ID   CSD_PSEPK               Reviewed;         401 AA.
AC   Q9Z408;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Probable cysteine desulfurase;
DE            EC=2.8.1.7;
GN   Name=csdA; OrderedLocusNames=PP_1529;
OS   Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS   / KT2440).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=160488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Nashimoto H.;
RL   Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX   PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA   Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA   Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA   Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA   Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA   Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA   Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA   Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA   Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT   "Complete genome sequence and comparative analysis of the metabolically
RT   versatile Pseudomonas putida KT2440.";
RL   Environ. Microbiol. 4:799-808(2002).
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; AB024602; BAA75914.1; -; Genomic_DNA.
DR   EMBL; AE015451; AAN67150.1; -; Genomic_DNA.
DR   RefSeq; NP_743686.1; NC_002947.4.
DR   RefSeq; WP_010952615.1; NC_002947.4.
DR   AlphaFoldDB; Q9Z408; -.
DR   SMR; Q9Z408; -.
DR   STRING; 160488.PP_1529; -.
DR   EnsemblBacteria; AAN67150; AAN67150; PP_1529.
DR   KEGG; ppu:PP_1529; -.
DR   PATRIC; fig|160488.4.peg.1618; -.
DR   eggNOG; COG0520; Bacteria.
DR   HOGENOM; CLU_003433_2_5_6; -.
DR   OMA; PVCLRYG; -.
DR   PhylomeDB; Q9Z408; -.
DR   BioCyc; PPUT160488:G1G01-1620-MON; -.
DR   Proteomes; UP000000556; 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; IPR020578; Aminotrans_V_PyrdxlP_BS.
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   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..401
FT                   /note="Probable cysteine desulfurase"
FT                   /id="PRO_0000150308"
FT   MOD_RES         223
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   401 AA;  43287 MW;  17C1CF71A109406E CRC64;
     MFQPSPWRAD FPAIAALQRQ HQTYLDSAAT TQKPQALLDA LSHYYGHGAA NVHRAQHLPG
     ALATQAFETS RDKVAAWLNA ADSRQIVFTH GATSALNLLA YGLEHRLEAG DEIAISALEH
     HANLLPWQQL AHRRNLHLVV LPLDAHGRID QDQALQLIGP RTRVLAISQL SNVLGTWQPL
     PALLAHARAQ GALTVVDGAQ GVVHGRQDMQ QLGCDFYVFS SHKLYGPDGV GVLYGRAQAL
     ELLRHWQFGG EMVQLAEYHS ASFRPAPLGF EAGTPPIAGV IGLGATLDYL ASLDAHAVAA
     HEASLHQHLL RGLGDREGVR VLGAPQTALA SFVIEGVHNA DIAHLLTEQG IAVRAGHHCA
     MPLLKGLGLE GAIRVSLGLY NDSDDVQRFF DALDQGLELL R