ID   CYD_MYCLE               Reviewed;         611 AA.
AC   O32975;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Probable cysteine desulfurase 1;
DE            EC=2.8.1.7;
GN   Name=cyd {ECO:0000250|UniProtKB:Q8KUU5}; Synonyms=csd1;
GN   OrderedLocusNames=ML0842; ORFNames=MLCB22.44c;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
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: Cargo protein of a type 2A encapsulin nanocompartment
CC       involved in sulfur metabolism. Cysteine desulfurases mobilize the
CC       sulfur from L-cysteine to yield L-alanine, an essential step in sulfur
CC       metabolism for biosynthesis of a variety of sulfur-containing
CC       biomolecules. {ECO:0000250|UniProtKB:Q8KUU5}.
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:Q8KUU5};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:P77444};
CC   -!- SUBUNIT: There are 1-2 copies of this protein in each type 2A
CC       encapsulin shell. {ECO:0000250|UniProtKB:Q8KUU5}.
CC   -!- SUBCELLULAR LOCATION: Encapsulin nanocompartment
CC       {ECO:0000250|UniProtKB:Q8KUU5}.
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. Csd subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAC31223.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; Z98741; CAB11409.1; -; Genomic_DNA.
DR   EMBL; AL583920; CAC31223.1; ALT_INIT; Genomic_DNA.
DR   PIR; D87014; D87014.
DR   PIR; T44909; T44909.
DR   RefSeq; WP_010907960.1; NC_002677.1.
DR   AlphaFoldDB; O32975; -.
DR   SMR; O32975; -.
DR   STRING; 272631.ML0842; -.
DR   EnsemblBacteria; CAC31223; CAC31223; CAC31223.
DR   KEGG; mle:ML0842; -.
DR   Leproma; ML0842; -.
DR   eggNOG; COG0520; Bacteria.
DR   HOGENOM; CLU_003433_2_5_11; -.
DR   Proteomes; UP000000806; Chromosome.
DR   GO; GO:0140737; C:encapsulin nanocompartment; IC:UniProtKB.
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; 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.
PE   3: Inferred from homology;
KW   Encapsulin nanocompartment; Pyridoxal phosphate; Reference proteome;
KW   Transferase.
FT   CHAIN           1..611
FT                   /note="Probable cysteine desulfurase 1"
FT                   /id="PRO_0000150301"
FT   REGION          1..208
FT                   /note="Cargo-loading domain"
FT                   /evidence="ECO:0000250|UniProtKB:Q8KUU5"
FT   ACT_SITE        566
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P77444"
FT   MOD_RES         428
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P77444"
SQ   SEQUENCE   611 AA;  64812 MW;  82F5C187A624AF26 CRC64;
     MRATQLYAAS FRPGFDSPPQ LVPVALRGSA PDTTTVASAG ELAVGTTDPC PAPVAQIGVA
     DVYVPAPTSP EPEGLPQVAP VFSRGNVPDT TAVPAAAGTT VGVADPYLPP GVGHLSGFAV
     PSHGIVPTVP GVLAGGPPTA PVAPRNSAPV LRPEWPYHVP SVSDLDWFDA VPAGVPGGDE
     HNYNFLIAAP QVPRLADEHE MVDVFDIQAV RADFPILQET VNGKPLIWFD NAATTQKPQV
     VIDRLSYFYA HENSNIHRAA HELAARATDA YEEARETARR FIGAAKAQEI IFVRGTTEAI
     NLVAYAWGGK HLQPGDEVVI THLEHHANIV PWQLLSSQTG AILKVAPVDD AGNLLMSEFE
     DLLGPRTKLV AATQVSNALG TVTQGEKIVE LGHRYGARVL IDGAQSIPHL PINVSELGAD
     FFVFSGHKIY GPTGIGVLYG CEDVLTEMPP WQGGGNMIVD VTLERSLYQG PPNKFEAGTG
     NIADAVGLGE ALRYVERVGV QRIASHEQAL LDYATPRLAD IPGVRLVGTA TEKASVLSFV
     LAGHEPLEVG KALNAEGIAV RAGHHCAQPV LRRLGLEATV RPSFAFYNTY EEIDVFINVV
     RRIAEGGTNI G