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 25-MAY-2022, entry version 99.
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}.
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DR EMBL; AJ438779; CAD27656.1; -; Genomic_DNA.
DR EMBL; AE016816; AAS51441.2; -; Genomic_DNA.
DR RefSeq; NP_983617.2; NM_208970.2.
DR AlphaFoldDB; Q75BQ6; -.
DR SMR; Q75BQ6; -.
DR STRING; 33169.AAS51441; -.
DR EnsemblFungi; AAS51441; AAS51441; AGOS_ACR215C.
DR GeneID; 4619749; -.
DR KEGG; ago:AGOS_ACR215C; -.
DR eggNOG; KOG2467; Eukaryota.
DR HOGENOM; CLU_022477_0_1_1; -.
DR InParanoid; Q75BQ6; -.
DR OMA; SHPAGLI; -.
DR BRENDA; 2.1.2.1; 484.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000000591; Chromosome III.
DR GO; GO:0005737; C:cytoplasm; 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: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 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
