Serine hydroxymethyltransferase {ECO:0000256|RuleBase:RU000585};
DE EC=2.1.2.1 {ECO:0000256|RuleBase:RU000585};
GN Name=SHMT {ECO:0000313|EMBL:CRH02783.1};
GN ORFNames=PRELSG_1451700 {ECO:0000313|EMBL:CRH02783.1};
OS Plasmodium relictum.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Haemamoeba).
OX NCBI_TaxID=85471 {ECO:0000313|EMBL:CRH02783.1, ECO:0000313|Proteomes:UP000220158};
RN [1] {ECO:0000313|EMBL:CRH02783.1, ECO:0000313|Proteomes:UP000220158}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SGS1 {ECO:0000313|EMBL:CRH02783.1,
RC ECO:0000313|Proteomes:UP000220158};
RG Pathogen Informatics;
RL Submitted (APR-2015) 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; LN835309; CRH02783.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J1HBV3; -.
DR VEuPathDB; PlasmoDB:PRELSG_1451700; -.
DR OMA; CQFANVQ; -.
DR OrthoDB; 5358603at2759; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000220158; Chromosome 14.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 3: Inferred from homology;
KW Methyltransferase {ECO:0000313|EMBL:CRH02783.1};
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 Reference proteome {ECO:0000313|Proteomes:UP000220158};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000585}.
FT DOMAIN 8..393
FT /note="Serine hydroxymethyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF00464"
FT MOD_RES 237
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000412-50"
SQ SEQUENCE 442 AA; 49810 MW; B8F34FB1D9C35145 CRC64;
MFNGDSLEII DKELFDILED EQKRQKETIN LIASENFINK AVRECLGHRV SNKYSEGYPR
KRYYGGNDYI DKIEELCYKR ALEAYNISEN EWGVNVQALS GSAANVQALY GLVGLKGKIL
GMHLCSGGHL THGFFNEKKK VSITSDLFES RLYKCNSEGY LDYDSIRKIA LEFRPKVIIC
GYTSYPRDID YKKFRDICDE VDAYLLADIS HISSFVACKL LNNPFEYADV VTTTTHKTLR
GPRSALIFFN KKRNPGIDEK INSAVFPSFQ GGPHNNKIAA VACQLKEVNS DFFRKYAKQV
LLNSKALSKY LIDNNVDIVT NGTDNHLILV DLRRYNITGS KLQEVCNAIN VSLNKNTIPS
DVDCVSPSGV RIGTPAITTR GAKEKDMEFI AQILIKAIKL TADLQQIYGK KLVDFKKGLV
NNSDIEKLKS EVVEWASHLP LP
//
