ID   CSD_UREPA               Reviewed;         402 AA.
AC   Q9PQ36;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=Probable cysteine desulfurase;
DE            EC=2.8.1.7;
GN   Name=csd; OrderedLocusNames=UU454;
OS   Ureaplasma parvum serovar 3 (strain ATCC 700970).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX   NCBI_TaxID=273119;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700970;
RX   PubMed=11048724; DOI=10.1038/35037619;
RA   Glass J.I., Lefkowitz E.J., Glass J.S., Heiner C.R., Chen E.Y.,
RA   Cassell G.H.;
RT   "The complete sequence of the mucosal pathogen Ureaplasma urealyticum.";
RL   Nature 407:757-762(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; AF222894; AAF30866.1; -; Genomic_DNA.
DR   RefSeq; WP_006689089.1; NC_002162.1.
DR   AlphaFoldDB; Q9PQ36; -.
DR   SMR; Q9PQ36; -.
DR   STRING; 273119.UU454; -.
DR   REBASE; 203824; M.Bli1441DndAP.
DR   EnsemblBacteria; AAF30866; AAF30866; UU454.
DR   GeneID; 29672596; -.
DR   KEGG; uur:UU454; -.
DR   eggNOG; COG0520; Bacteria.
DR   HOGENOM; CLU_003433_2_5_14; -.
DR   OMA; HKLCGPT; -.
DR   Proteomes; UP000000423; 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; 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.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..402
FT                   /note="Probable cysteine desulfurase"
FT                   /id="PRO_0000150321"
FT   MOD_RES         218
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   402 AA;  45636 MW;  5B251163C2CB5A23 CRC64;
     MNDYKQFFPW FKNNKDVIYL DSSATSLKPQ VVIDAIVDYY TKYSTNPHNT DSNFTFHTHE
     IMNETRANVA KFINANFDEI IFTSGATESL NLIANGLRPH LKKGDEIILT YIEHASNLLP
     WYKLRDDLGV KIIFANQKNQ FPQLSDFLKV ISPKTKVVSF ASGGNLIGNV LDENLIIKNI
     KKIKPDVLVC VDATQSIQHR MFDVKKCKSD FMVFSAHKLL GPTGIGVAYI KNDLIKKMQP
     LKYGGGMNFS IDLNSYQLYD NYMKFEGGTP HVAGFYGFNA ALKFLMDIGY NKIHEHELKI
     TKYARDQLAL IPEIKTYVQD ATSSTITFSY NGVFCQDFAN YLGSKNIIVR SGLSCAKIIN
     NVIQTECAIR ASFYIYNDFN DVDRLIKAIK EYQKGDELNG IL