ID GLYC_CANGA Reviewed; 469 AA.
AC Q6FUP6;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 111.
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=CAGL0F01749g;
OS Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 /
OS NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Interconversion of serine and glycine. {ECO:0000250}.
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 {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the SHMT family. {ECO:0000305}.
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DR EMBL; CR380952; CAG58972.1; -; Genomic_DNA.
DR RefSeq; XP_446048.1; XM_446048.1.
DR AlphaFoldDB; Q6FUP6; -.
DR SMR; Q6FUP6; -.
DR STRING; 284593.Q6FUP6; -.
DR EnsemblFungi; CAGL0F01749g-T; CAGL0F01749g-T-p1; CAGL0F01749g.
DR GeneID; 2887952; -.
DR KEGG; cgr:CAGL0F01749g; -.
DR CGD; CAL0131260; SHM2.
DR VEuPathDB; FungiDB:B1J91_F01749g; -.
DR VEuPathDB; FungiDB:CAGL0F01749g; -.
DR eggNOG; KOG2467; Eukaryota.
DR HOGENOM; CLU_022477_0_0_1; -.
DR InParanoid; Q6FUP6; -.
DR OMA; CQFANVQ; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000002428; Chromosome F.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0062040; C:fungal biofilm matrix; IDA:CGD.
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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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; SERINE HYDROXYMETHYLTRANSFERASE; 1.
DR PANTHER; PTHR11680:SF66; SERINE HYDROXYMETHYLTRANSFERASE, CYTOSOLIC; 1.
DR Pfam; PF00464; SHMT; 1.
DR PIRSF; PIRSF000412; SHMT; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 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_0000113512"
FT MOD_RES 248
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 469 AA; 52304 MW; D07B42FC13D30951 CRC64;
MPYALSDKHL KMVSGHLSET DPEVEQIIKD EVDRQKHSID LIASENFTTT SVFDALGTPL
CNKYSEGYPG ARYYGGNEHI DRIERLCQQR ALEAFHVTPD RWGVNVQTLS GSPANLQVYQ
ALMKPHERLM GLYLPDGGHL SHGYATENRK ISAVSTYFES FPYRVNPETG IIDYDTLEKN
AILYRPKILV AGTSAYCRLI DYKRMREIAD KCGAYLMVDM AHISGLVAAG VIPSPFEYAD
IVTTTTHKSL RGPRGAMIFF RRGIRSVNQK TGKEIPYDLE NPINFSVFPG HQGGPHNHTI
AALATALKQA ATPEFKEYQT QVLKNAKALE NEFQTLGYRL VSNGTDSHMV LVSLREKGVD
GARVEYVCEK INIALNKNSI PGDKSALVPG GVRIGAPAMT TRGMGEEDFH RIVRYIDQAV
KFAEQTQSSL PKEANKLKDF KAKVDEIADQ LAPLKKEIYD WTAEYPLAV
//
