ID   CSD_MYCPN               Reviewed;         408 AA.
AC   P75298;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, 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=MPN_487; ORFNames=MP355;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS   pneumoniae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U00089; AAB96003.1; -; Genomic_DNA.
DR   PIR; S73681; S73681.
DR   RefSeq; NP_110175.1; NC_000912.1.
DR   RefSeq; WP_010874843.1; NC_000912.1.
DR   AlphaFoldDB; P75298; -.
DR   SMR; P75298; -.
DR   IntAct; P75298; 2.
DR   STRING; 272634.MPN_487; -.
DR   EnsemblBacteria; AAB96003; AAB96003; MPN_487.
DR   KEGG; mpn:MPN_487; -.
DR   PATRIC; fig|272634.6.peg.526; -.
DR   HOGENOM; CLU_003433_2_5_14; -.
DR   OMA; PVCLRYG; -.
DR   BioCyc; MPNE272634:G1GJ3-795-MON; -.
DR   Proteomes; UP000000808; Chromosome.
DR   GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC.
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; 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..408
FT                   /note="Probable cysteine desulfurase"
FT                   /id="PRO_0000150300"
FT   MOD_RES         225
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   408 AA;  46483 MW;  0D0AF371A2AFE26F CRC64;
     MTKTKFNPYQ FRKQFKWFKN NPQWVNFDNA ATSIALDTVS QACKEYYELF SVNPHNKTPD
     LNNQIIAIIA ETRQLVADWF NVTALEIIFT SSATESINLF AHGLKPWIKP GDEIVLKGDE
     HSANVLPWVA LAKQTKARLV WVEKQANQSL EDTFKSLINP KTKVVAITAT SNLFGNSIDF
     AQIADYLKQV NPKAFVAVDA VQTVQHKQID IAKTQIDFLA FSTHKFYGPT GLGVAYIKKS
     LQPQLQPLKL GGDIFTQIDP DNTIHFKSTP LKFEAGTPNI MAIYALNKLL RFFKQKFNFA
     QMMAYGHQLK QQAYELLNSN PQIVLANHDQ DVPIFSFKHR QLATIDLATF LNINKIMVRQ
     GSICVGRYRN KDYFVRVSLM HYNTVKELQY LAKLLATDTK TIIKNVIK