(data stored in SCRATCH9089 zone)

SWISSPROT: ISCS_PASMU

ID   ISCS_PASMU              Reviewed;         404 AA.
AC   P57803;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 1.
DT   11-DEC-2019, entry version 123.
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=PM0318;
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: 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}.
DR   EMBL; AE004439; AAK02402.1; -; Genomic_DNA.
DR   RefSeq; WP_010906586.1; NC_002663.1.
DR   SMR; P57803; -.
DR   PRIDE; P57803; -.
DR   EnsemblBacteria; AAK02402; AAK02402; PM0318.
DR   KEGG; pmu:PM0318; -.
DR   PATRIC; fig|272843.6.peg.331; -.
DR   eggNOG; ENOG4105C3J; Bacteria.
DR   eggNOG; COG1104; LUCA.
DR   HOGENOM; HOG000017510; -.
DR   KO; K04487; -.
DR   OMA; EPIQSGG; -.
DR   BioCyc; PMUL272843:G1FZ8-336-MONOMER; -.
DR   UniPathway; UPA00266; -.
DR   Proteomes; UP000000809; 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; 3.40.640.10; -; 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; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
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;
DR   PRODOM; P57803.
DR   SWISS-2DPAGE; P57803.
KW   2Fe-2S; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Pyridoxal phosphate;
KW   Reference proteome; Transferase.
FT   CHAIN           1..404
FT                   /note="Cysteine desulfurase IscS"
FT                   /id="PRO_0000150273"
FT   REGION          75..76
FT                   /note="Pyridoxal phosphate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00331"
FT   REGION          203..205
FT                   /note="Pyridoxal phosphate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00331"
FT   ACT_SITE        328
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00331"
FT   METAL           328
FT                   /note="Iron-sulfur (2Fe-2S); via persulfide group; shared
FT                   with IscU"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00331"
FT   BINDING         155
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00331"
FT   BINDING         183
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00331"
FT   BINDING         243
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00331"
FT   MOD_RES         206
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00331"
SQ   SEQUENCE   404 AA;  45169 MW;  665BBE307DBC2C76 CRC64;
     MKLPIYLDYA ATCPVDERVA KKMMEYLTVE GNFGNPASRS HKFGWQAEEA VDVARNYIAD
     LIGADSREIV FTSGATESDN LAIKGAAHFY QSKGKHIITC KTEHKAVLDT CRQLEREGFE
     VTYLNPKSDG LIDLEELKNA MRDDTILVSI MHVNNEIGVI QDIAAIGELC RARKILFHVD
     ATQSVGKLPI NLAELKVDLM SMSSHKLYGP KGIGALYVSR KPRVRLEAII HGGGHERGMR
     SGTLPVHQIV GMGEAYRICK EEMASEMPRL KALRDRLYNG LKDIEETYVN GSMEHRLDSN
     LNISFNYVEG ESLMMALRDI AVSSGSACTS ASLEPSYVLR ALGLNDELAH SSIRFTLGRY
     TTEEEIDYTI ELVKNAVAKL RELSPLWDMF KEGIDLNTIE WTHH
//

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