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GLYD_SCHPO
ID   GLYD_SCHPO              Reviewed;         467 AA.
AC   O13972;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 150.
DE   RecName: Full=Probable serine hydroxymethyltransferase, cytosolic;
DE            Short=SHMT;
DE            EC=2.1.2.1;
DE   AltName: Full=Glycine hydroxymethyltransferase;
DE   AltName: Full=Serine methylase;
GN   ORFNames=SPAC24C9.12c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
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         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; CU329670; CAB11269.1; -; Genomic_DNA.
DR   PIR; T38353; T38353.
DR   RefSeq; NP_594037.1; NM_001019462.2.
DR   AlphaFoldDB; O13972; -.
DR   SMR; O13972; -.
DR   BioGRID; 279105; 32.
DR   STRING; 4896.SPAC24C9.12c.1; -.
DR   iPTMnet; O13972; -.
DR   MaxQB; O13972; -.
DR   PaxDb; O13972; -.
DR   PRIDE; O13972; -.
DR   EnsemblFungi; SPAC24C9.12c.1; SPAC24C9.12c.1:pep; SPAC24C9.12c.
DR   GeneID; 2542651; -.
DR   KEGG; spo:SPAC24C9.12c; -.
DR   PomBase; SPAC24C9.12c; -.
DR   VEuPathDB; FungiDB:SPAC24C9.12c; -.
DR   eggNOG; KOG2467; Eukaryota.
DR   HOGENOM; CLU_022477_0_1_1; -.
DR   InParanoid; O13972; -.
DR   OMA; SHPAGLI; -.
DR   PhylomeDB; O13972; -.
DR   Reactome; R-SPO-196757; Metabolism of folate and pterines.
DR   UniPathway; UPA00193; -.
DR   PRO; PR:O13972; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; ISS:PomBase.
DR   GO; GO:0004372; F:glycine hydroxymethyltransferase activity; ISS:PomBase.
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..467
FT                   /note="Probable serine hydroxymethyltransferase, cytosolic"
FT                   /id="PRO_0000113515"
FT   MOD_RES         243
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   467 AA;  51861 MW;  0C21D7EF010C3725 CRC64;
     MSSNDSIMLT PLKEQDPTVA EIMRHEADRQ RSSVVLIASE NFTSRAVMDA LGSVMSNKYS
     EGYPGARYYG GNKFIDQIET LCQERALAAF NLDPAKWGVN VQCLSGSPAN MQVYQAIMPP
     HGRLMGLDLP SGGHLSHGYQ TDTKKISAVS TYFESMPYRV DPNTGLIDYD MLEHDAQLFR
     PKILVAGTSA YCRLIDYARM RQIADSVNAY LVVDMAHISG LVSAGVIPSP FEYADVVTTT
     THKSLRGPRG AMIFFRRGLR KHDKKGNPIY YDLEDKINFS VFPGHQGGPH NHTITALAVA
     LKQCQEPAYK EYQAQVVKNA KVCEEEFKKR GYKLAADGTD SHMVLVDVKS KGVDGARAER
     VLELINIVTN KNTVPSDKSA FSPSGIRVGT PAMTTRGFKE QDFVRVVDYI DRALTFAANL
     QKELPKDANK LKDFKAKLGE GEQYPELVQL QKEVAEWASS FPLADKW
 
 
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