ID   MET7_SCHPO              Reviewed;         610 AA.
AC   O74314; Q9USA0;
DT   23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 121.
DE   RecName: Full=Probable cystathionine gamma-synthase;
DE            EC=2.5.1.48;
DE   AltName: Full=O-succinylhomoserine (thiol)-lyase;
GN   ORFNames=SPBC15D4.09c;
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-213, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=ATCC 38364 / 968;
RX   PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA   Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA   Hiraoka Y.;
RT   "Large-scale screening of intracellular protein localization in living
RT   fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL   Genes Cells 5:169-190(2000).
CC   -!- FUNCTION: Catalyzes the formation of L-cystathionine from O-succinyl-L-
CC       homoserine (OSHS) and L-cysteine, via a gamma-replacement reaction. In
CC       the absence of thiol, catalyzes gamma-elimination to form 2-
CC       oxobutanoate, succinate and ammonia (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-cysteine + O-succinyl-L-homoserine = H(+) + L,L-
CC         cystathionine + succinate; Xref=Rhea:RHEA:20397, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:35235, ChEBI:CHEBI:57661,
CC         ChEBI:CHEBI:58161; EC=2.5.1.48;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC       pathway; L-cystathionine from O-succinyl-L-homoserine: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10759889}. Nucleus
CC       {ECO:0000269|PubMed:10759889}.
CC   -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family. MET7
CC       subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CU329671; CAA20484.1; -; Genomic_DNA.
DR   EMBL; AB027923; BAA87227.1; -; Genomic_DNA.
DR   PIR; T39485; T39485.
DR   RefSeq; NP_596249.1; NM_001022168.2.
DR   AlphaFoldDB; O74314; -.
DR   SMR; O74314; -.
DR   BioGRID; 276299; 1.
DR   STRING; 4896.SPBC15D4.09c.1; -.
DR   MaxQB; O74314; -.
DR   PaxDb; O74314; -.
DR   EnsemblFungi; SPBC15D4.09c.1; SPBC15D4.09c.1:pep; SPBC15D4.09c.
DR   GeneID; 2539747; -.
DR   KEGG; spo:SPBC15D4.09c; -.
DR   PomBase; SPBC15D4.09c; -.
DR   VEuPathDB; FungiDB:SPBC15D4.09c; -.
DR   eggNOG; KOG0053; Eukaryota.
DR   HOGENOM; CLU_011302_1_0_1; -.
DR   InParanoid; O74314; -.
DR   OMA; DVYLFPS; -.
DR   PhylomeDB; O74314; -.
DR   UniPathway; UPA00051; UER00077.
DR   PRO; PR:O74314; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0003962; F:cystathionine gamma-synthase activity; ISS:PomBase.
DR   GO; GO:0102028; F:cystathionine gamma-synthase activity (acts on O-phosphohomoserine); IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019281; P:L-methionine biosynthetic process from homoserine via O-succinyl-L-homoserine and cystathionine; ISS:PomBase.
DR   GO; GO:0009086; P:methionine biosynthetic process; EXP:PomBase.
DR   GO; GO:0019346; P:transsulfuration; IBA:GO_Central.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; Methionine biosynthesis; Nucleus;
KW   Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..610
FT                   /note="Probable cystathionine gamma-synthase"
FT                   /id="PRO_0000114780"
FT   MOD_RES         427
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   610 AA;  68968 MW;  129F54785ADC71EF CRC64;
     MSANISYLVN PPTEVGSSIP ADTEHAISVT LPTWKSNVGY EEGDPNVTTK MKSGYPRFFI
     SAHVKDCISI IKKFPEIEIL KLKDYDMFLY PSLSVAKQSA AFLESKGPID SAEVIIYDAT
     KGLRKHLDSI DRNRKYTEEI HIPQVYSVLF PSKYFGIAKQ FWQHTGDGIS SRRAAAFLHS
     YKKIQSISEF LVAQRSISHL KSKSRSRYAS HPDLQALNTW MTNEGNQAND EMEDVSLYLE
     ERYGRNLDLS LATAAKLVLR RRIAGTLKDE VDLQKALPKE GSQYLREVKG LSHDDVFLFP
     TGMSAIYNTH RILRLVLDDS RKSVCFGFCY VDTLKILQKW GSGCYFYGLG NDEQLDEFEK
     RLESGEKVMA LFCEFPSNPL LNSPDLVRIR KLADSYDFAV VVDETIGNFV NVEVLPLADV
     VVSSLTKIFS GDSNVMGGSM VLNPSSRYYS RIKDAMKALY EDLLYDEDAL TLERNSRDFA
     ERSQVINHNA ETICNLLYQN PKIKTLYYPK YNTSKEHFEA CRRENGGYGG LLSVVFHNPE
     DARQFYDKIQ VAKGPSLGTN FTLASPYAIL AHYQELDWAG ENGIDRNLVR VSVGMEPSEH
     LKNVFINALS