ID   CBL_NEUCR               Reviewed;         457 AA.
AC   Q1K8G0; Q96VU8;
DT   24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=Cystathionine beta-lyase;
DE            EC=4.4.1.13 {ECO:0000269|PubMed:14209950};
DE   AltName: Full=Cysteine-S-conjugate beta-lyase;
GN   Name=met-2; ORFNames=NCU07987.1;
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 [GENOMIC DNA].
RA   Reveal B.S., Paietta J.V.;
RT   "Molecular cloning and regulatory analysis of the cystathionine beta- and
RT   gamma-lyase genes of Neurospora crassa.";
RL   Fungal Genet. Newsl. 47S:29-29(2001).
RN   [2]
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   [3]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=14209950;
RA   Flavin M., Slaughter C.;
RT   "Cystathionine cleavage enzymes of Neurospora.";
RL   J. Biol. Chem. 239:2212-2219(1964).
CC   -!- FUNCTION: Involved in de novo synthesis of methionine.
CC       {ECO:0000269|PubMed:14209950}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L,L-cystathionine = L-homocysteine + NH4(+) + pyruvate;
CC         Xref=Rhea:RHEA:13965, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:58161, ChEBI:CHEBI:58199;
CC         Evidence={ECO:0000269|PubMed:14209950};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an S-substituted L-cysteine + H2O = a thiol + NH4(+) +
CC         pyruvate; Xref=Rhea:RHEA:18121, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:29256, ChEBI:CHEBI:58717; EC=4.4.1.13;
CC         Evidence={ECO:0000269|PubMed:14209950};
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-homocysteine from L-cystathionine: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC       {ECO:0000305}.
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DR   EMBL; AF401237; AAK94039.1; -; Genomic_DNA.
DR   EMBL; CM002239; EAA33421.1; -; Genomic_DNA.
DR   RefSeq; XP_962657.1; XM_957564.3.
DR   AlphaFoldDB; Q1K8G0; -.
DR   SMR; Q1K8G0; -.
DR   STRING; 5141.EFNCRP00000008300; -.
DR   EnsemblFungi; EAA33421; EAA33421; NCU07987.
DR   GeneID; 3878796; -.
DR   KEGG; ncr:NCU07987; -.
DR   VEuPathDB; FungiDB:NCU07987; -.
DR   HOGENOM; CLU_018986_2_1_1; -.
DR   InParanoid; Q1K8G0; -.
DR   OMA; THGGIIV; -.
DR   BRENDA; 4.4.1.13; 3627.
DR   UniPathway; UPA00051; UER00078.
DR   Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016846; F:carbon-sulfur lyase activity; IBA:GO_Central.
DR   GO; GO:0004121; F:cystathionine beta-lyase activity; IEA:InterPro.
DR   GO; GO:0004123; F:cystathionine gamma-lyase activity; IBA:GO_Central.
DR   GO; GO:0047804; F:cysteine-S-conjugate beta-lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR   GO; GO:0071266; P:'de novo' L-methionine biosynthetic process; IEA:InterPro.
DR   GO; GO:0019343; P:cysteine biosynthetic process via cystathionine; IBA:GO_Central.
DR   GO; GO:0019346; P:transsulfuration; IBA:GO_Central.
DR   CDD; cd00614; CGS_like; 1.
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; IPR006238; Cys_b_lyase_euk.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11808; PTHR11808; 1.
DR   Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR   PIRSF; PIRSF001434; CGS; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01329; cysta_beta_ly_E; 1.
DR   PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Cytoplasm; Lyase; Methionine biosynthesis;
KW   Nucleus; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..457
FT                   /note="Cystathionine beta-lyase"
FT                   /id="PRO_0000422971"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   457 AA;  49160 MW;  5CBCE8615A3A2BBA CRC64;
     MSTPNSDSPA AQAAKKVFSR LDLDGHNLPP SPAPSSPHNG RRYALATELV YTETKDQYGA
     SSIPIYQSAT FKQSSSNGGS EYDYTRSGNP TRTHLERHLA KIMNANRCLS VSSGMGALDV
     ITRLLKPGDE VITGDDLYGG TNRLLTYLKN NQGVIVHHVD TTNVESVRQI ISPKTTMVLL
     ETPTNPLIKI CDIPTIARIT HEANEKAVVV VDNTMLSPML FNPLDVGADI VYESGTKYLS
     GHHDIMAGVI AVNDTELGDK LYFTINATGC GLSPNDSFLL MRGVKTLAIR MEKQQANAQR
     IAEFLESHGF KVRYPGLKSH PQYDLHWSMA RGAGAVLSFE TGDVALSERI VEAARLWGIS
     VSFGCVNSLI SMPCRMSHAS IDAKTRAERQ MPEDIIRLCV GIEDADDLID DLSRALVQAG
     AVTLTVDGFH ANTAEGAAAA AAGSEAAETT TTAAPSL