GLYC_ENCCU
ID GLYC_ENCCU Reviewed; 460 AA.
AC O62585; Q8SQH9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Serine hydroxymethyltransferase, cytosolic;
DE Short=SHMT;
DE EC=2.1.2.1 {ECO:0000250|UniProtKB:P34896};
DE AltName: Full=Glycine hydroxymethyltransferase;
DE AltName: Full=Serine methylase;
GN Name=SHMT-1; OrderedLocusNames=ECU01_0190;
GN and
GN Name=SHMT-2; OrderedLocusNames=ECU01_1420;
OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=284813;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (SHMT-1).
RX PubMed=11013707; DOI=10.1089/omi.1.1998.3.1;
RA Duffieux F., Peyret P., Roe B.A., Vivares C.P.;
RT "First report on the systematic sequencing of the small genome of
RT Encephalitozoon cuniculi (Protozoa, Microspora): gene organization of a 4.3
RT kbp region on chromosome I.";
RL Microb. Comp. Genomics 3:1-11(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (SHMT-1 AND SHMT-2).
RC STRAIN=GB-M1;
RX PubMed=11157783; DOI=10.1101/gr.164301;
RA Peyret P., Katinka M.D., Duprat S., Duffieux F., Barbe V., Barbazanges M.,
RA Weissenbach J., Saurin W., Vivares C.P.;
RT "Sequence and analysis of chromosome I of the amitochondriate intracellular
RT parasite Encephalitozoon cuniculi (Microspora).";
RL Genome Res. 11:198-207(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (SHMT-1 AND SHMT-2).
RC STRAIN=GB-M1;
RX PubMed=11719806; DOI=10.1038/35106579;
RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA Vivares C.P.;
RT "Genome sequence and gene compaction of the eukaryote parasite
RT Encephalitozoon cuniculi.";
RL Nature 414:450-453(2001).
CC -!- FUNCTION: Interconversion of serine and glycine.
CC {ECO:0000250|UniProtKB:P34896}.
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:0000250|UniProtKB:P34896};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P34896};
CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC {ECO:0000250|UniProtKB:P34896}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P34896}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the SHMT family. {ECO:0000305}.
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DR EMBL; AJ005644; CAA06649.1; -; Genomic_DNA.
DR EMBL; AL391737; CAD24889.1; -; Genomic_DNA.
DR EMBL; AL391737; CAD25015.1; -; Genomic_DNA.
DR RefSeq; XP_965854.1; XM_960761.1.
DR RefSeq; XP_965980.1; XM_960887.1.
DR AlphaFoldDB; O62585; -.
DR SMR; O62585; -.
DR STRING; 284813.O62585; -.
DR PRIDE; O62585; -.
DR GeneID; 860192; -.
DR GeneID; 860193; -.
DR KEGG; ecu:ECU01_0190; -.
DR KEGG; ecu:ECU01_1420; -.
DR VEuPathDB; MicrosporidiaDB:ECU01_0190; -.
DR VEuPathDB; MicrosporidiaDB:ECU01_1420; -.
DR HOGENOM; CLU_022477_0_2_1; -.
DR InParanoid; O62585; -.
DR OMA; VTNRNAI; -.
DR OrthoDB; 372408at2759; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000000819; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IEA:UniProtKB-EC.
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:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
DR CDD; cd00378; SHMT; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 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; PTHR11680; 1.
DR Pfam; PF00464; SHMT; 1.
DR PIRSF; PIRSF000412; SHMT; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00096; SHMT; 1.
PE 3: Inferred from homology;
KW Cytoplasm; One-carbon metabolism; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..460
FT /note="Serine hydroxymethyltransferase, cytosolic"
FT /id="PRO_0000113509"
FT MOD_RES 244
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P34896"
FT CONFLICT 98
FT /note="V -> A (in Ref. 1; CAA06649)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="N -> Y (in Ref. 1; CAA06649)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 460 AA; 50181 MW; E322D7A78AC0DAAE CRC64;
MTDAREKGFW TGPLEMADPE LHALICGEVE RQKKTINLIA SENYAHQSAM EACGSVLTNK
YSEGRVGERY YGGTHWVDRI ELLCQKRALE LFGLDPDVWG VNVQPYSGSP ANFAIYTAVV
PPGGRIMGLD LPSGGHLTHG YKTKTRKISA SSVYFDSRPY TVGSNGLIDY EGLEKTFTDF
LPHILICGYS AYSRDIDYKR LQSIAGRNGA FLFADISHIS PLVASGLMNS PFEHCDIVMT
TTQKGLRGPR GALIFYRRAV TKNGETVDLD ARINFAVFPM LQGGPHNHTI AGIASALLHA
GTPEFAEYTR RVVENSRELC SRLQSLGLDI LTGGTDNHML LVDLRSTGVD GAAVEHMCDA
LGISLNRNAI VGNSSPLSPS GIRVGTYAVT ARGFGPEEMR EVGDIIGGVV KLCREMTGGR
KMSKADLHRV TSDARVMGSE QVLVLRRRVC ALAEAYPIYE
