ID   CYSA_STRCO              Reviewed;         392 AA.
AC   Q59829; Q9S1N0;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   25-MAY-2022, entry version 126.
DE   RecName: Full=Putative cystathionine gamma-lyase;
DE            EC=4.4.1.1;
DE   AltName: Full=Gamma-cystathionase;
GN   Name=cysA; OrderedLocusNames=SCO3920; ORFNames=SCQ11.03c;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A3(2) / 1147;
RA   Strohl W.R.;
RL   Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-205.
RC   STRAIN=A3(2) / 1147;
RX   PubMed=8550407; DOI=10.1128/jb.178.1.136-142.1996;
RA   Li Y., Strohl W.R.;
RT   "Cloning, purification, and properties of a phosphotyrosine protein
RT   phosphatase from Streptomyces coelicolor A3(2).";
RL   J. Bacteriol. 178:136-142(1996).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L,L-cystathionine = 2-oxobutanoate + L-cysteine +
CC         NH4(+); Xref=Rhea:RHEA:14005, ChEBI:CHEBI:15377, ChEBI:CHEBI:16763,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:35235, ChEBI:CHEBI:58161; EC=4.4.1.1;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC       from L-homocysteine and L-serine: step 2/2.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC       {ECO:0000305}.
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DR   EMBL; U37580; AAC43615.1; -; Genomic_DNA.
DR   EMBL; AL939118; CAB46958.1; -; Genomic_DNA.
DR   PIR; T37173; T37173.
DR   RefSeq; NP_628105.1; NC_003888.3.
DR   RefSeq; WP_011029309.1; NZ_VNID01000003.1.
DR   AlphaFoldDB; Q59829; -.
DR   SMR; Q59829; -.
DR   STRING; 100226.SCO3920; -.
DR   GeneID; 1099356; -.
DR   KEGG; sco:SCO3920; -.
DR   PATRIC; fig|100226.15.peg.3994; -.
DR   eggNOG; COG0626; Bacteria.
DR   HOGENOM; CLU_018986_2_2_11; -.
DR   InParanoid; Q59829; -.
DR   OMA; GPYTYGR; -.
DR   PhylomeDB; Q59829; -.
DR   UniPathway; UPA00136; UER00202.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016846; F:carbon-sulfur lyase activity; IBA:GO_Central.
DR   GO; GO:0004123; F:cystathionine gamma-lyase activity; IBA:GO_Central.
DR   GO; GO:0003962; F:cystathionine gamma-synthase activity; IBA:GO_Central.
DR   GO; GO:0080146; F:L-cysteine desulfhydrase activity; IEA:UniProtKB-EC.
DR   GO; GO:0044540; F:L-cystine L-cysteine-lyase (deaminating); 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: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; 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   PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cysteine biosynthesis; Cytoplasm; Lyase;
KW   Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..392
FT                   /note="Putative cystathionine gamma-lyase"
FT                   /id="PRO_0000114755"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         216
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        118
FT                   /note="P -> R (in Ref. 1 and 3)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        384
FT                   /note="L -> V (in Ref. 1; AAC43615)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   392 AA;  41368 MW;  0B4A25355B1732C9 CRC64;
     MSDSATTDSA GTGGERSASA PGDGTRAVRA GLPEPVKHEP TLPGPVFAAH FHLPGDPTGP
     YTYGRDENPT WTRLESAIGE LEAPGEAGVE TLVFASGMAA ISSVLFSQLR AGDTAVLPDD
     GYQALPLVRA QLEAYGIEVR TAPTGRDAQL DVLDGAKLLW IETPSNPGLD VCDVRRLVEA
     AHAGGALVAV DNTLATPLGQ RPLELGADFS VASGTKQLTG HGDVLLGYVA GRDAGAMAAV
     RRWRKIVGAI PGPMEAWLAH RSIATLQLRV DRQDSTALKV AEALRTRPEI TGLRYPGLPD
     DPSHKVASQQ MLRYGCVVSF TLPSRARADR FLDALRLVEG ATSFGGVRST AERRGRWGGD
     AVPEGFIRLS VGAEDPDDLV ADLLRALDET TE