(data stored in ACNUC7421 zone)

SWISSPROT: GLYC_ASHGO

ID   GLYC_ASHGO              Reviewed;         469 AA.
AC   Q75BQ6; Q5K599;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 2.
DT   11-DEC-2019, entry version 92.
DE   RecName: Full=Serine hydroxymethyltransferase, cytosolic;
DE            Short=SHMT;
DE            EC=2.1.2.1;
DE   AltName: Full=Glycine hydroxymethyltransferase;
DE   AltName: Full=Serine methylase;
GN   Name=SHM2; OrderedLocusNames=ACR215C;
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, AND SEQUENCE REVISION TO 446.
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: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the SHMT family. {ECO:0000305}.
DR   EMBL; AJ438779; CAD27656.1; -; Genomic_DNA.
DR   EMBL; AE016816; AAS51441.2; -; Genomic_DNA.
DR   RefSeq; NP_983617.2; NM_208970.2.
DR   SMR; Q75BQ6; -.
DR   STRING; 33169.AAS51441; -.
DR   PRIDE; Q75BQ6; -.
DR   EnsemblFungi; AAS51441; AAS51441; AGOS_ACR215C.
DR   GeneID; 4619749; -.
DR   KEGG; ago:AGOS_ACR215C; -.
DR   HOGENOM; HOG000239405; -.
DR   InParanoid; Q75BQ6; -.
DR   KO; K00600; -.
DR   OMA; PLEHIIA; -.
DR   BRENDA; 2.1.2.1; 484.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000000591; Chromosome III.
DR   GO; GO:0005737; C:cytoplasm; 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; Q75BQ6.
DR   SWISS-2DPAGE; Q75BQ6.
KW   Cytoplasm; One-carbon metabolism; Pyridoxal phosphate; Reference proteome;
KW   Transferase.
FT   CHAIN           1..469
FT                   /note="Serine hydroxymethyltransferase, cytosolic"
FT                   /id="PRO_0000113510"
FT   MOD_RES         248
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   469 AA;  52243 MW;  902BB2FC16FEAF39 CRC64;
     MPYHLSESHK KLISSHLSES DPEVDAIIKD EIDRQKHSIV LIASENLTST AVFDALGTPM
     CNKYSEGYPG ARYYGGNQHI DRMELLCQRR ALEAFHVTPD RWGVNVQSLS GSPANLQVYQ
     ALMKPHERLM GLHLPDGGHL SHGYQTETRK ISAVSTYFES FPYRVDPETG IIDYDTLEKN
     AVLYRPKILV AGTSAYCRLI DYKRMREIAD KVGAYLMVDM AHISGLVAAG VIPSPFEYAD
     IVTTTTHKSL RGPRGAMIFF RRGVRSVHPK TGEEVMYDLE GPINFSVFPG HQGGPHNHTI
     SALATALKQA TTPEFREYQE LVLKNAKVLE TEFKKLNYRL VSDGTDSHMV LVSLREKGVD
     GARVEHVCEK INIALNKNSI PGDKSALVPG GVRIGAPAMT TRGMGEEDFA RIVGYINRAV
     EIARSIQQSL PKEANRLKDF KAKVEDGTDE IAQLAQEIYS WTEEYPLPV
//

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