ID   CSD_STAEQ               Reviewed;         413 AA.
AC   Q5HQQ0;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Probable cysteine desulfurase;
DE            EC=2.8.1.7;
GN   Name=csd; OrderedLocusNames=SERP0498;
OS   Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35984 / RP62A;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
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; CP000029; AAW53865.1; -; Genomic_DNA.
DR   RefSeq; WP_002438997.1; NC_002976.3.
DR   AlphaFoldDB; Q5HQQ0; -.
DR   SMR; Q5HQQ0; -.
DR   STRING; 176279.SERP0498; -.
DR   EnsemblBacteria; AAW53865; AAW53865; SERP0498.
DR   KEGG; ser:SERP0498; -.
DR   eggNOG; COG0520; Bacteria.
DR   HOGENOM; CLU_003433_2_5_9; -.
DR   OMA; HKLCGPT; -.
DR   OrthoDB; 446447at2; -.
DR   Proteomes; UP000000531; 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; Reference proteome; Transferase.
FT   CHAIN           1..413
FT                   /note="Probable cysteine desulfurase"
FT                   /id="PRO_0000150316"
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;  46005 MW;  1C08DFB20F7EC72E 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 FVSKYDATWA DLPTKFEAGT PLIAQAIGLA EAIHYIENLG
     FNAIHQHEKE LTEYAYEQML TIDGLEIYGP PKDRRAGVIT FNLADIHPHD VATAVDTEGV
     AVRAGHHCAQ PLMKWLGVSS TARASFYVYN TKEDVDQLVQ ALKQTKEFFS YEF