ID ISCS_RICCN Reviewed; 410 AA. AC Q92HP1; DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 27-MAR-2024, entry version 122. 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}; Synonyms=spl1; GN OrderedLocusNames=RC0731; OS Rickettsia conorii (strain ATCC VR-613 / Malish 7). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group. OX NCBI_TaxID=272944; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC VR-613 / Malish 7; RX PubMed=11557893; DOI=10.1126/science.1061471; RA Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V., RA Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.; RT "Mechanisms of evolution in Rickettsia conorii and R. prowazekii."; RL Science 293:2093-2098(2001). 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}. 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; AE006914; AAL03268.1; -; Genomic_DNA. DR PIR; B97791; B97791. DR RefSeq; WP_010977349.1; NC_003103.1. DR AlphaFoldDB; Q92HP1; -. DR SMR; Q92HP1; -. DR GeneID; 928569; -. DR KEGG; rco:RC0730; -. DR HOGENOM; CLU_003433_0_2_5; -. DR UniPathway; UPA00266; -. DR Proteomes; UP000000816; Chromosome. 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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1. DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1. DR 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 NCBIfam; TIGR02006; IscS; 1. DR PANTHER; PTHR11601:SF34; CYSTEINE DESULFURASE, MITOCHONDRIAL; 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. PE 3: Inferred from homology; KW 2Fe-2S; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Pyridoxal phosphate; KW Transferase. FT CHAIN 1..410 FT /note="Cysteine desulfurase IscS" FT /id="PRO_0000150275" FT ACT_SITE 334 FT /note="Cysteine persulfide intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00331" FT BINDING 80..81 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00331" FT BINDING 160 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00331" FT BINDING 188 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00331" FT BINDING 208..210 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00331" FT BINDING 248 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00331" FT BINDING 334 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 211 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00331" SQ SEQUENCE 410 AA; 45475 MW; 930AB52556C2F9BE CRC64; MNPQLNNLTL PIYMDYQATT PIDPRVMEAM LPYFTTKFGN PHSRSHSFGW EAENAVEEAR SMVAKLIGAD TKEIIFTSGA TESNNLAIKG IAKFYSNKKN HIITVVSEHK CVLDACRHLE QEGIKITYLP IKPNGIIDLE TLKNAITDQT MLVSVMVVNN EIGVVQPLKE IGKICREKGV FFHSDIAQGF GKIPIDVNAF NIDLASISGH KIYGPKGIGA LYVRKKPRVR VTPLINGGGQ ERGMRSGTLP TPLIVGLGMA AEIAYSEMEK DTKHVNYLFD RFLNNIHKRI SEVYLNGDKN QRYKGNLNLS FAGVEGESMI LAIKDLAVSS GSACTSASLE PSYVLRSMGI GEELAHTAIR FGIGRFTTEQ EVDYAVNLIC SKIDKLRELS PLWEMMQEGI DLKKIKWAVH //