ID   CSD_STAES               Reviewed;         413 AA.
AC   Q8CTA4;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=Probable cysteine desulfurase;
DE            EC=2.8.1.7;
GN   Name=csd; OrderedLocusNames=SE_0608;
OS   Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12228 / FDA PCI 1200;
RX   PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA   Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA   Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
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; AE015929; AAO04205.1; -; Genomic_DNA.
DR   RefSeq; NP_764163.1; NC_004461.1.
DR   RefSeq; WP_002485415.1; NZ_WBME01000029.1.
DR   AlphaFoldDB; Q8CTA4; -.
DR   SMR; Q8CTA4; -.
DR   STRING; 176280.SE_0608; -.
DR   EnsemblBacteria; AAO04205; AAO04205; SE_0608.
DR   KEGG; sep:SE_0608; -.
DR   PATRIC; fig|176280.10.peg.579; -.
DR   eggNOG; COG0520; Bacteria.
DR   HOGENOM; CLU_003433_2_5_9; -.
DR   OMA; HKLCGPT; -.
DR   Proteomes; UP000001411; 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: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; IPR016454; Cysteine_dSase.
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   PIRSF; PIRSF005572; NifS; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01979; sufS; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate; Transferase.
FT   CHAIN           1..413
FT                   /note="Probable cysteine desulfurase"
FT                   /id="PRO_0000150315"
FT   ACT_SITE        368
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         229
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   413 AA;  46021 MW;  0F29E092C37F272E CRC64;
     MAEHSFDVKA VIKDFPILEQ KVNNKRLAYL DSTATSQTPV QVLNVLDDYY KRYNSNVHRG
     VHTLGSLATD GYENARETVR RFINAKYFEE IIFTRGTTAS INIVAHSYGD ANISEGDEIV
     VTEMEHHANI VPWQQLAKRK NATLKFIPMT KDGELQLDDI KATINDKTKI VAIAHVSNVL
     GTINDVKTIA KIAHEHGAVI SVDGAQSAPH MALDMQDIDA DFYSFSGHKM LGPTGIGVLY
     GKRELLQNME PVEFGGDMID FVSKYDSTWA DLPTKFEAGT PLIAQAIGLA EAIHYIENLG
     FNAIHQHEKE LTEYAYEQML TIDGLEIYGP PKDRRAGVIT FNLADIHPHD VATAVDTEGV
     AVRAGHHCAQ PLMKWLGVSS TARASFYVYN TKEDVDQLVQ ALKQTKEFFS YEF