ID   CSD2_MYCLE              Reviewed;         418 AA.
AC   Q49690;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 118.
DE   RecName: Full=Probable cysteine desulfurase 2;
DE            EC=2.8.1.7;
GN   Name=csd2; OrderedLocusNames=ML0596; ORFNames=B1496_C2_193, MLCL536.25c;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Smith D.R., Robison K.;
RL   Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
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; U00013; AAA17128.1; -; Genomic_DNA.
DR   EMBL; Z99125; CAB16168.1; -; Genomic_DNA.
DR   EMBL; AL583919; CAC30104.1; -; Genomic_DNA.
DR   PIR; S72761; S72761.
DR   RefSeq; NP_301505.1; NC_002677.1.
DR   RefSeq; WP_010907829.1; NC_002677.1.
DR   AlphaFoldDB; Q49690; -.
DR   SMR; Q49690; -.
DR   STRING; 272631.ML0596; -.
DR   EnsemblBacteria; CAC30104; CAC30104; CAC30104.
DR   KEGG; mle:ML0596; -.
DR   PATRIC; fig|272631.5.peg.1034; -.
DR   Leproma; ML0596; -.
DR   eggNOG; COG0520; Bacteria.
DR   HOGENOM; CLU_003433_2_5_11; -.
DR   OMA; HKLCGPT; -.
DR   Proteomes; UP000000806; 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; Reference proteome; Transferase.
FT   CHAIN           1..418
FT                   /note="Probable cysteine desulfurase 2"
FT                   /id="PRO_0000150302"
FT   ACT_SITE        374
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         234
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   418 AA;  44894 MW;  978FC5977B2B5DFB CRC64;
     MTISLTPLDL SAIRADFPIL KRVMRGGNQL AYLDSGATSQ RPVQVLDAER EFLVTSNGAV
     HRGAHQLMEE ATDAYERGRV DIAAFIGAAA DELVFTKNAT ESLNLVSYVF GDNRFEGTSG
     DGGDVIVTTE LEHHANLIPW QELARRIGAT LRWYGVTDDG QIDLDSLQLD ERVKVVAFSH
     HSNVTGAVAP VRELVARAKE VGALTVLDAC QSVPHQPVDL HGLGVDFAAF SGHKMLGPNG
     IGVLYARREL LSVMPPFLTG GSMIETVTME STTYAPAPQR FEAGTPMTSQ VVGLAAAARY
     LDAIGMKAVE AHERELVAAA VEGLSRIDGV RIIGPKSMEN RGSPVSFVVD GVHAHDIGQV
     LDDDGVAVRV GHHCALPLHR RFALAATARA SFAVYNTVDE VDRLVAGVLR ALDFFGRE