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MET7_NEUCR
ID   MET7_NEUCR              Reviewed;         621 AA.
AC   P38675; Q7RV94;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 3.
DT   25-MAY-2022, entry version 126.
DE   RecName: Full=Cystathionine gamma-synthase;
DE            EC=2.5.1.48;
DE   AltName: Full=O-succinylhomoserine (thiol)-lyase;
GN   Name=met-7; ORFNames=NCU02430;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 49-621.
RX   PubMed=1531800; DOI=10.1016/0378-1119(92)90698-o;
RA   Crawford J.M., Geever R.F., Asch D.K., Case M.E.;
RT   "Sequence and characterization of the met-7 gene of Neurospora crassa.";
RL   Gene 111:265-266(1992).
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   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC       pathway; L-cystathionine from O-succinyl-L-homoserine: step 1/1.
CC   -!- SUBUNIT: Both met-3 and met-7 are required to form a functional
CC       cystathionine gamma-synthase.
CC   -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family. MET7
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CM002242; EAA30199.2; -; Genomic_DNA.
DR   EMBL; M64066; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; JQ1524; JQ1524.
DR   RefSeq; XP_959435.2; XM_954342.3.
DR   AlphaFoldDB; P38675; -.
DR   SMR; P38675; -.
DR   STRING; 5141.EFNCRP00000003145; -.
DR   EnsemblFungi; EAA30199; EAA30199; NCU02430.
DR   GeneID; 3875582; -.
DR   KEGG; ncr:NCU02430; -.
DR   VEuPathDB; FungiDB:NCU02430; -.
DR   HOGENOM; CLU_011302_1_0_1; -.
DR   InParanoid; P38675; -.
DR   OMA; FPVAKQY; -.
DR   UniPathway; UPA00051; UER00077.
DR   Proteomes; UP000001805; Chromosome 7, Linkage Group VII.
DR   GO; GO:0003962; F:cystathionine gamma-synthase activity; IBA:GO_Central.
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:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
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.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Methionine biosynthesis; Pyridoxal phosphate;
KW   Reference proteome; Transferase.
FT   CHAIN           1..621
FT                   /note="Cystathionine gamma-synthase"
FT                   /id="PRO_0000114779"
FT   MOD_RES         429
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        194
FT                   /note="R -> A (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   621 AA;  68938 MW;  7A3B6166218B162A CRC64;
     MPPFELGDPI PSETAHAVSV SLPTWSANVG YEEGQDWVVK RMATGYPRFF IHRTIQAFAA
     DIVATHVSTK AKRTSDITAM LFPTPTIASR CVDFIRSRAP ADVCSNIEVV NLVLDMSDPE
     ARALEPLCPS ISAVIMPQDG FPFAKQYWQH SGDGVSSRRA EFCHGLFKDG LLRPDTELRN
     AAVSAAKPCR GPKRYQRQAS LDAGGNQQTI MHGHIHRATG ETAMIQETSR FLEERFGRNL
     DLSFVHPAKS AIKRRIAGAL RSADHDLGGS PSLSEKQMSS NTRGIANLRE EDIYLFPCGM
     NAIFHAHRAL YSIRTPPGST PLKSVNFGFP YVDTLKILEK FNPSGALFYG HGSKSDLDDL
     ETRLESGERY LALFCEFPGN PLLTCPDLVR IRELADKYEF AVVVDETIGT FANVNVLQFA
     DIVVSSLTKI FSGDCNVMGG GAIFNPNSRY YSALKSFVQQ QLEDTYWPED VIFMERNSRD
     FVARIDRVNA NAEAICRVLQ DHPLVKTLYY PKYNDSRANY EAVKLPQGGY GGLISVVLKG
     KKQAVAFYDA IETAKGPSLG TNFTLTSPYV LLAHYQELDW AEQYGVDRNL IRISVGLEGT
     DELINVFTRA LKVAEEQSQY P
 
 
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