CBL_SCHPO
ID CBL_SCHPO Reviewed; 390 AA.
AC O94350;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 4.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Cystathionine beta-lyase;
DE Short=CBL;
DE EC=4.4.1.13;
DE AltName: Full=Beta-cystathionase;
DE AltName: Full=Cysteine lyase;
DE AltName: Full=Cysteine-S-conjugate beta-lyase;
GN Name=str3; ORFNames=SPCC11E10.01, SPCC61.06;
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 -!- 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 -!- 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 -!- 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; CU329672; CAA22275.2; -; Genomic_DNA.
DR RefSeq; NP_588197.2; NM_001023187.2.
DR AlphaFoldDB; O94350; -.
DR SMR; O94350; -.
DR BioGRID; 275592; 1.
DR STRING; 4896.SPCC11E10.01.1; -.
DR iPTMnet; O94350; -.
DR MaxQB; O94350; -.
DR PaxDb; O94350; -.
DR PRIDE; O94350; -.
DR EnsemblFungi; SPCC11E10.01.1; SPCC11E10.01.1:pep; SPCC11E10.01.
DR GeneID; 2539019; -.
DR KEGG; spo:SPCC11E10.01; -.
DR PomBase; SPCC11E10.01; -.
DR VEuPathDB; FungiDB:SPCC11E10.01; -.
DR eggNOG; KOG0053; Eukaryota.
DR HOGENOM; CLU_018986_2_1_1; -.
DR OMA; THGGIIV; -.
DR PhylomeDB; O94350; -.
DR UniPathway; UPA00051; UER00078.
DR PRO; PR:O94350; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; ISS:PomBase.
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:0019343; P:cysteine biosynthetic process via cystathionine; IBA:GO_Central.
DR GO; GO:0019279; P:L-methionine biosynthetic process from L-homoserine via cystathionine; IC:PomBase.
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 3: Inferred from homology;
KW Amino-acid biosynthesis; Cytoplasm; Lyase; Methionine biosynthesis;
KW Nucleus; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..390
FT /note="Cystathionine beta-lyase"
FT /id="PRO_0000352810"
FT MOD_RES 202
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 390 AA; 42773 MW; FBC40B8CF2D1CD60 CRC64;
MPSDCKYSVD TELVHVEGNE DQYHASSVPI YQSATFKQPC LEHMGKFDYT RSGNPTRSVL
QVHLAKLMKA KHAFVTSNGM SALDMILRCC KSNSHVVAGH DLYGGSDRLL SFNQRQYGFK
VDNVDTSDLA AFEAALRPDT NLVLIESPTN PRISICDIRA IVKITRSKAK DALLVMDNTM
LSPVLCNPLD FGYDIVYESA TKYLSGHHDL MGGVIATKSD EIAKSVFFNI NAMGAAMAPF
ECFLLLRGIK TMGLRVERAQ QNAIEIAKFL KSKGLQVNFP GLDPDAKSTA IFYSFARGPG
AVMSVFTGDV EVSKTIVNTT KLFEISVSFG AVNSLISMPA YMSHASIKKE VRDARGLSED
LIRICVGIEN VDDLKADLEN ALAQANFKQN
