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Database: UniProt
Entry: A0A0L1I2L6_PLAFA
LinkDB: A0A0L1I2L6_PLAFA
Original site: A0A0L1I2L6_PLAFA 
ID   A0A0L1I2L6_PLAFA        Unreviewed;       442 AA.
AC   A0A0L1I2L6;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   22-FEB-2023, entry version 27.
DE   RecName: Full=glycine hydroxymethyltransferase {ECO:0000256|ARBA:ARBA00012256};
DE            EC=2.1.2.1 {ECO:0000256|ARBA:ARBA00012256};
GN   ORFNames=PFMG_00021 {ECO:0000313|EMBL:KNG73886.1};
OS   Plasmodium falciparum IGH-CR14.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=580059 {ECO:0000313|EMBL:KNG73886.1, ECO:0000313|Proteomes:UP000054562};
RN   [1] {ECO:0000313|Proteomes:UP000054562}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IGH-CR14 {ECO:0000313|Proteomes:UP000054562};
RG   The Broad Institute Genome Sequencing Platform;
RA   Volkman S.K., Neafsey D.E., Dash A.P., Chitnis C.E., Hartl D.L.,
RA   Young S.K., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA   Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heilman E.R., Heiman D.I., Howarth C., Jen D.,
RA   Larson L., Mehta T., Neiman D., Park D., Pearson M., Roberts A., Saif S.,
RA   Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA   Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.;
RT   "Annotation of Plasmodium falciparum IGH-CR14.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000054562}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IGH-CR14 {ECO:0000313|Proteomes:UP000054562};
RG   The Broad Institute Genome Sequencing Platform;
RA   Volkman S.K., Neafsey D.E., Dash A.P., Chitnis C.E., Hartl D.L.,
RA   Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Godfrey P., Alvarado L.,
RA   Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C.,
RA   Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA   Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T.,
RA   White J., Yandava C., Wirth D.F., Nusbaum C., Birren B.;
RT   "The genome sequence of Plasmodium falciparum IGH-CR14.";
RL   Submitted (JUL-2015) 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   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC       {ECO:0000256|ARBA:ARBA00004777}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the SHMT family.
CC       {ECO:0000256|ARBA:ARBA00006376}.
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DR   EMBL; GG664959; KNG73886.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L1I2L6; -.
DR   SMR; A0A0L1I2L6; -.
DR   EnsemblProtists; KNG73886; KNG73886; PFMG_00021.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000054562; Unassembled WGS sequence.
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; IPR039429; SHMT-like_dom.
DR   PANTHER; PTHR11680:SF35; GLYCINE HYDROXYMETHYLTRANSFERASE; 1.
DR   PANTHER; PTHR11680; 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   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Methyltransferase {ECO:0000313|EMBL:KNG73886.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR000412-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054562};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KNG73886.1}.
FT   DOMAIN          7..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;  49780 MW;  87E1C14AAFF0B8E7 CRC64;
     MFNNDPLQKY DKELFDLLEK EKNRQIETIN LIASENLTNT AVRECLGDRI SNKYSEGYPH
     KRYYGGNDYV DKIEELCYKR ALEAFNVSEE EWGVNVQPLS GSAANVQALY ALVGVKGKIM
     GMHLCSGGHL THGFFDEKKK VSITSDLFES KLYKCNSEGY VDMESVRNLA LSFQPKVIIC
     GYTSYPRDID YKGFREICDE VNAYLFADIS HISSFVACNL LNNPFTYADV VTTTTHKILR
     GPRSALIFFN KKRNPGIDQK INSSVFPSFQ GGPHNNKIAA VACQLKEVNT PFFKEYTKQV
     LLNSKALAEC LLKRNLDLVT NGTDNHLIVV DLRKYNITGS KLQETCNAIN IALNKNTIPS
     DVDCVSPSGI RIGTPALTTR GCKEKDMEFI ADMLLKAILL TDELQQKYGK KLVDFKKGLV
     NNPKIDELKK EVVQWAKNLP FA
//
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