GLYM_YEAST
ID GLYM_YEAST Reviewed; 490 AA.
AC P37292; D6VQR0;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 185.
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; Synonyms=SHMT1; OrderedLocusNames=YBR263W; ORFNames=YBR1732;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=8132653; DOI=10.1016/s0021-9258(17)37089-8;
RA McNeil J.B., McIntosh E.M., Taylor B.V., Zhang F.-R., Tang S., Bognar A.L.;
RT "Cloning and molecular characterization of three genes, including two genes
RT encoding serine hydroxymethyltransferases, whose inactivation is required
RT to render yeast auxotrophic for glycine.";
RL J. Biol. Chem. 269:9155-9165(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8465606; DOI=10.1002/yea.320090210;
RA Doignon F., Biteau N., Crouzet M., Aigle M.;
RT "The complete sequence of a 19,482 bp segment located on the right arm of
RT chromosome II from Saccharomyces cerevisiae.";
RL Yeast 9:189-199(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP INTERACTION WITH NAP1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18086883; DOI=10.1128/mcb.01035-07;
RA Calvert M.E.K., Keck K.M., Ptak C., Shabanowitz J., Hunt D.F.,
RA Pemberton L.F.;
RT "Phosphorylation by casein kinase 2 regulates Nap1 localization and
RT function.";
RL Mol. Cell. Biol. 28:1313-1325(2008).
CC -!- FUNCTION: Interconversion of serine and glycine.
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 -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC -!- SUBUNIT: Homotetramer (By similarity). Interacts with NAP1.
CC {ECO:0000250, ECO:0000269|PubMed:18086883}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- MISCELLANEOUS: In eukaryotes there are two forms of the enzymes: a
CC cytosolic one and a mitochondrial one.
CC -!- MISCELLANEOUS: Present with 17700 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SHMT family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA49927.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA85226.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L22528; AAA21024.1; -; Genomic_DNA.
DR EMBL; X70529; CAA49927.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z36131; CAA85226.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006936; DAA07380.1; -; Genomic_DNA.
DR PIR; S29348; S29348.
DR RefSeq; NP_009822.4; NM_001178611.3.
DR AlphaFoldDB; P37292; -.
DR SMR; P37292; -.
DR BioGRID; 32958; 120.
DR DIP; DIP-4952N; -.
DR IntAct; P37292; 6.
DR MINT; P37292; -.
DR STRING; 4932.YBR263W; -.
DR iPTMnet; P37292; -.
DR MaxQB; P37292; -.
DR PaxDb; P37292; -.
DR PRIDE; P37292; -.
DR EnsemblFungi; YBR263W_mRNA; YBR263W; YBR263W.
DR GeneID; 852565; -.
DR KEGG; sce:YBR263W; -.
DR SGD; S000000467; SHM1.
DR VEuPathDB; FungiDB:YBR263W; -.
DR eggNOG; KOG2467; Eukaryota.
DR GeneTree; ENSGT00390000002762; -.
DR HOGENOM; CLU_022477_0_1_1; -.
DR InParanoid; P37292; -.
DR OMA; RCQHSEV; -.
DR BioCyc; MetaCyc:YBR263W-MON; -.
DR BioCyc; YEAST:YBR263W-MON; -.
DR Reactome; R-SCE-196757; Metabolism of folate and pterines.
DR Reactome; R-SCE-71262; Carnitine synthesis.
DR UniPathway; UPA00193; -.
DR PRO; PR:P37292; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P37292; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IMP:SGD.
DR GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IMP:SGD.
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; IMP:SGD.
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 1: Evidence at protein level;
KW Mitochondrion; One-carbon metabolism; Pyridoxal phosphate;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..20
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 21..490
FT /note="Serine hydroxymethyltransferase, mitochondrial"
FT /id="PRO_0000032568"
FT MOD_RES 265
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 72
FT /note="L -> S (in Ref. 1; AAA21024)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 490 AA; 53686 MW; 8DECF1ECD6349450 CRC64;
MFPRASALAK CMATVHRRGL LTSGAQSLVS KPVSEGDPEM FDILQQERHR QKHSITLIPS
ENFTSKAVMD LLGSELQNKY SEGYPGERYY GGNEIIDKSE SLCQARALEL YGLDPAKWGV
NVQPLSGAPA NLYVYSAIMN VGERLMGLDL PDGGHLSHGY QLKSGTPISF ISKYFQSMPY
HVDHTTGLID YDNLQVLAKA FRPKVIVAGT SAYSRLIDYA RFKEISQGCG AYLMSDMAHI
SGLVAANVVP SPFEHSDIVT TTTHKSLRGP RGAMIFFRKG IKSVTKKGKE IPYELEKKIN
FSVFPGHQGG PHNHTIGAMA VALKQAMSPE FKEYQQKIVD NSKWFAQELT KMGYKLVSGG
TDNHLIVIDL SGTQVDGARV ETILSALNIA ANKNTIPGDK SALFPSGLRI GTPAMTTRGF
GREEFSQVAK YIDSAVKLAE NLKTLEPTTK LDARSRLNEF KKLCNESSEV AALSGEISKW
VGQYPVPGDI
