ID   ISCS_DECAR              Reviewed;         405 AA.
AC   Q47EN5;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Cysteine desulfurase IscS {ECO:0000255|HAMAP-Rule:MF_00331};
DE            EC=2.8.1.7 {ECO:0000255|HAMAP-Rule:MF_00331};
GN   Name=iscS {ECO:0000255|HAMAP-Rule:MF_00331}; OrderedLocusNames=Daro_1950;
OS   Dechloromonas aromatica (strain RCB).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Azonexaceae;
OC   Dechloromonas.
OX   NCBI_TaxID=159087;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCB;
RX   PubMed=19650930; DOI=10.1186/1471-2164-10-351;
RA   Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G.,
RA   Lapidus A.;
RT   "Metabolic analysis of the soil microbe Dechloromonas aromatica str. RCB:
RT   indications of a surprisingly complex life-style and cryptic anaerobic
RT   pathways for aromatic degradation.";
RL   BMC Genomics 10:351-351(2009).
CC   -!- FUNCTION: Master enzyme that delivers sulfur to a number of partners
CC       involved in Fe-S cluster assembly, tRNA modification or cofactor
CC       biosynthesis. Catalyzes the removal of elemental sulfur atoms from
CC       cysteine to produce alanine. Functions as a sulfur delivery protein for
CC       Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as
CC       well as other S acceptor proteins. {ECO:0000255|HAMAP-Rule:MF_00331}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00331};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00331};
CC   -!- PATHWAY: Cofactor biosynthesis; iron-sulfur cluster biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00331}.
CC   -!- SUBUNIT: Homodimer. Forms a heterotetramer with IscU, interacts with
CC       other sulfur acceptors. {ECO:0000255|HAMAP-Rule:MF_00331}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00331}.
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. NifS/IscS subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_00331}.
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DR   EMBL; CP000089; AAZ46696.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q47EN5; -.
DR   SMR; Q47EN5; -.
DR   STRING; 159087.Daro_1950; -.
DR   EnsemblBacteria; AAZ46696; AAZ46696; Daro_1950.
DR   KEGG; dar:Daro_1950; -.
DR   eggNOG; COG1104; Bacteria.
DR   HOGENOM; CLU_003433_0_2_4; -.
DR   OMA; KGLYWAR; -.
DR   UniPathway; UPA00266; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0044571; P:[2Fe-2S] cluster assembly; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_00331; Cys_desulf_IscS; 1.
DR   InterPro; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR   InterPro; IPR010240; Cys_deSase_IscS.
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   PANTHER; PTHR11601:SF34; PTHR11601:SF34; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF005572; NifS; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR02006; IscS; 1.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE   3: Inferred from homology;
KW   2Fe-2S; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Pyridoxal phosphate;
KW   Transferase.
FT   CHAIN           1..405
FT                   /note="Cysteine desulfurase IscS"
FT                   /id="PRO_1000133114"
FT   ACT_SITE        329
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00331"
FT   BINDING         156
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00331"
FT   BINDING         329
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_note="ligand shared with IscU"
FT                   /note="via persulfide group"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00331"
FT   MOD_RES         207
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00331"
SQ   SEQUENCE   405 AA;  44781 MW;  DA32A703094FF956 CRC64;
     MTMKLPIYLD YSATTPVDPR VAEKMIPYLC EHFGNPASRS HSFGWVADAA VEEAREQVAA
     LVNADPKEIV WTSGATESNN LAIKGAANFY ASTKGKHIIT VKTEHKAILD TVREMERQGF
     EATYLDVKED GLLDLEVFKA AIRPDTVLAS VMFVNNEVGV IQPIAELGEI CREKGIIFHV
     DAAQATGKVD IDLSKLKVDL MSFCAHKTYG PKGIGALYVR RKPRIRLEAQ MHGGGHERGF
     RSGTLPTHQI VGMGECFRLA KEEMAEENKR VGALRDKLLK GLQDIEATFV NGDLTQRVAH
     NLNISFAYVE GESMIMAIKD LAVSSGSACT SASLEPSYVL RALGRDDELA HSSIRFSIGR
     FTTEEEIDYA IKLLHQKVGK LRELSPLWEM YKDGIDLSTV QWAAH