GLYM_ASHGO
ID GLYM_ASHGO Reviewed; 497 AA.
AC Q758F0; Q5K5A0;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Serine hydroxymethyltransferase, mitochondrial;
DE Short=SHMT;
DE EC=2.1.2.1;
DE AltName: Full=Glycine hydroxymethyltransferase;
DE AltName: Full=Serine methylase;
DE Flags: Precursor;
GN Name=SHM1; OrderedLocusNames=AEL188W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=12350229; DOI=10.1042/bj20021224;
RA Schluepen C., Santos M.A., Weber U., de Graaf A., Revuelta J.L.,
RA Stahmann K.-P.;
RT "Disruption of the SHM2 gene, encoding one of two serine
RT hydroxymethyltransferase isoenzymes, reduces the flux from glycine to
RT serine in Ashbya gossypii.";
RL Biochem. J. 369:263-273(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
CC -!- FUNCTION: Interconversion of serine and glycine.
CC {ECO:0000269|PubMed:12350229}.
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- MISCELLANEOUS: In eukaryotes there are two forms of the enzymes: a
CC cytosolic one and a mitochondrial one.
CC -!- SIMILARITY: Belongs to the SHMT family. {ECO:0000305}.
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DR EMBL; AJ438778; CAD27655.1; -; Genomic_DNA.
DR EMBL; AE016818; AAS52497.1; -; Genomic_DNA.
DR RefSeq; NP_984673.1; NM_210026.1.
DR AlphaFoldDB; Q758F0; -.
DR SMR; Q758F0; -.
DR STRING; 33169.AAS52497; -.
DR EnsemblFungi; AAS52497; AAS52497; AGOS_AEL188W.
DR GeneID; 4620858; -.
DR KEGG; ago:AGOS_AEL188W; -.
DR eggNOG; KOG2467; Eukaryota.
DR HOGENOM; CLU_022477_0_1_1; -.
DR InParanoid; Q758F0; -.
DR OMA; CATTHKV; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000000591; Chromosome V.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0070905; F:serine binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0046655; P:folic acid metabolic process; IBA:GO_Central.
DR GO; GO:0019264; P:glycine biosynthetic process from serine; IBA:GO_Central.
DR GO; GO:0006565; P:L-serine catabolic process; IBA:GO_Central.
DR GO; GO:0006730; P:one-carbon metabolic process; IBA:GO_Central.
DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
DR GO; GO:0046653; P:tetrahydrofolate metabolic process; IBA:GO_Central.
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 Mitochondrion; One-carbon metabolism; Pyridoxal phosphate;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..27
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 28..497
FT /note="Serine hydroxymethyltransferase, mitochondrial"
FT /id="PRO_0000032564"
FT MOD_RES 272
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 90
FT /note="G -> R (in Ref. 1; CAD27655)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 497 AA; 54708 MW; 43D6F2B5230F5969 CRC64;
MFIRRLHTSS RRLTCGEALR ACQQTGARSA NGQLMLSQHV QEFDPEMYDI LTKERSRQKR
SITLIPSENF TSVAVMNLLG SEMQNKYSEG YPGQRYYGGN QYIDMAESLC QKRALELYGL
DPAKWGVNVQ SLSGAPANLY AYSAIMEVGD RMMGLDLPHG GHLSHGYQLQ NGNKISYISK
YFQTMAYRVD PATGLVDYDT LSETSKLFRP KVIVAGTSAY ARVLDYKRFR EIADACGAYL
LSDMAHVSGL VAAGVHPSPF EYSDIVTTTT HKSLRGPRGA MIFYRKGIRK VTKKGTEIMY
DLDKRINFSV FPAHQGGPHN HTISALAVAL KQAATPEFKN YQTAVVENAK VFGEELSKRG
FSLVSGGTDT HLLLIDLSPM GIDGSRLETI LERLNIAANK NTIPGDKSAL YPSGLRVGTP
AMTTRGFGPA EFGRVAAYIN EAVKLAIGLK SQEPVDAKDA KTRLAHFKSF CAESEQVTKL
ANEVADWVAQ YPVPGEL
