ID   CSD_CHLTR               Reviewed;         401 AA.
AC   O84693;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 110.
DE   RecName: Full=Probable cysteine desulfurase;
DE            EC=2.8.1.7;
GN   Name=csd; OrderedLocusNames=CT_687;
OS   Chlamydia trachomatis (strain D/UW-3/Cx).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=272561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT   trachomatis.";
RL   Science 282:754-759(1998).
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; AE001273; AAC68282.1; -; Genomic_DNA.
DR   PIR; C71483; C71483.
DR   RefSeq; NP_220206.1; NC_000117.1.
DR   RefSeq; WP_009872062.1; NC_000117.1.
DR   AlphaFoldDB; O84693; -.
DR   SMR; O84693; -.
DR   STRING; 813.O172_03805; -.
DR   EnsemblBacteria; AAC68282; AAC68282; CT_687.
DR   GeneID; 884483; -.
DR   KEGG; ctr:CT_687; -.
DR   PATRIC; fig|272561.5.peg.756; -.
DR   HOGENOM; CLU_003433_2_5_0; -.
DR   InParanoid; O84693; -.
DR   OMA; HKLCGPT; -.
DR   Proteomes; UP000000431; 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; IPR020578; Aminotrans_V_PyrdxlP_BS.
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.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..401
FT                   /note="Probable cysteine desulfurase"
FT                   /id="PRO_0000150297"
FT   ACT_SITE        358
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         219
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   401 AA;  43747 MW;  0D97B29F3FB9EC19 CRC64;
     MYNVKKDFPI FKNQGDPYVY LDSAATTHKP QCVIDSIVDY YSSSYATVNR ALYTASHDIT
     FAHWQVRSKV GSWIGAQYDQ EIIFTRGTTS SLNLLAIAAN DSWLAGGTVV ISEAEHHANL
     VSWELACQRS GATIKKVRVD DEGMVDCSHL EQLLKQGVQL VSLAHVSNVS GAVLPLPEIA
     HLVHRYEALF AVDGAQGVGK GPLNLSEWGV DFYAFSGHKL YAPTGIGVLY GKKELLESLP
     PVEGGGDMVI VYDFEELSYQ EPPLRFEAGT PHIAGVLGLG AAIDYLQALP FSITDRLTEL
     THFLYEQLLT VPGIQIIGPK QGAARGSLCS ISIPGVQASD LGFLLDGRGI SVRSGHQCSQ
     PAMVRWDLGH VLRASLGIYN EQQDILLFVE ALKDILRAYR S