ID   CSD_VIBCH               Reviewed;         404 AA.
AC   Q9KPQ7;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Probable cysteine desulfurase;
DE            EC=2.8.1.7;
GN   Name=csd; OrderedLocusNames=VC_2309;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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; AE003852; AAF95453.1; -; Genomic_DNA.
DR   PIR; F82092; F82092.
DR   RefSeq; NP_231940.1; NC_002505.1.
DR   AlphaFoldDB; Q9KPQ7; -.
DR   SMR; Q9KPQ7; -.
DR   STRING; 243277.VC_2309; -.
DR   DNASU; 2613105; -.
DR   EnsemblBacteria; AAF95453; AAF95453; VC_2309.
DR   KEGG; vch:VC_2309; -.
DR   PATRIC; fig|243277.26.peg.2201; -.
DR   eggNOG; COG0520; Bacteria.
DR   HOGENOM; CLU_003433_2_5_6; -.
DR   OMA; PVCLRYG; -.
DR   BioCyc; VCHO:VC2309-MON; -.
DR   Proteomes; UP000000584; Chromosome 1.
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   GO; GO:0016226; P:iron-sulfur cluster assembly; 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; IPR022471; Cys_desulphurase_CdsA.
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   TIGRFAMs; TIGR03392; FeS_syn_CsdA; 1.
DR   TIGRFAMs; TIGR01979; sufS; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..404
FT                   /note="Probable cysteine desulfurase"
FT                   /id="PRO_0000150322"
FT   ACT_SITE        363
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         226
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   404 AA;  43438 MW;  2F7A1FF473369D06 CRC64;
     MMLNLDAIRA QFPALQQIVN GNPLVYLDSA ATTQKPQCVI DAISHYYSQH NANVHRGSHS
     LTAQATSQFE GAREQVAQFI GAPSSKNIIW TRGATEALNL IAQSYARSTL QAGDEILVSE
     TEHHANIVPW QMVAEQTGAK VVKIPMTTTG EFGLAAFRQL LSPRCKIVAL AHITNVTGTR
     QPIEAVIQAA HQQGAIVVID GAQGIVHETV DVRALDADFY VFSGHKLYAP AGIGVLYGKT
     ALLEAMPPWH GGGKMVEKVS FDGTTFTGLP GKFEAGTPNV AGAIALATAI DWYQSLDRAA
     VEAHLHQLQQ QAYQAISQID DIRVLGYQPN ASVLSLVMDG VHHQDLATLL DQQGIAVRAG
     HHCAHPLMDA FGVKGTVRIS FGVYNSAEEV ERLIAAIHKA VDLL