ID   CSD_MYCTO               Reviewed;         417 AA.
AC   P9WQ68; L0T9P9; O53155; P63516;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 37.
DE   RecName: Full=Probable cysteine desulfurase;
DE            EC=2.8.1.7;
GN   Name=csd; OrderedLocusNames=MT1511;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(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; AE000516; AAK45775.1; -; Genomic_DNA.
DR   PIR; C70872; C70872.
DR   RefSeq; WP_003407490.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WQ68; -.
DR   SMR; P9WQ68; -.
DR   EnsemblBacteria; AAK45775; AAK45775; MT1511.
DR   GeneID; 45425442; -.
DR   KEGG; mtc:MT1511; -.
DR   PATRIC; fig|83331.31.peg.1625; -.
DR   HOGENOM; CLU_003433_2_5_11; -.
DR   Proteomes; UP000001020; 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; 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.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate; Transferase.
FT   CHAIN           1..417
FT                   /note="Probable cysteine desulfurase"
FT                   /id="PRO_0000426828"
FT   ACT_SITE        373
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         233
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   417 AA;  44596 MW;  8247BE35BFF83736 CRC64;
     MTASVNSLDL AAIRADFPIL KRIMRGGNPL AYLDSGATSQ RPLQVLDAER EFLTASNGAV
     HRGAHQLMEE ATDAYEQGRA DIALFVGADT DELVFTKNAT EALNLVSYVL GDSRFERAVG
     PGDVIVTTEL EHHANLIPWQ ELARRTGATL RWYGVTDDGR IDLDSLYLDD RVKVVAFTHH
     SNVTGVLTPV SELVSRAHQS GALTVLDACQ SVPHQPVDLH ELGVDFAAFS GHKMLGPNGI
     GVLYGRRELL AQMPPFLTGG SMIETVTMEG ATYAPAPQRF EAGTPMTSQV VGLAAAARYL
     GAIGMAAVEA HERELVAAAI EGLSGIDGVR ILGPTSMRDR GSPVAFVVEG VHAHDVGQVL
     DDGGVAVRVG HHCALPLHRR FGLAATARAS FAVYNTADEV DRLVAGVRRS RHFFGRA