(data stored in ACNUC7421 zone)

SWISSPROT: 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   11-DEC-2019, entry version 96.
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}.
DR   EMBL; AJ438778; CAD27655.1; -; Genomic_DNA.
DR   EMBL; AE016818; AAS52497.1; -; Genomic_DNA.
DR   RefSeq; NP_984673.1; NM_210026.1.
DR   SMR; Q758F0; -.
DR   STRING; 33169.AAS52497; -.
DR   PRIDE; Q758F0; -.
DR   EnsemblFungi; AAS52497; AAS52497; AGOS_AEL188W.
DR   GeneID; 4620858; -.
DR   KEGG; ago:AGOS_AEL188W; -.
DR   HOGENOM; HOG000239405; -.
DR   InParanoid; Q758F0; -.
DR   KO; K00600; -.
DR   OMA; FSGRWFD; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0016597; F:amino acid binding; IBA:GO_Central.
DR   GO; GO:0050897; F:cobalt ion binding; IBA:GO_Central.
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:1904482; P:cellular response to tetrahydrofolate; 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:0006544; P:glycine metabolic process; 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; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
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;
DR   PRODOM; Q758F0.
DR   SWISS-2DPAGE; Q758F0.
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
//

If you have problems or comments...

PBIL Back to PBIL home page