ID   A7TUX7_STRLI            Unreviewed;       397 AA.
AC   A7TUX7;
DT   02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   02-OCT-2007, sequence version 1.
DT   02-SEP-2026, entry version 86.
DE   RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE            EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN   Name=dndA {ECO:0000313|EMBL:ABP49156.1};
GN   ORFNames=SLG80 {ECO:0000313|EMBL:ABP49156.1};
OS   Streptomyces lividans.
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1916 {ECO:0000313|EMBL:ABP49156.1};
RN   [1] {ECO:0000313|EMBL:ABP49156.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=66 {ECO:0000313|EMBL:ABP49156.1};
RX   PubMed=16102010; DOI=10.1111/j.1365-2958.2005.04764.x;
RA   Zhou X., He X., Liang J., Li A., Xu T., Kieser T., Helmann J.D., Deng Z.;
RT   "A novel DNA modification by sulphur.";
RL   Mol. Microbiol. 57:1428-1438(2005).
RN   [2] {ECO:0000313|EMBL:ABP49156.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=66 {ECO:0000313|EMBL:ABP49156.1};
RX   PubMed=17640271; DOI=10.1111/j.1365-2958.2007.05846.x;
RA   He X., Ou H.Y., Yu Q., Zhou X., Wu J., Liang J., Zhang W., Rajakumar K.,
RA   Deng Z.;
RT   "Analysis of a genomic island housing genes for DNA S-modification system
RT   in Streptomyces lividans 66 and its counterparts in other distantly related
RT   bacteria.";
RL   Mol. Microbiol. 65:1034-1048(2007).
RN   [3] {ECO:0007829|PDB:3VAX}
RP   X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 19-397 IN COMPLEX WITH PYRIDOXAL
RP   5'-PHOSPHATE.
RX   PubMed=22570733; DOI=10.1371/journal.pone.0036635;
RA   Chen F., Zhang Z., Lin K., Qian T., Zhang Y., You D., He X., Wang Z.,
RA   Liang J., Deng Z., Wu G.;
RT   "Crystal structure of the cysteine desulfurase DndA from Streptomyces
RT   lividans which is involved in DNA phosphorothioation.";
RL   PLoS ONE 7:e36635-e36635(2012).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU004504};
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. NifS/IscS subfamily.
CC       {ECO:0000256|ARBA:ARBA00006490}.
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; EF210454; ABP49156.1; -; Genomic_DNA.
DR   PDB; 3VAX; X-ray; 2.40 A; A/B=19-397.
DR   AlphaFoldDB; A7TUX7; -.
DR   SMR; A7TUX7; -.
DR   REBASE; 186945; M.Sli66DndAP.
DR   BRENDA; 2.8.1.7; 6052.
DR   EvolutionaryTrace; A7TUX7; -.
DR   GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC.
DR   Gene3D; 1.10.260.50; -; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR   InterPro; IPR017644; Cysteine_desulfurase_DndA.
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   NCBIfam; TIGR03235; DNA_S_dndA; 1.
DR   PANTHER; PTHR11601:SF34; CYSTEINE DESULFURASE; 1.
DR   PANTHER; PTHR11601; CYSTEINE DESULFURYLASE FAMILY MEMBER; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF005572; NifS; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
DR   PDBsum; 3VAX; -.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:3VAX}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          19..373
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
FT   BINDING         86
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0007829|PDB:3VAX"
FT   BINDING         87
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0007829|PDB:3VAX"
FT   BINDING         116
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0007829|PDB:3VAX"
FT   BINDING         214
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0007829|PDB:3VAX"
FT   BINDING         216
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0007829|PDB:3VAX"
FT   BINDING         217
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0007829|PDB:3VAX"
SQ   SEQUENCE   397 AA;  42821 MW;  6021329924BCCBE2 CRC64;
     MTYGTCRLTL KGGLGSMVTY LDAAATTRVD QRVADIVLHW MTAEFGNAGS RHEYGIRAKR
     GVERAREYLA STVSAEPDEL IFTSGATESN NIALLGLAPY GERTGRRHII TSAIEHKAVL
     EPLEHLAGRG FEVDFLTPGP SGRISVEGVM ERLRPDTLLV SLMHVNNETG VIQPVAELAQ
     QLRATPTYLH VDAAQGYGKV PGDLTTPIDM ISISGHKIGA PKGVGALVTR RREEMDDERV
     PLEPIMFGGG QERKLRPGTL PVPLIMGLAE AAKIFEAEHA QWQVAAQDLR SRLLAGLAST
     SFQVNGDQDH VVPHILNLSF EDVDAEAFLV TLKDLVAVAT GSACTSASFT PSHVLRAMGL
     PEEAASKSLR FSWTPGQATD LDVEELARGV AKLKPSY
//