ID   CSD_STRCO               Reviewed;         418 AA.
AC   Q9XAD5;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Probable cysteine desulfurase;
DE            EC=2.8.1.7;
GN   Name=csd; OrderedLocusNames=SCO1921; ORFNames=SCC22.03c;
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 [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).
CC   -!- FUNCTION: Catalyzes the removal of elemental sulfur and selenium atoms
CC       from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to
CC       produce L-alanine. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-
CC         alanine; Xref=Rhea:RHEA:43892, Rhea:RHEA-COMP:14737, Rhea:RHEA-
CC         COMP:14739, ChEBI:CHEBI:29917, ChEBI:CHEBI:35235, ChEBI:CHEBI:57972,
CC         ChEBI:CHEBI:64428; EC=2.8.1.7;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. Csd subfamily. {ECO:0000305}.
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DR   EMBL; AL939110; CAB50746.1; -; Genomic_DNA.
DR   PIR; T35993; T35993.
DR   RefSeq; NP_626186.1; NC_003888.3.
DR   RefSeq; WP_003976898.1; NZ_VNID01000001.1.
DR   AlphaFoldDB; Q9XAD5; -.
DR   SMR; Q9XAD5; -.
DR   STRING; 100226.SCO1921; -.
DR   GeneID; 1097355; -.
DR   KEGG; sco:SCO1921; -.
DR   PATRIC; fig|100226.15.peg.1947; -.
DR   eggNOG; COG0520; Bacteria.
DR   HOGENOM; CLU_003433_2_5_11; -.
DR   InParanoid; Q9XAD5; -.
DR   OMA; PVCLRYG; -.
DR   PhylomeDB; Q9XAD5; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:0006534; P:cysteine metabolic process; IEA:InterPro.
DR   CDD; cd06453; SufS_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR010970; Cys_dSase_SufS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01979; sufS; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..418
FT                   /note="Probable cysteine desulfurase"
FT                   /id="PRO_0000150317"
FT   ACT_SITE        376
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         236
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   418 AA;  45902 MW;  7B510207857BE189 CRC64;
     MTQLPGLLDT EAIRKDFPIL DRQVHDGHKL VYLDNAATSQ KPRQVLDALS EYYERYNANV
     HRGVHVLAEE ATALYEGARD KVAEFINAPS RDEVIFTKNA SESLNLVANM LGWADDPYRV
     DHETEIVITE MEHHSNIVPW QLLAQRTGAK LRWFGLTDDG RLDLSNIDEV ITEKTKVVSF
     VLVSNILGTQ NPVEAIVRRA QEVGALVCID ASQAAPHMPL DVQALQADFV AFTGHKMCGP
     TGIGVLWGRQ ELLEDLPPFL GGGEMIETVS MHSSTYAPAP HKFEAGTPPV AQAVGLGAAI
     DYLNSIGMDK ILAHEHALTE YAVKRLLEVP DLRIIGPTTA EERGAAISFT LGDIHPHDVG
     QVLDEQGIAV RVGHHCARPV CLRYGIPATT RASFYLYSTP AEIDALVDGL EHVRNFFG