ID   CSD_THEMA               Reviewed;         413 AA.
AC   Q9X191;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 120.
DE   RecName: Full=Probable cysteine desulfurase;
DE            EC=2.8.1.7;
GN   Name=csd; OrderedLocusNames=TM_1371;
OS   Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS   / MSB8).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=243274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=10360571; DOI=10.1038/20601;
RA   Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA   Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA   Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA   Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA   Smith H.O., Venter J.C., Fraser C.M.;
RT   "Evidence for lateral gene transfer between Archaea and Bacteria from
RT   genome sequence of Thermotoga maritima.";
RL   Nature 399:323-329(1999).
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; AE000512; AAD36460.1; -; Genomic_DNA.
DR   PIR; D72260; D72260.
DR   RefSeq; NP_229172.1; NC_000853.1.
DR   RefSeq; WP_004081567.1; NZ_CP011107.1.
DR   AlphaFoldDB; Q9X191; -.
DR   SMR; Q9X191; -.
DR   STRING; 243274.THEMA_07480; -.
DR   EnsemblBacteria; AAD36460; AAD36460; TM_1371.
DR   KEGG; tma:TM1371; -.
DR   eggNOG; COG0520; Bacteria.
DR   InParanoid; Q9X191; -.
DR   OMA; HKLCGPT; -.
DR   OrthoDB; 446447at2; -.
DR   Proteomes; UP000008183; 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; 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   Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..413
FT                   /note="Probable cysteine desulfurase"
FT                   /id="PRO_0000150319"
FT   ACT_SITE        363
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         223
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   413 AA;  46749 MW;  092866323FF984F0 CRC64;
     MLSTGLYEDF PTLKMKINGK RIVYLDSAAT TLKPKQVVKK LEEFYYNSYA NVHRAVHTLA
     VRATTEFEET REEFAEFLGA SPEEIIFTSG TTMAINLAVV SLLRSGILKE DDLVLVSLLE
     HHANFVPWLR LSKFHGYRID FIRPSGRFGT LEMDDLLKHR DKNPKVVAIT GLSNVTGQRI
     PVEELRNVFP NSIILLDGAQ LIPHEPVKPK EIGVDFLAFS LHKMLGPTGV GVLYGKREVL
     EQMEPFLYGG EMIDRVSLED VTFNELPYKF EAGTPNIADI VASREALRYL KETGFDSVHE
     KIEQLTQMAL KEMMKIGGVE IYGPLDERQH GIVSFNVKGI HPHDVAHILD QEFGIAVRSG
     HHCAQPLMSI LKEQSQIDFP NSTCRASFYI YNTEEDVKIL VEGVKKVKEW FSR