ID   ISCS_ECOLI              Reviewed;         404 AA.
AC   P0A6B7; P39171; P76581; P76992; Q8XA86;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   20-JAN-2009, entry version 42.
DE   RecName: Full=Cysteine desulfurase;
DE            EC=2.8.1.7;
DE   AltName: Full=ThiI transpersulfidase;
DE   AltName: Full=NifS protein homolog;
GN   Name=iscS; Synonyms=yfhO, yzzO; OrderedLocusNames=b2530, JW2514;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   MEDLINE=97349980; PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA   Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K.,
RA   Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N.,
RA   Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H.,
RA   Oshima T., Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S.,
RA   Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C.,
RA   Yamagata S., Horiuchi T.;
RT   "Construction of a contiguous 874-kb sequence of the Escherichia coli-
RT   K12 genome corresponding to 50.0-68.8 min on the linkage map and
RT   analysis of its sequence features.";
RL   DNA Res. 4:91-113(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1474(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   PROTEIN SEQUENCE OF 1-38; 43-66; 117-127; 212-219; 241-257; 319-339
RP   AND 382-391, AND CHARACTERIZATION.
RX   MEDLINE=96279148; PubMed=8663056;
RA   Flint D.H.;
RT   "Escherichia coli contains a protein that is homologous in function
RT   and N-terminal sequence to the protein encoded by the nifS gene of
RT   Azotobacter vinelandii and that can participate in the synthesis of
RT   the Fe-S cluster of dihydroxy-acid dehydratase.";
RL   J. Biol. Chem. 271:16068-16074(1996).
RN   [5]
RP   PROTEIN SEQUENCE OF 1-16, AND CHARACTERIZATION.
RC   STRAIN=K12;
RX   MEDLINE=20068850; PubMed=10600118; DOI=10.1021/bi991119r;
RA   Kambampati R., Lauhon C.T.;
RT   "IscS is a sulfurtransferase for the in vitro biosynthesis of 4-
RT   thiouridine in Escherichia coli tRNA.";
RL   Biochemistry 38:16561-16568(1999).
RN   [6]
RP   PROTEIN SEQUENCE OF 1-12.
RC   STRAIN=K12 / EMG2;
RX   MEDLINE=97443975; PubMed=9298646; DOI=10.1002/elps.1150180807;
RA   Link A.J., Robison K., Church G.M.;
RT   "Comparing the predicted and observed properties of proteins encoded
RT   in the genome of Escherichia coli K-12.";
RL   Electrophoresis 18:1259-1313(1997).
RN   [7]
RP   PROTEIN SEQUENCE OF 1-9, AND MUTAGENESIS OF CYS-328.
RC   STRAIN=K12;
RX   MEDLINE=20206733; PubMed=10739946;
RA   Mihara H., Kurihara T., Yoshimura T., Esaki N.;
RT   "Kinetic and mutational studies of three NifS homologs from
RT   Escherichia coli: mechanistic difference between L-cysteine
RT   desulfurase and L-selenocysteine lyase reactions.";
RL   J. Biochem. 127:559-567(2000).
RN   [8]
RP   CHARACTERIZATION.
RC   STRAIN=C41(DE3);
RX   MEDLINE=20013001; PubMed=10544286;
RA   Takahashi Y., Nakamura M.;
RT   "Functional assignment of the ORF2-iscS-iscU-iscA-hscB-hscA-fdx-ORF3
RT   gene cluster involved in the assembly of Fe-S clusters in Escherichia
RT   coli.";
RL   J. Biochem. 126:917-926(1999).
RN   [9]
RP   CHARACTERIZATION.
RC   STRAIN=ATCC 33694 / HB101;
RX   MEDLINE=20245547; PubMed=10781558;
RX   DOI=10.1128/JB.182.10.2879-2885.2000;
RA   Kiyasu T., Asakura A., Nagahashi Y., Hoshino T.;
RT   "Contribution of cysteine desulfurase (NifS protein) to the biotin
RT   synthase reaction of Escherichia coli.";
RL   J. Bacteriol. 182:2879-2885(2000).
RN   [10]
RP   CHARACTERIZATION.
RC   STRAIN=K12 / MC1061 / ATCC 53338 / DSM 7140;
RX   MEDLINE=20347927; PubMed=10781607; DOI=10.1074/jbc.M002680200;
RA   Lauhon C.T., Kambampati R.;
RT   "The iscS gene in Escherichia coli is required for the biosynthesis of
RT   4-thiouridine, thiamin, and NAD.";
RL   J. Biol. Chem. 275:20096-20103(2000).
RN   [11]
RP   FUNCTION.
RC   STRAIN=MBO8;
RX   MEDLINE=20379012; PubMed=10829016; DOI=10.1074/jbc.M000926200;
RA   Lacourciere G.M., Mihara H., Kurihara T., Esaki N., Stadtman T.C.;
RT   "Escherichia coli NifS-like proteins provide selenium in the pathway
RT   for the biosynthesis of selenophosphate.";
RL   J. Biol. Chem. 275:23769-23773(2000).
RN   [12]
RP   CHARACTERIZATION.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   MEDLINE=20381327; PubMed=10908675; DOI=10.1073/pnas.160261497;
RA   Schwartz C.J., Djaman O., Imlay J.A., Kiley P.J.;
RT   "The cysteine desulfurase, IscS, has a major role in in vivo Fe-S
RT   cluster formation in Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:9009-9014(2000).
RN   [13]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=16387657; DOI=10.1016/j.molcel.2005.11.001;
RA   Ikeuchi Y., Shigi N., Kato J., Nishimura A., Suzuki T.;
RT   "Mechanistic insights into sulfur relay by multiple sulfur mediators
RT   involved in thiouridine biosynthesis at tRNA wobble positions.";
RL   Mol. Cell 21:97-108(2006).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), PYRIDOXAL PHOSPHATE AT LYS-206,
RP   SUBUNIT, AND ACTIVE SITE CYS-328.
RX   MEDLINE=22745176; PubMed=12860127; DOI=10.1016/S0022-2836(03)00690-9;
RA   Cupp-Vickery J.R., Urbina H., Vickery L.E.;
RT   "Crystal structure of IscS, a cysteine desulfurase from Escherichia
RT   coli.";
RL   J. Mol. Biol. 330:1049-1059(2003).
CC   -!- FUNCTION: Catalyzes the removal of elemental sulfur and selenium
CC       atoms from cysteine and selenocysteine to produce alanine.
CC       Functions as a sulfur delivery protein for NAD, biotin and Fe-S
CC       cluster synthesis. Transfers sulfur on 'Cys-456' of thiI in a
CC       transpersulfidation reaction. Transfers sulfur on 'Cys-19' of tusA
CC       in a transpersulfidation reaction. Functions also as a selenium
CC       delivery protein in the pathway for the biosynthesis of
CC       selenophosphate.
CC   -!- CATALYTIC ACTIVITY: L-cysteine + [enzyme]-cysteine = L-alanine +
CC       [enzyme]-S-sulfanylcysteine.
CC   -!- COFACTOR: Pyridoxal phosphate.
CC   -!- SUBUNIT: Homodimer. The homodimer interacts with tusA.
CC   -!- INTERACTION:
CC       P0ACD4:nifU; NbExp=3; IntAct=EBI-550055, EBI-561646;
CC       P0A7E3:pyrE; NbExp=1; IntAct=EBI-550055, EBI-1133376;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. NifS/iscS subfamily.
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DR   EMBL; U00096; AAT48142.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA16424.1; -; Genomic_DNA.
DR   RefSeq; AP_003116.1; -.
DR   RefSeq; YP_026169.1; -.
DR   PDB; 1P3W; X-ray; 2.10 A; A/B=1-404.
DR   PDBsum; 1P3W; -.
DR   DIP; DIP:29109N; -.
DR   IntAct; P0A6B7; 43.
DR   GeneID; 947004; -.
DR   GenomeReviews; AP009048_GR; JW2514.
DR   GenomeReviews; U00096_GR; b2530.
DR   KEGG; ecj:JW2514; -.
DR   KEGG; eco:b2530; -.
DR   EchoBASE; EB2542; -.
DR   EcoGene; EG12677; iscS.
DR   HOGENOM; P0A6B7; -.
DR   BioCyc; EcoCyc:G7325-MON; -.
DR   BioCyc; MetaCyc:G7325-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0031071; F:cysteine desulfurase activity; IEA:HAMAP.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006534; P:cysteine metabolic process; IEA:InterPro.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR   HAMAP; MF_00331; -; 1.
DR   InterPro; IPR000192; Aminotrans_V/Cys_dSase.
DR   InterPro; IPR010240; Cys_deSase.
DR   InterPro; IPR016454; Cysteine_dSase_NifS.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   Gene3D; G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF005572; NifS; 1.
DR   TIGRFAMs; TIGR02006; IscS; 1.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
KW   Pyridoxal phosphate; Transferase; tRNA processing.
FT   CHAIN         1    404       Cysteine desulfurase.
FT                                /FTId=PRO_0000150264.
FT   ACT_SITE    328    328       Cysteine persulfide intermediate.
FT   BINDING     206    206       Pyridoxal phosphate (covalent).
FT   MUTAGEN     328    328       C->A: Loss of cysteine desulfurization.
FT   CONFLICT     31     31       G -> D (in Ref. 4; AA sequence).
FT   CONFLICT     34     34       G -> F (in Ref. 4; AA sequence).
FT   CONFLICT     37     38       AS -> NA (in Ref. 4; AA sequence).
FT   CONFLICT    118    118       G -> L (in Ref. 4; AA sequence).
FT   CONFLICT    126    126       P -> M (in Ref. 4; AA sequence).
FT   CONFLICT    320    320       L -> I (in Ref. 4; AA sequence).
FT   CONFLICT    326    327       SA -> YL (in Ref. 4; AA sequence).
FT   CONFLICT    339    339       L -> V (in Ref. 4; AA sequence).
FT   STRAND        4      6
FT   TURN          9     11
FT   HELIX        17     24
FT   TURN         25     27
FT   HELIX        42     62
FT   HELIX        66     68
FT   STRAND       69     74
FT   HELIX        75     90
FT   HELIX        91     93
FT   STRAND       96    100
FT   HELIX       105    116
FT   STRAND      120    124
FT   HELIX       134    140
FT   STRAND      145    149
FT   TURN        155    157
FT   HELIX       163    172
FT   STRAND      176    180
FT   TURN        182    184
FT   TURN        192    194
FT   STRAND      198    204
FT   TURN        205    208
FT   STRAND      214    218
FT   TURN        220    223
FT   TURN        235    239
FT   HELIX       246    279
FT   TURN        280    283
FT   STRAND      287    289
FT   TURN        293    295
FT   STRAND      300    305
FT   HELIX       310    316
FT   TURN        317    319
FT   HELIX       337    342
FT   HELIX       346    350
FT   STRAND      352    356
FT   HELIX       363    382
FT   HELIX       385    390
SQ   SEQUENCE   404 AA;  45090 MW;  1E4F2E6F9CD266B0 CRC64;
     MKLPIYLDYS ATTPVDPRVA EKMMQFMTMD GTFGNPASRS HRFGWQAEEA VDIARNQIAD
     LVGADPREIV FTSGATESDN LAIKGAANFY QKKGKHIITS KTEHKAVLDT CRQLEREGFE
     VTYLAPQRNG IIDLKELEAA MRDDTILVSI MHVNNEIGVV QDIAAIGEMC RARGIIYHVD
     ATQSVGKLPI DLSQLKVDLM SFSGHKIYGP KGIGALYVRR KPRVRIEAQM HGGGHERGMR
     SGTLPVHQIV GMGEAYRIAK EEMATEMERL RGLRNRLWNG IKDIEEVYLN GDLEHGAPNI
     LNVSFNYVEG ESLIMALKDL AVSSGSACTS ASLEPSYVLR ALGLNDELAH SSIRFSLGRF
     TTEEEIDYTI ELVRKSIGRL RDLSPLWEMY KQGVDLNSIE WAHH
//