ID   CSD_PASMU               Reviewed;         421 AA.
AC   P57989;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 1.
DT   25-MAY-2022, entry version 114.
DE   RecName: Full=Probable cysteine desulfurase;
DE            EC=2.8.1.7;
GN   Name=csd; OrderedLocusNames=PM0882;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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; AE004439; AAK02966.1; -; Genomic_DNA.
DR   AlphaFoldDB; P57989; -.
DR   SMR; P57989; -.
DR   STRING; 747.DR93_1723; -.
DR   EnsemblBacteria; AAK02966; AAK02966; PM0882.
DR   KEGG; pmu:PM0882; -.
DR   HOGENOM; CLU_003433_2_3_6; -.
DR   OMA; PVCLRYG; -.
DR   Proteomes; UP000000809; 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; 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.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..421
FT                   /note="Probable cysteine desulfurase"
FT                   /id="PRO_0000150306"
FT   MOD_RES         242
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   421 AA;  46490 MW;  8A5E8CA7BC7CC7D5 CRC64;
     MDYGKTLTQS LLSNGADKRE NKMAFNPSVF KQHFPYLQQA DAVVYLDSAA TALKPQVLTD
     ATIAFYQSAG SVHRSQYDEK QTALFEQARE NVKNFIGAES EETIIWTSGT THAINCVARG
     LSHQLHPKAE IIISEADHHA NFVTWSEIAR QYGATLHILP INEQWLIEEQ DLIAVLNTNT
     VLVALNMVSN VTGTEQPVAN LIKLIRQHSH ALVLVDAAQA ISHLPIDLQR LDADFIAFSA
     HKLYGPNGLG VLSGKRHALE QLHPLLYGGK MVERVSAQHI RFAELPYRLE AGTPNIAGVI
     GFNAVLEWLS QWDLTAAEQH AIALAEQCKM RLKNYPHCQL FLSPQPSSIV CFVFNGIATS
     DIATLLAEQN IALRAGEHCA QPYLARLGQH STLRLSFAPY NQQADVDAFF SALDNALALL
     D