ID   GLYM_YEAST              Reviewed;         490 AA.
AC   P37292;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 2.
DT   01-SEP-2009, entry version 82.
DE   RecName: Full=Serine hydroxymethyltransferase, mitochondrial;
DE            Short=SHMT;
DE            Short=Serine methylase;
DE            EC=2.1.2.1;
DE   AltName: Full=Glycine hydroxymethyltransferase;
DE   Flags: Precursor;
GN   Name=SHM1; Synonyms=SHMT1; OrderedLocusNames=YBR263W;
GN   ORFNames=YBR1732;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 208353 / W303-1A;
RX   MEDLINE=94179335; PubMed=8132653;
RA   McNeil J.B., McIntosh E.M., Taylor B.V., Zhang F.-R., Tang S.,
RA   Bognar A.L.;
RT   "Cloning and molecular characterization of three genes, including two
RT   genes encoding serine hydroxymethyltransferases, whose inactivation is
RT   required 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   MEDLINE=93220397; 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
RT   of 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   MEDLINE=95112788; PubMed=7813418;
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.,
RA   Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C.,
RA   Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M.,
RA   Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L.,
RA   Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J.,
RA   Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T.,
RA   Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A.,
RA   Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B.,
RA   Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I.,
RA   Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M.,
RA   Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A.,
RA   van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I.,
RA   Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H.,
RA   Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.;
RT   "Complete DNA sequence of yeast chromosome II.";
RL   EMBO J. 13:5795-5809(1994).
RN   [4]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [5]
RP   INTERACTION WITH NAP1, AND 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: 5,10-methylenetetrahydrofolate + glycine +
CC       H(2)O = tetrahydrofolate + L-serine.
CC   -!- COFACTOR: Pyridoxal phosphate.
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate pathway.
CC   -!- SUBUNIT: Homotetramer (By similarity). Interacts with NAP1.
CC   -!- INTERACTION:
CC       P23255:TAF2; NbExp=1; IntAct=EBI-7748, EBI-18862;
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.
CC   -!- SIMILARITY: Belongs to the SHMT family.
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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   PIR; S29348; S29348.
DR   RefSeq; NP_009822.2; -.
DR   HSSP; P07511; 1CJ0.
DR   DIP; DIP:4952N; -.
DR   IntAct; P37292; 12.
DR   STRING; P37292; -.
DR   PeptideAtlas; P37292; -.
DR   Ensembl; YBR263W; YBR263W; YBR263W; Saccharomyces cerevisiae.
DR   GeneID; 852565; -.
DR   GenomeReviews; Y13134_GR; YBR263W.
DR   KEGG; sce:YBR263W; -.
DR   NMPDR; fig|4932.3.peg.538; -.
DR   CYGD; YBR263w; -.
DR   SGD; S000000467; SHM1.
DR   HOGENOM; P37292; -.
DR   OMA; P37292; QVIDNAQ.
DR   BRENDA; 2.1.2.1; 250.
DR   NextBio; 971682; -.
DR   ArrayExpress; P37292; -.
DR   GermOnline; YBR263W; Saccharomyces cerevisiae.
DR   GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR   GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IMP:SGD.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006544; P:glycine metabolic process; IEA:InterPro.
DR   GO; GO:0006563; P:L-serine metabolic process; IEA:InterPro.
DR   GO; GO:0006730; P:one-carbon compound metabolic process; IMP:SGD.
DR   GO; GO:0009070; P:serine family amino acid biosynthetic process; IGI:SGD.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR001085; Ser_HO-MeTrfase.
DR   InterPro; IPR019798; Ser_HO-MeTrfase_PLP_BS.
DR   Gene3D; G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1.
DR   PANTHER; PTHR11680; Gly_HO-Metrfase; 1.
DR   Pfam; PF00464; SHMT; 1.
DR   PIRSF; PIRSF000412; SHMT; 1.
DR   PROSITE; PS00096; SHMT; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Mitochondrion; One-carbon metabolism;
KW   Pyridoxal phosphate; Transferase; Transit peptide.
FT   TRANSIT       1     20       Mitochondrion (Potential).
FT   CHAIN        21    490       Serine hydroxymethyltransferase,
FT                                mitochondrial.
FT                                /FTId=PRO_0000032568.
FT   MOD_RES     265    265       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
FT   CONFLICT     72     72       L -> S (in Ref. 1; AAA21024).
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
//