ID   ISCSL_MYCTO             Reviewed;         393 AA.
AC   P9WQ70; F2GP44; L0TE93; O53272; Q7D698;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=Iscs-like cysteine desulfurase {ECO:0000250|UniProtKB:P9WQ71};
DE            EC=2.8.1.7 {ECO:0000250|UniProtKB:P9WQ71};
GN   Name=iscS; OrderedLocusNames=MT3109;
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 from cysteine to
CC       produce alanine. {ECO:0000250|UniProtKB:P9WQ71}.
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         Evidence={ECO:0000250|UniProtKB:P9WQ71};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:P0A6B9};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P9WQ71}.
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. NifS/IscS subfamily. {ECO:0000305}.
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DR   EMBL; AE000516; AAK47439.1; -; Genomic_DNA.
DR   PIR; D70858; D70858.
DR   RefSeq; WP_003415911.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WQ70; -.
DR   SMR; P9WQ70; -.
DR   EnsemblBacteria; AAK47439; AAK47439; MT3109.
DR   KEGG; mtc:MT3109; -.
DR   PATRIC; fig|83331.31.peg.3351; -.
DR   HOGENOM; CLU_003433_0_0_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0044571; P:[2Fe-2S] cluster assembly; IEA:InterPro.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR010240; Cys_deSase_IscS.
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   PANTHER; PTHR11601:SF34; PTHR11601:SF34; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF005572; NifS; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   3: Inferred from homology;
KW   Aminotransferase; Iron; Iron-sulfur; Metal-binding; Pyridoxal phosphate;
KW   Transferase.
FT   CHAIN           1..393
FT                   /note="Iscs-like cysteine desulfurase"
FT                   /id="PRO_0000426827"
FT   ACT_SITE        329
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6B7"
FT   BINDING         68..69
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT   BINDING         154
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:O29689"
FT   BINDING         182
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT   BINDING         202..204
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT   BINDING         240
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT   BINDING         329
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /note="via persulfide group"
FT                   /evidence="ECO:0000250|UniProtKB:O29689"
FT   MOD_RES         205
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6B9"
SQ   SEQUENCE   393 AA;  40947 MW;  D8CF10B6F88C85A1 CRC64;
     MAYLDHAATT PMHPAAIEAM AAVQRTIGNA SSLHTSGRSA RRRIEEAREL IADKLGARPS
     EVIFTAGGTE SDNLAVKGIY WARRDAEPHR RRIVTTEVEH HAVLDSVNWL VEHEGAHVTW
     LPTAADGSVS ATALREALQS HDDVALVSVM WANNEVGTIL PIAEMSVVAM EFGVPMHSDA
     IQAVGQLPLD FGASGLSAMS VAGHKFGGPP GVGALLLRRD VTCVPLMHGG GQERDIRSGT
     PDVASAVGMA TAAQIAVDGL EENSARLRLL RDRLVEGVLA EIDDVCLNGA DDPMRLAGNA
     HFTFRGCEGD ALLMLLDANG IECSTGSACT AGVAQPSHVL IAMGVDAASA RGSLRLSLGH
     TSVEADVDAA LEVLPGAVAR ARRAALAAAG ASR