ID   CSD_BORBU               Reviewed;         422 AA.
AC   O51111;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 122.
DE   RecName: Full=Probable cysteine desulfurase;
DE            EC=2.8.1.7;
GN   Name=csd; OrderedLocusNames=BB_0084;
OS   Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS   (Borrelia burgdorferi).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=224326;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX   PubMed=9403685; DOI=10.1038/37551;
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA   Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA   Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA   van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA   Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA   Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA   Smith H.O., Venter J.C.;
RT   "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL   Nature 390:580-586(1997).
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; AE000783; AAC66472.1; -; Genomic_DNA.
DR   PIR; D70110; D70110.
DR   RefSeq; NP_212218.1; NC_001318.1.
DR   RefSeq; WP_002656576.1; NC_001318.1.
DR   AlphaFoldDB; O51111; -.
DR   SMR; O51111; -.
DR   STRING; 224326.BB_0084; -.
DR   PRIDE; O51111; -.
DR   EnsemblBacteria; AAC66472; AAC66472; BB_0084.
DR   GeneID; 56568134; -.
DR   KEGG; bbu:BB_0084; -.
DR   PATRIC; fig|224326.49.peg.482; -.
DR   HOGENOM; CLU_003433_2_5_12; -.
DR   OMA; HKLCGPT; -.
DR   Proteomes; UP000001807; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:CAFA.
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; IPR016454; Cysteine_dSase.
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   PIRSF; PIRSF005572; NifS; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..422
FT                   /note="Probable cysteine desulfurase"
FT                   /id="PRO_0000150294"
FT   MOD_RES         235
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   422 AA;  48125 MW;  0D37CE39059C2EDD CRC64;
     MDFKQIKSNV EKVKFLRKDF PILNKKFDNK YIIYFDNAAT SQKPKNVIYS NVEYYENYNA
     NVHRSGHKFA IQSSIKIEKT RELVKNFINA ESAKNIIFTS GTTDGINTIA SSFFYSKYFK
     KKDEIILTTL EHNSNLLPWV NLANLANLKI KLAKFNEMGI ITPEEIEKLI TEKTKLISIS
     GINNTLGTIN DLESIGKIAK KYNICLFVDA AQMAPHIKID VKKIGCDFLV FSGHKMLAPT
     GIGILYISNN MAEKLHSSKL GGNTVEEIFI ENEKIKFKAS DSPNKFESGT PNIAGIIGLE
     EAIKYIDNIS MDFILEHDKQ LIEYGVKKLQ ELDEVEFILN TNLKRNSIIS FTVKNIHSHD
     IETYLDTMGI ATRAGRTCSY VAFFPENLNK DHLLRISFYF YNTQEEIDNF ILGLKKVIKE
     LS